131:
1494:
165:
148:
1923:
1899:
2059:
2076:
1526:
2216:(CAN) systems in order to allow for dynamic breakage and reformation of crosslinks. By incorporating disulfide functional groups as crosslinks between polymer chains, materials can be produced which are stable at room temperature while also allowing for reversible crosslink dissociation upon application of elevated temperature. The mechanism behind this reaction can be attributed to the cleavage of disulfide linkages (RS−SR) into
3540:
1661:
2196:
physical properties of the resulting rubber- namely, a greater degree of crosslinking corresponds to a stronger and more rigid material. The current conventional methods of rubber manufacturing are typically irreversible, as the unregulated reaction mechanisms can result in complex networks of sulfide linkages; as such, rubber is considered to be a
1452:) does not change the number of disulfide bonds within a protein, merely their location (i.e., which cysteines are bonded). Disulfide reshuffling is generally much faster than oxidation/reduction reactions, which change the number of disulfide bonds within a protein. The oxidation and reduction of protein disulfide bonds
1307:(TCEP) is useful, beside being odorless compared to β-ME and DTT, because it is selective, working at both alkaline and acidic conditions (unlike DTT), is more hydrophilic and more resistant to oxidation in air. Furthermore, it is often not needed to remove TCEP before modification of protein thiols.
2241:
materials, as said materials consist of polymer chains which are not bonded to each other at the molecular level; as a result, they can be melted down and reformed (as the addition of thermal energy allows the chains to untangle, move past each other, and adopt new configurations), but this comes at
1830:
production and gene expression according to light intensity. Additionally, It has been reported that disulfides plays a significant role on redox state regulation of Two-component systems (TCSs), which could be found in certain bacteria including photogenic strain. A unique intramolecular cysteine
2254:
resistance, and the like (as the bonding between chains provides resistance to deformation at the macroscopic level), but due to the permanence of said crosslinks, these materials cannot be reprocessed akin to thermoplastics. However, due to the dynamic nature of the crosslinks in disulfide CANs,
1640:
is a grouping of all disulfide species with the same number of disulfide bonds, and is usually denoted as the 1S ensemble, the 2S ensemble, etc. for disulfide species having one, two, etc. disulfide bonds. Thus, the (26–84) disulfide species belongs to the 1S ensemble, whereas the (26–84, 58–110)
2224:
characteristics for the bulk material. However, since the bond dissociation energy of the disulfide bond is still fairly high, it is typically necessary to augment the bond with adjacent chemistry that can stabilize the unpaired electron of the intermediate state. As such, studies usually employ
2916:
Tiwari, Nitija; López-Redondo, Marisa; Miguel-Romero, Laura; Kulhankova, Katarina; Cahill, Michael P.; Tran, Phuong M.; Kinney, Kyle J.; Kilgore, Samuel H.; Al-Tameemi, Hassan; Herfst, Christine A.; Tuffs, Stephen W.; Kirby, John R.; Boyd, Jeffery M.; McCormick, John K.; Salgado-Pabón, Wilmara;
2195:
of the material. Although the exact mechanism underlying the vulcanization process is not entirely understood (as multiple reaction pathways are present but the predominant one is unknown), it has been extensively shown that the extent to which the process is allowed to proceed determines the
1418:
Thiol–disulfide exchange showing the linear intermediate in which the charge is shared among the three sulfur atoms. The thiolate group (shown in red) attacks a sulfur atom (shown in blue) of the disulfide bond, displacing the other sulfur atom (shown in green) and forming a new disulfide
1768:
There are notable exceptions to this rule. For example, many nuclear and cytosolic proteins can become disulfide-crosslinked during necrotic cell death. Similarly, a number of cytosolic proteins which have cysteine residues in proximity to each other that function as oxidation sensors or
1468:
between the protein and the reagent. This mixed disulfide bond when attacked by another thiolate from the reagent, leaves the cysteine oxidized. In effect, the disulfide bond is transferred from the protein to the reagent in two steps, both thiol–disulfide exchange reactions.
738:
is treated with an alkyl dihalide. In the converse reaction, carbanionic reagents react with elemental sulfur to afford mixtures of the thioether, disulfide, and higher polysulfides. These reactions are often unselective but can be optimized for specific applications.
1628:, a disulfide bond stabilizes secondary structure in its vicinity. For example, researchers have identified several pairs of peptides that are unstructured in isolation, but adopt stable secondary and tertiary structure upon formation of a disulfide bond between them.
2255:
they can be designed to exhibit the best attributes of both of the aforementioned material types. Studies have shown that disulfide CANs can be reprocessed multiple times with negligible degradation in performance while also exhibiting creep resistance,
1560:
the "Cys26–Cys84 disulfide bond", or the "26–84 disulfide bond", or most simply as "C26–C84" where the disulfide bond is understood and does not need to be mentioned. The prototype of a protein disulfide bond is the two-amino-acid peptide
2229:
disulfides or disulfidediamine (RNS−SNR) functional groups to encourage the dynamic dissociation of the S−S bond; these chemistries can result in the bond dissociation energy being reduced to half (or even less) of its prior magnitude.
843:
1411:. The original disulfide bond is broken, and its other sulfur atom is released as a new thiolate, carrying away the negative charge. Meanwhile, a new disulfide bond forms between the attacking thiolate and the original sulfur atom.
1810:, for example, the enzymatic reduction of disulfide bonds has been linked to the control of numerous metabolic pathways as well as gene expression. The reductive signaling activity has been shown, thus far, to be carried by the
1301:
1484:
arrangement (i.e., next to each other), which allows it to form an internal disulfide bond, or disulfide bonds with other proteins. As such, it can be used as a repository of reduced or oxidized disulfide bond moieties.
1652:. In proteins with more than two cysteines, non-native disulfide species may be formed, which are almost always misfolded. As the number of cysteines increases, the number of nonnative species increases factorially.
1856:
have similar keratins and are extremely resistant to protein digestive enzymes. The stiffness of hair and feather is determined by the disulfide content. Manipulating disulfide bonds in hair is the basis for the
718:
1835:
is a good example of disulfides in regulatory proteins, which the redox state of SrrB molecule is controlled by cysteine disulfide bonds, leading to the modification of SrrA activity including gene regulation.
1852:, which have a high disulfide content, from the amino acid cysteine. The robustness conferred in part by disulfide linkages is illustrated by the recovery of virtually intact hair from ancient Egyptian tombs.
988:
1865:. The high disulfide content of feathers dictates the high sulfur content of bird eggs. The high sulfur content of hair and feathers contributes to the disagreeable odor that results when they are burned.
1779:
also produces cytosolic proteins and peptides that have many disulfide bonds; although the reason for this is unknown presumably they have protective effects against intracellular proteolysis machinery.
583:
350:
2191:
results in crosslinking groups which consist of disulfide (and polysulfide) bonds; in analogy to the role of disulfides in proteins, the S−S linkages in rubber strongly affect the stability and
1108:
1360:
1068:
1876:
is a condition where cystine precipitates as a solid in various organs. This accumulation interferes with bodily function and can be fatal. This disorder can be resolved by treatment with
1415:
438:
1636:
is a particular pairing of cysteines in a disulfide-bonded protein and is usually depicted by listing the disulfide bonds in parentheses, e.g., the "(26–84, 58–110) disulfide species". A
2446:"Copper(II)-Mediated Hydrogen Sulfide and Thiol Oxidation to Disulfides and Organic Polysulfanes and Their Reductive Cleavage in Wine: Mechanistic Elucidation and Potential Applications"
2865:
Samson, Andre L.; Knaupp, Anja S.; Sashindranath, Maithili; Borg, Rachael J.; Au, Amanda E.-L.; Cops, Elisa J.; Saunders, Helen M.; Cody, Stephen H.; McLean, Catriona A. (2012-10-25).
1880:. Cysteamine acts to solubilize the cystine by (1) forming the mixed disulfide cysteine-cysteamine, which is more soluble and exportable, and (2) reducing cystine to cysteine.
1645:
is much faster than the formation of new disulfide bonds or their reduction; hence, the disulfide species within an ensemble equilibrate more quickly than between ensembles.
3126:"Reprocessable covalent adaptable networks with excellent elevated-temperature creep resistance: facilitation by dynamic, dissociative bis(hindered amino) disulfide bonds"
1127:
2094:
are orthogonally isomeric with disulfides, having the second sulfur branching from the first and not partaking in a continuous chain, i.e. >S=S rather than −S−S−.
1510:
and play an important role in the folding and stability of some proteins, usually proteins secreted to the extracellular medium. Since most cellular compartments are
2822:
1648:
The native form of a protein is usually a single disulfide species, although some proteins may cycle between a few disulfide states as part of their function, e.g.,
3366:
Futami, J.; Tada, H.; Seno, M.; Ishikami, S.; Yamada, H. (2000). "Stabilization of human RNAse 1 by introduction of a disulfide bond between residues 4 and 118".
2785:
Ruoppolo, M.; Vinci, F.; Klink, T. A.; Raines, R. T.; Marino, G. (2000). "Contribution of individual disulfide bonds to the oxidative folding of ribonuclease A".
5760:
723:
Such reactions are mediated by enzymes in some cases and in other cases are under equilibrium control, especially in the presence of a catalytic amount of base.
1818:
to catalytically reduce disulfides in regulated proteins in a light dependent manner. In this way chloroplasts adjust the activity of key processes such as the
2603:
Nikolai S. Zefirov, Nikolai V. Zyk, Elena K. Beloglazkina, Andrei G. Kutateladze (1993). "Thiosulfonates: Synthesis, Reactions and
Practical Applications".
235:. Unsymmetrical disulfide are less common in organic chemistry, but many disulfides in nature are unsymmetrical. Illustrative of a symmetric disulfide is
5166:
5822:
5119:
1641:
species belongs to the 2S ensemble. The single species with no disulfide bonds is usually denoted as R for "fully reduced". Under typical conditions,
1444:. The rearrangement of disulfide bonds within a protein generally occurs via intra-protein thiol–disulfide exchange reactions; a thiolate group of a
389:
of disulfides is usually not practical, the equilibrium constant for the reaction provides a measure of the standard redox potential for disulfides:
3337:
Wu, J.; Watson, J. T. (1998). "Optimization of the cleavage reaction for cyanylated cysteinyl proteins for efficient and simplified mass mapping".
2630:
5238:
2923:
2820:
Ladenstein, R.; Ren, B. (2008). "Reconsideration of an early dogma, saying "there is no evidence for disulfide bonds in proteins from archaea"".
2867:"Nucleocytoplasmic coagulation: an injury-induced aggregation event that disulfide crosslinks proteins and facilitates their removal by plasmin"
5587:
3395:
Wittenberg, G.; Danon, A. (2008). "Disulfide bond formation in chloroplasts: Formation of disulfide bonds in signaling chloroplast proteins".
5577:
3308:
Thannhauser, T. W.; Konishi, Y.; Scheraga, H. A. (1984). "Sensitive quantitative analysis of disulfide bonds in polypeptides and proteins".
1556:, cannot form disulfide bonds. A disulfide bond is typically denoted by hyphenating the abbreviations for cysteine, e.g., when referring to
2237:
to polymeric materials while still exhibiting physical properties similar to that of thermosets. Typically, recyclability is restricted to
4160:
1965:, or S−S. In disulfide, sulfur exists in the reduced state with oxidation number −1. Its electron configuration then resembles that of a
2978:
Besouw, Martine; Masereeuw, Rosalinde; Van Den Heuvel, Lambert; Levtchenko, Elena (2013). "Cysteamine: An Old Drug with new
Potential".
2490:
M. E. Alonso; H. Aragona (1978). "Sulfide
Synthesis in Preparation of Unsymmetrical Dialkyl Disulfides: Sec-butyl Isopropyl Disulfide".
2162:
is described with the structural formula i.e. S=C=S. This molecule is not a disulfide in the sense that it lacks a S-S bond. Similarly,
1073:
1317:
1020:
1806:
As disulfide bonds can be reversibly reduced and re-oxidized, the redox state of these bonds has evolved into a signaling element. In
5079:
1765:). Thus disulfide bonds are mostly found in secretory proteins, lysosomal proteins, and the exoplasmic domains of membrane proteins.
1761:. This is due to the more oxidizing environment of the aforementioned compartments and more reducing environment of the cytosol (see
5955:
757:
5112:
5084:
614:
477:
600:
in the presence of base is commonly employed to oxidize thiols to disulfides. Several metals, such as copper(II) and iron(III)
2242:
the expense of their physical robustness. Meanwhile, conventional thermosets contain permanent crosslinks which bolster their
2367:
1773:
catalysts; when the reductive potential of the cell fails, they oxidize and trigger cellular response mechanisms. The virus
1586:
It holds two portions of the protein together, biasing the protein towards the folded topology. That is, the disulfide bond
883:
747:
Many specialized methods have been developed for forming unsymmetrical disulfides. Reagents that deliver the equivalent of "
3572:
1601:
of the folded protein, i.e., local hydrophobic residues may condense around the disulfide bond and onto each other through
285:
3068:
3178:
Zheng, Jie; Png, Zhuang Mao; Ng, Shi Hoe; Tham, Guo Xiong; Ye, Enyi; Goh, Shermin S.; Loh, Xian Jun; Li, Zibiao (2021).
5105:
215:
Two kinds of disulfides are recognized, symmetric and unsymmetric. Symmetrical disulfides are compounds of the formula
2706:
2661:
2342:
1754:
1811:
1476:
oxidation and reduction of protein disulfide bonds by thiol–disulfide exchange is facilitated by a protein called
395:
4153:
2109:
bonds. Intermediate compounds of these also exist, for example thioperoxides (also known as oxasulfides) such as
1456:
also generally occurs via thiol–disulfide exchange reactions. Typically, the thiolate of a redox reagent such as
1427:(typically, below 8) where the protonated thiol form is favored relative to the deprotonated thiolate form. (The
5097:
2919:"The SrrAB two-component system regulates Staphylococcus aureus pathogenicity through redox sensitive cysteines"
2602:
5132:
3416:
Kadokura, Hiroshi; Katzen, Federico; Beckwith, Jon (2003). "Protein
Disulfide Bond Formation in Prokaryotes".
2516:
Hervé This. Can a cooked egg white be uncooked? The
Chemical Intelligencer (Springer Verlag), 1996 (14), 51.
4983:
2732:"Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of
371:
approaching 90°. When the angle approaches 0° or 180°, then the disulfide is a significantly better oxidant.
1448:
residue attacks one of the protein's own disulfide bonds. This process of disulfide rearrangement (known as
5782:
1440:
Thiol–disulfide exchange is the principal reaction by which disulfide bonds are formed and rearranged in a
5945:
3544:
3130:
3024:
1750:
444:
382:. When the two R groups are not identical, the compound is said to be an asymmetric or mixed disulfide.
5965:
5950:
4556:
4146:
2213:
1480:. This small protein, essential in all known organisms, contains two cysteine amino acid residues in a
3019:
5233:
5128:
3125:
4593:
3565:
2279:
2209:
1642:
1423:
Thiolates, not thiols, attack disulfide bonds. Hence, thiol–disulfide exchange is inhibited at low
605:
248:
1569:
amino acids joined by a disulfide bond. The structure of a disulfide bond can be described by its
1013:. Hydride agents are typical reagents, and a common laboratory demonstration "uncooks" eggs with
263:
bonds, the disulfide bond is often the "weak link" in many molecules. Furthermore, reflecting the
87:, the anion appears in a few rare minerals, but the functional group has tremendous importance in
5876:
5066:
3490:"The human protein disulphide isomerase family: substrate interactions and functional properties"
3041:
1602:
2648:. Advances in Enzymology and Related Areas of Molecular Biology. Vol. 63. pp. 69–172.
2154:
Disulfide is also used to refer to compounds that contain two sulfide (S) centers. The compound
4966:
1862:
1827:
1620:
the effective local concentration of water molecules. Since water molecules attack amide-amide
3064:"Making the Best of Polymers with Sulfur–Nitrogen Bonds: From Sources to Innovative Materials"
5675:
5073:
4961:
3879:
3748:
3429:
2690:
2624:
2243:
2221:
2220:(2 RS•) which can subsequently reassociate into new bonds, resulting in reprocessability and
2197:
2110:
5151:
5042:
4487:
2932:
2685:
Gilbert, H. F. (1995). "Thiol/disulfide exchange equilibria and disulfide bond stability".
2307:
2163:
1511:
1507:
259:
3379:
1704:
as a reversible switch that turns a protein on or off when bacterial cells are exposed to
130:
8:
4348:
3740:
3712:
3661:
3558:
2417:
2251:
2019:
1928:
1861:
in hairstyling. Reagents that affect the making and breaking of S−S bonds are key, e.g.,
1819:
1625:
1481:
84:
2936:
2311:
1674:
Please expand the section to include this information. Further details may exist on the
1672:
about intermolecular disulfide bonds of the protein-protein and protein-thiol varieties.
471:) groups, especially in biological contexts. The transformation is depicted as follows:
164:
5481:
5331:
3813:
3792:
3678:
3608:
3514:
3489:
3471:
3446:
3203:
3147:
3095:
2955:
2918:
2847:
2762:
2731:
2394:
2005:
1519:
1014:
735:
379:
375:
209:
170:
3037:
219:. Most disulfides encountered in organo sulfur chemistry are symmetrical disulfides.
5435:
5321:
5280:
5032:
5002:
4760:
4382:
3895:
3652:
3550:
3519:
3476:
3433:
3383:
3354:
3325:
3321:
3296:
3292:
3267:
3242:
3238:
3207:
3151:
3099:
3087:
2995:
2960:
2898:
2890:
2839:
2802:
2767:
2712:
2702:
2698:
2667:
2657:
2644:
Gilbert, H. F. (1990). "Molecular and
Cellular Aspects of Thiol–Disulfide Exchange".
2573:
2550:
2465:
2386:
2338:
2298:
Lee, J. D.; Bryant, M. W. R. (1969). "The
Crystal Structure of Diphenyl Disulphide".
2120:
1709:
1549:
589:
2851:
2445:
1493:
374:
Disulfides where the two R groups are the same are called symmetric, examples being
5738:
5716:
5615:
5534:
5425:
5402:
5326:
5298:
4737:
4231:
4169:
3509:
3501:
3466:
3458:
3425:
3408:
3404:
3375:
3346:
3317:
3288:
3259:
3234:
3193:
3139:
3077:
3033:
2987:
2950:
2940:
2880:
2831:
2794:
2757:
2747:
2694:
2649:
2612:
2582:
2559:
2499:
2457:
2426:
2398:
2376:
2315:
2256:
2155:
1598:
1003:
50:
1296:{\displaystyle {\ce {RS-SR + 2 HOCH2CH2SH <=> HOCH2CH2S-SCH2CH2OH + 2 RSH}}}
5960:
5849:
5549:
5440:
5316:
5275:
5127:
4956:
4715:
4710:
4693:
4676:
4477:
4226:
3225:
Sela, M.; Lifson, S. (1959). "The reformation of disulfide bridges in proteins".
3198:
3184:
3179:
2991:
2885:
2866:
2300:
2260:
1311:
1113:
604:
affect this reaction. Alternatively, disulfide bonds in proteins often formed by
251:
of 60 kcal/mol (251 kJ mol). However, being about 40% weaker than
147:
39:
3263:
1124:. The thiol reagents are used in excess to drive the equilibrium to the right:
95:
residues are an important component of the tertiary and quaternary structure of
5711:
5605:
5582:
5524:
5374:
5356:
5243:
5209:
5027:
5022:
4898:
4893:
4888:
4681:
4648:
4432:
4414:
4404:
2263:
values comparable to those observed in similar conventional thermoset systems.
2188:
1922:
1858:
1675:
1576:
1557:
1461:
1437:
of a typical thiol group is roughly 8.3, but can vary due to its environment.)
1117:
368:
264:
205:
2835:
2687:
Biothiols, Part A: Monothiols and
Dithiols, Protein Thiols, and Thiyl Radicals
2653:
2616:
2563:
2319:
2170:, is not a disulfide in the sense again that its sulfur atoms are not linked.
5939:
5730:
5657:
5633:
5572:
5567:
5519:
5514:
5463:
5420:
5341:
5285:
5189:
5047:
4995:
4926:
4812:
4802:
4797:
4787:
4782:
4732:
4727:
4643:
4638:
4628:
4482:
4437:
4399:
4387:
4358:
4236:
3505:
2894:
2586:
2503:
2461:
2272:
2238:
2217:
2184:
2091:
1815:
1621:
1369:
1365:
601:
593:
386:
356:
2945:
2917:
Marina, Alberto; Schlievert, Patrick M.; Fuentes, Ernesto J. (19 May 2020).
2212:(in comparison to C−C bonds and the like), disulfides have been employed in
2058:
1898:
1582:
The disulfide bond stabilizes the folded form of a protein in several ways:
367:
axis is subject to a low barrier. Disulfides show a distinct preference for
5529:
5346:
5161:
5146:
4978:
4865:
4860:
4837:
4588:
4427:
4353:
4290:
4285:
4263:
4219:
4204:
4194:
3523:
3480:
3437:
3387:
3350:
3246:
3091:
3082:
3063:
2999:
2964:
2902:
2871:
2843:
2806:
2771:
2752:
2571:
Douglass, Irwin B.; Norton, Richard V. (1960). "Methanesulfinyl
Chloride".
2469:
2430:
2390:
2132:
2102:
1969:
atom. It thus tends to form a covalent bond with another S center to form
1807:
1591:
1414:
742:
272:
88:
3462:
3358:
3329:
3300:
2915:
2716:
2671:
2525:
5651:
5610:
5539:
5504:
5499:
5458:
5430:
5397:
5379:
5351:
5204:
5194:
5184:
5156:
5037:
4990:
4951:
4832:
4720:
4705:
4700:
4688:
4253:
4248:
4214:
4209:
4199:
4177:
3767:
3271:
2226:
1762:
1749:
cells, in general, stable disulfide bonds are formed in the lumen of the
1649:
1477:
1457:
857:
731:
276:
153:
588:
A variety of oxidants participate in this reaction including oxygen and
447:(pH = 7). By comparison, the standard reduction potential for
5891:
5797:
5774:
5770:
5726:
5690:
5667:
5450:
5254:
5220:
5176:
4946:
4937:
4817:
4772:
4668:
4633:
4623:
4563:
4499:
4422:
4370:
3775:
3143:
2977:
2106:
2075:
1877:
1873:
1733:
at low concentrations if not for the protective action of the SS-bond.
1553:
998:
The most important aspect of disulfide bonds is their scission, as the
861:
727:
448:
108:
3447:"Oxidative protein folding in eukaryotes: mechanisms and consequences"
2798:
5920:
5833:
5643:
5562:
5509:
5473:
5412:
5389:
5336:
5267:
5199:
4913:
4827:
4792:
4765:
4608:
4583:
4392:
2529:
2247:
2234:
2114:
1791:
1784:
1746:
1705:
460:
27:
20:
4138:
3180:"Vitrimers: Current research trends and their emerging applications"
2415:
Witt, D. (2008). "Recent developments in disulfide bond formation".
2233:
In practical terms, disulfide-containing CANs can be used to impart
5908:
5904:
5900:
5837:
5810:
5752:
5703:
5699:
5597:
5544:
5366:
5308:
5290:
4921:
4875:
4842:
4538:
4444:
4318:
4273:
4258:
3759:
3704:
3279:
Thornton, J. M. (1981). "Disulphide bridges in globular proteins".
2381:
2362:
2192:
2113:, have the formula ROSR (equivalently RSOR). These are isomeric to
2098:
1990:
1966:
1775:
1730:
1713:
1701:
1566:
1545:
1533:
1525:
1445:
253:
92:
2117:
in a similar manner to the above; i.e. >S=O rather than −S−O−.
1002:
bond is usually the weakest bond in a molecule. Many specialized
5868:
5860:
5841:
5814:
5625:
4883:
4807:
4658:
4653:
4618:
4603:
4598:
4568:
4551:
4375:
4302:
4268:
3853:
3783:
1853:
1849:
1758:
1734:
1562:
1529:
1515:
1441:
236:
136:
96:
5899:
2730:
Hatahet, F.; Nguyen, V. D.; Salo, K. E.; Ruddock, L. W. (2010).
1981:
group, similar to elemental chlorine existing as the diatomic Cl
1831:
disulfide bonds in the ATP-binding domain of SrrAB TCs found in
1660:
5912:
5864:
5806:
5748:
5491:
5263:
4971:
4903:
4747:
4456:
4449:
4343:
4324:
4313:
4297:
4243:
3539:
2041:
1986:
1904:
1823:
1795:
1719:
1401:
1010:
597:
1497:
Schematic of disulfide bonds crosslinking regions of a protein
838:{\displaystyle {\ce {RSH + R'SNR''_2 -> RS-SR' + HNR''_2}}}
5557:
5228:
4852:
4822:
4755:
4613:
4578:
4573:
4546:
4494:
4461:
4365:
4189:
2864:
2646:
Advances in Enzymology and Related Areas of Molecular Biology
1950:
1788:
1770:
1541:
1393:
1017:. Alkali metals effect the same reaction more aggressively:
464:
77:
65:
2363:"Formation and transfer of disulphide bonds in living cells"
1536:
linked by a disulfide bond (shown here in its neutral form).
4280:
2131:, are disulfides but they behave distinctly because of the
2097:
Disulfide bonds are analogous but more common than related
2033:
1845:
1616:
the effective local concentration of protein residues, and
1579:
between the C−S−S−C atoms, which is usually close to ±90°.
1404:
1304:
713:{\displaystyle {\ce {RS-SR + R'SH <=> R'S-SR + RSH}}}
578:{\displaystyle {\ce {2 RSH <=> RS-SR + 2 H+ + 2 e-}}}
3307:
3258:. Methods in Enzymology. Vol. 47. pp. 129–132.
1726:
1428:
1338:
1276:
1263:
1242:
1229:
1173:
1160:
1070:
followed by protonation of the resulting metal thiolate:
976:
963:
918:
905:
830:
790:
416:
5850:
4-(p-hydroxybenzylidene)-5-imidazolinone (HBI) formation
2784:
2729:
743:
Synthesis of unsymmetrical disulfides (heterodisulfides)
271:
bond is susceptible to scission by polar reagents, both
1737:
typically have fewer disulfides than higher organisms.
1424:
983:{\displaystyle {\ce {Na + NaSR' -> RSSR' + Na2SO3}}}
91:. Disulfide bridges formed between thiol groups in two
3580:
3415:
3365:
2489:
1700:
Disulfide bonds play an important protective role for
1200:
665:
510:
3123:
1914:, "fool's gold". Color code: yellow = S, violet = Fe
1320:
1310:
In Zincke cleavage, halogens oxidize disulfides to a
1130:
1076:
1023:
886:
760:
751:" react with thiols to give asymmetrical disulfides:
617:
480:
398:
345:{\displaystyle {\ce {RS-SR + Nu- -> RS-Nu + RS-}}}
288:
16:
Functional group with the chemical structure R−S−S−R′
3254:
Stark, G. R.; Stern, K.; Atala, A.; Yoo, J. (1977).
1801:
1364:
More unusually, oxidation of disulfides gives first
877:
are also used to generate unsymmetrical disulfides:
1814:, channeling electrons from the light reactions of
1783:Disulfide bonds are also formed within and between
1540:Disulfide bonds in proteins are formed between the
1103:{\displaystyle {\ce {NaSR + HCl -> HSR + NaCl}}}
208:approaching 90°. The S-S bond length is 2.03 Å in
5823:p-Hydroxybenzylidene-imidazolinone (HBI) formation
3253:
1514:, in general, disulfide bonds are unstable in the
1464:attacks the disulfide bond on a protein forming a
1355:{\displaystyle {\ce {ArSSAr + Cl2 -> 2 ArSCl}}}
1354:
1295:
1102:
1063:{\displaystyle {\ce {RS-SR + 2 Na -> 2 NaSR,}}}
1062:
982:
837:
712:
577:
432:
344:
1208:
1207:
1190:
1189:
673:
672:
655:
654:
518:
517:
500:
499:
5937:
3124:Bin Rusayyis, Mohammed; Torkelson, John (2021).
1518:, with some exceptions as noted below, unless a
734:gives disulfides. "Thiokol" polymers arise when
3487:
3394:
2924:Proceedings of the National Academy of Sciences
2146:, are called trisulfides, or trisulfide bonds.
247:The disulfide bonds are strong, with a typical
3177:
3020:"Vulcanization and crosslinking in elastomers"
2570:
2203:
5113:
4154:
3566:
2819:
2138:Compounds with three sulfur atoms, such as CH
1597:The disulfide bond may form the nucleus of a
1121:
1009:A variety of reductants reduce disulfides to
433:{\displaystyle {\ce {RSSR + H2 -> 2 RSH}}}
5783:Tryptophan tryptophylquinone (TTQ) formation
2629:: CS1 maint: multiple names: authors list (
2360:
592:. Such reactions are thought to proceed via
459:Disulfide bonds are usually formed from the
443:This value is about −250 mV versus the
3061:
3017:
1387:
5120:
5106:
4161:
4147:
3573:
3559:
3488:Ellgaard, Lars; Ruddock, Lloyd W. (2005).
3444:
3224:
2450:Journal of Agricultural and Food Chemistry
1695:
1552:. The other sulfur-containing amino acid,
1112:In biochemistry labwork, thiols such as β-
1006:have been developed to cleave the bond.
359:in length, about 0.5 Å longer than a
3513:
3470:
3197:
3081:
2954:
2944:
2884:
2761:
2751:
2380:
2335:An Introduction to Organosulfur Chemistry
2297:
1501:
1347:
1288:
1149:
1052:
1042:
563:
546:
485:
425:
3430:10.1146/annurev.biochem.72.121801.161459
3336:
3278:
2778:
2543:
2519:
2443:
2356:
2354:
1524:
1492:
1488:
1413:
212:, similar to that in elemental sulfur.
5877:Methylidene-imidazolone (MIO) formation
3062:Mutlu, Hatice; Theato, Patrick (2020).
2723:
2684:
2643:
2332:
2178:
1883:
1839:
1608:Related to 1 and 2, the disulfide bond
1183:
648:
493:
5938:
3621:
3256:Cleavage at cysteine after cyanylation
2596:
2410:
2408:
2368:Nature Reviews Molecular Cell Biology
1753:(rough endoplasmic reticulum) and the
1725:) in particular could severely damage
355:The disulfide bond is about 2.05
5761:Lysine tyrosylquinone (LTQ) formation
5101:
4168:
4142:
4029:
3554:
3380:10.1093/oxfordjournals.jbchem.a022747
3173:
3171:
3169:
3167:
3165:
3163:
3161:
3119:
3117:
3115:
3113:
3111:
3109:
3057:
3055:
3053:
3051:
3013:
3011:
3009:
2361:Sevier, C. S.; Kaiser, C. A. (2002).
2351:
115:
2414:
2048:
1654:
1506:Disulfide bonds can be formed under
5234:Glycosyl phosphatidylinositol (GPI)
3445:Tu, B. P.; Weissman, J. S. (2004).
3069:Macromolecular Rapid Communications
2405:
2337:. Chichester: John Wiley and Sons.
2016:), the simplest inorganic disulfide
1989:may also behave similarly, e.g. in
1612:two segments of the protein chain,
13:
3217:
3158:
3106:
3048:
3006:
2444:Kreitman, Gal Y. (March 5, 2017).
1120:(DTT) serve as reductants through
596:intermediates. In the laboratory,
14:
5977:
5545:Oxidative deamination to aldehyde
3532:
1802:Disulfides in regulatory proteins
1755:mitochondrial intermembrane space
123:A selection of organic disulfides
68:. The linkage is also called an
3538:
3018:Akiba, M.; Hashim, A.S. (1997).
2693:. Vol. 251. pp. 8–28.
2074:
2057:
1921:
1897:
1740:
1659:
163:
146:
129:
5956:Post-translational modification
5133:posttranslational modifications
2971:
2909:
2858:
2813:
2678:
2637:
2173:
1590:of the protein by lowering its
1392:In thiol–disulfide exchange, a
231:) are compounds of the formula
3409:10.1016/j.plantsci.2008.05.011
2548:-Nitrophenylsulfur Chloride".
2534:
2510:
2483:
2437:
2326:
2291:
1942:, a common industrial chemical
1844:Over 90% of the dry weight of
1588:destabilizes the unfolded form
1379:RS(=O)SR + → RS(=O)
1341:
1210:
1185:
1087:
1046:
939:
924:
892:
794:
675:
650:
520:
495:
419:
314:
139:, crosslinker in many proteins
1:
3418:Annual Review of Biochemistry
3227:Biochimica et Biophysica Acta
3038:10.1016/S0079-6700(96)00015-9
2285:
2208:Due to their relatively weak
1868:
1812:ferredoxin-thioredoxin system
1305:tris(2-carboxyethyl)phosphine
242:
76:and usually derived from two
42:) is a compound containing a
3322:10.1016/0003-2697(84)90786-3
3293:10.1016/0022-2836(81)90515-5
3281:Journal of Molecular Biology
3239:10.1016/0006-3002(59)90188-X
3199:10.1016/j.mattod.2021.07.003
2992:10.1016/j.drudis.2013.02.003
2886:10.1016/j.celrep.2012.08.026
2699:10.1016/0076-6879(95)51107-5
2149:
1376:RSSR + → RS(=O)SR
993:
454:
199:
192:, a common organic disulfide
7:
5352:Topaquinone (TPQ) formation
3451:The Journal of Cell Biology
3264:10.1016/j.ymeth.2008.09.005
3025:Progress in Polymer Science
2266:
2204:Covalent adaptable networks
1565:, which is composed of two
1548:residues by the process of
445:standard hydrogen electrode
10:
5982:
4031:
2544:Hubacher, Max H. (1935). "
2526:TCEP technical information
2214:covalent adaptable network
1848:comprises proteins called
864:, derivatives of the type
204:Disulfides have a C-S-S-C
18:
5889:
5859:
5832:
5805:
5796:Crosslinks between three
5795:
5769:
5747:
5725:
5698:
5688:
5666:
5642:
5624:
5596:
5490:
5472:
5449:
5411:
5388:
5365:
5307:
5262:
5252:
5219:
5175:
5139:
5129:Protein primary structure
5056:
5015:
4935:
4912:
4874:
4851:
4746:
4667:
4537:
4514:
4470:
4413:
4336:
4311:
4176:
3623:
3601:
2836:10.1007/s00792-007-0076-z
2654:10.1002/9780470123096.ch2
2617:10.1080/01961779308055018
2564:10.15227/orgsyn.015.00452
2320:10.1107/S0567740869005188
1891:A selection of disulfides
363:bond. Rotation about the
5890:Crosslinks between four
3506:10.1038/sj.embor.7400311
2740:Microbial Cell Factories
2587:10.15227/orgsyn.040.0062
2504:10.15227/orgsyn.058.0147
2462:10.1021/acs.jafc.6b05418
2280:organoselenium chemistry
2275: – Functional group
2210:bond dissociation energy
2030:), a distillable liquid.
1603:hydrophobic interactions
1388:Thiol-disulfide exchange
1122:thiol-disulfide exchange
730:of alkali metal di- and
606:thiol-disulfide exchange
267:of divalent sulfur, the
249:bond dissociation energy
221:Unsymmetrical disulfides
19:Not to be confused with
5689:Crosslinks between two
5067:chemical classification
3368:Journal of Biochemistry
3339:Analytical Biochemistry
3310:Analytical Biochemistry
3042:Elsevier Science Direct
2946:10.1073/pnas.1921307117
2333:Cremlyn, R. J. (1996).
1696:In bacteria and archaea
451:is about −430 mV.
5337:Porphyrin ring linkage
3351:10.1006/abio.1998.2596
3083:10.1002/marc.202000181
2753:10.1186/1475-2859-9-67
2431:10.1055/s-2008-1067188
1863:ammonium thioglycolate
1670:is missing information
1537:
1502:Occurrence in proteins
1498:
1420:
1356:
1297:
1104:
1064:
984:
839:
714:
579:
434:
346:
102:Compounds of the form
5398:Succinimide formation
5074:chemical nomenclature
3463:10.1083/jcb.200311055
2691:Methods in Enzymology
2123:, with the formula (R
2111:hydrogen thioperoxide
1833:Staphylococcus aureus
1643:disulfide reshuffling
1528:
1512:reducing environments
1496:
1489:Occurrence in biology
1417:
1357:
1298:
1105:
1065:
985:
840:
715:
580:
435:
347:
5152:Protein biosynthesis
3547:at Wikimedia Commons
2980:Drug Discovery Today
2179:Rubber manufacturing
2164:molybdenum disulfide
1884:Inorganic disulfides
1840:In hair and feathers
1508:oxidising conditions
1466:mixed disulfide bond
1407:in a disulfide bond
1318:
1128:
1074:
1021:
884:
758:
615:
478:
396:
286:
4530:not C, H or O)
2937:2020PNAS..11710989T
2931:(20): 10989–10999.
2793:(39): 12033–12042.
2312:1969AcCrB..25.2094L
2020:Disulfur dichloride
1929:Disulfur dichloride
1820:Calvin–Benson cycle
1626:secondary structure
1532:is composed of two
1450:disulfide shuffling
1340:
1278:
1265:
1244:
1231:
1196:
1175:
1162:
978:
965:
920:
907:
833:
793:
661:
506:
418:
106:are usually called
85:inorganic chemistry
5946:Organic disulfides
5482:Transglutamination
4972:Hypervalent iodine
3144:10.1039/D1PY00187F
2986:(15–16): 785–792.
2121:Thiuram disulfides
2006:Hydrogen disulfide
1638:disulfide ensemble
1538:
1520:sulfhydryl oxidase
1499:
1421:
1352:
1328:
1293:
1266:
1253:
1232:
1219:
1215:
1163:
1150:
1100:
1060:
1015:sodium borohydride
980:
966:
953:
908:
895:
835:
816:
776:
736:sodium polysulfide
710:
680:
575:
525:
430:
406:
380:dimethyl disulfide
376:diphenyl disulfide
342:
210:diphenyl disulfide
171:Diphenyl disulfide
116:Organic disulfides
5966:Functional groups
5951:Protein structure
5933:
5932:
5929:
5928:
5885:
5884:
5791:
5790:
5684:
5683:
5436:Polyglutamylation
5322:Dephosphorylation
5281:Dephosphorylation
5095:
5094:
5033:Sulfenyl chloride
5011:
5010:
4510:
4509:
4329:(only C, H and O)
4170:Functional groups
4136:
4135:
4130:
4129:
3543:Media related to
3138:(18): 2760–2771.
3131:Polymer Chemistry
2799:10.1021/bi001044n
2574:Organic Syntheses
2551:Organic Syntheses
2456:(12): 2564–2571.
2425:(16): 2491–2509.
2306:(10): 2094–2101.
2049:Related compounds
1710:Hydrogen peroxide
1693:
1692:
1634:disulfide species
1550:oxidative folding
1350:
1331:
1324:
1291:
1281:
1269:
1256:
1247:
1235:
1222:
1217:
1178:
1166:
1153:
1142:
1134:
1098:
1092:
1086:
1080:
1055:
1045:
1035:
1027:
1004:organic reactions
969:
956:
945:
934:
923:
911:
898:
890:
819:
808:
799:
779:
771:
764:
708:
702:
694:
687:
682:
643:
636:
629:
621:
590:hydrogen peroxide
567:
550:
539:
531:
527:
488:
428:
409:
402:
334:
327:
319:
307:
300:
292:
5973:
5897:
5896:
5803:
5802:
5739:Sulfilimine bond
5717:ADP-ribosylation
5696:
5695:
5616:ADP-ribosylation
5535:ADP-ribosylation
5426:ADP-ribosylation
5403:ADP-ribosylation
5327:ADP-ribosylation
5299:ADP-ribosylation
5260:
5259:
5253:Single specific
5122:
5115:
5108:
5099:
5098:
5062:
4967:Trifluoromethoxy
4535:
4534:
4531:
4334:
4333:
4330:
4183:
4163:
4156:
4149:
4140:
4139:
3605:
3604:
3596:and polysulfides
3595:
3593:
3592:
3575:
3568:
3561:
3552:
3551:
3542:
3527:
3517:
3484:
3474:
3441:
3412:
3391:
3362:
3333:
3304:
3275:
3250:
3212:
3211:
3201:
3175:
3156:
3155:
3121:
3104:
3103:
3085:
3059:
3046:
3045:
3015:
3004:
3003:
2975:
2969:
2968:
2958:
2948:
2913:
2907:
2906:
2888:
2862:
2856:
2855:
2817:
2811:
2810:
2782:
2776:
2775:
2765:
2755:
2727:
2721:
2720:
2682:
2676:
2675:
2641:
2635:
2634:
2628:
2620:
2600:
2594:
2589:
2566:
2538:
2532:
2523:
2517:
2514:
2508:
2507:
2487:
2481:
2480:
2478:
2476:
2441:
2435:
2434:
2412:
2403:
2402:
2384:
2358:
2349:
2348:
2330:
2324:
2323:
2295:
2257:glass transition
2156:carbon disulfide
2078:
2061:
1980:
1979:
1978:
1964:
1963:
1962:
1941:
1925:
1913:
1901:
1688:
1685:
1679:
1663:
1655:
1599:hydrophobic core
1410:
1399:
1361:
1359:
1358:
1353:
1351:
1348:
1339:
1336:
1329:
1322:
1302:
1300:
1299:
1294:
1292:
1289:
1279:
1277:
1274:
1267:
1264:
1261:
1254:
1252:
1245:
1243:
1240:
1233:
1230:
1227:
1220:
1218:
1216:
1214:
1213:
1206:
1198:
1197:
1195:
1188:
1180:
1176:
1174:
1171:
1164:
1161:
1158:
1151:
1140:
1139:
1132:
1109:
1107:
1106:
1101:
1099:
1096:
1090:
1084:
1078:
1069:
1067:
1066:
1061:
1059:
1053:
1043:
1033:
1032:
1025:
1001:
989:
987:
986:
981:
979:
977:
974:
967:
964:
961:
954:
949:
943:
938:
932:
927:
921:
919:
916:
909:
906:
903:
896:
888:
876:
874:
873:
870:
855:
844:
842:
841:
836:
834:
832:
831:
824:
817:
812:
806:
804:
797:
792:
791:
784:
777:
775:
769:
762:
750:
719:
717:
716:
711:
709:
706:
700:
699:
692:
691:
685:
683:
681:
679:
678:
671:
663:
662:
660:
653:
645:
641:
640:
634:
627:
626:
619:
584:
582:
581:
576:
574:
573:
572:
565:
556:
555:
548:
537:
536:
529:
528:
526:
524:
523:
516:
508:
507:
505:
498:
490:
486:
470:
439:
437:
436:
431:
429:
426:
417:
414:
407:
400:
366:
362:
351:
349:
348:
343:
341:
340:
339:
332:
325:
324:
317:
313:
312:
305:
298:
297:
290:
270:
262:
256:
234:
229:mixed disulfides
225:heterodisulfides
218:
191:
167:
150:
133:
105:
74:disulfide bridge
64:
63:
62:
51:functional group
49:
5981:
5980:
5976:
5975:
5974:
5972:
5971:
5970:
5936:
5935:
5934:
5925:
5881:
5855:
5828:
5787:
5765:
5743:
5721:
5680:
5676:C-mannosylation
5662:
5638:
5620:
5592:
5558:Imine formation
5486:
5468:
5445:
5441:Polyglycylation
5407:
5384:
5361:
5317:Phosphorylation
5303:
5276:Phosphorylation
5248:
5215:
5171:
5135:
5126:
5096:
5091:
5060:
5052:
5007:
4962:Trichloromethyl
4957:Trifluoromethyl
4931:
4908:
4870:
4847:
4742:
4711:Phosphine oxide
4663:
4529:
4527:
4526:
4524:
4522:
4520:
4518:
4516:
4506:
4466:
4409:
4328:
4327:
4322:
4317:
4307:
4181:
4180:
4172:
4167:
4137:
4132:
4131:
3903:
3899:
3887:
3883:
3857:
3821:
3817:
3787:
3779:
3771:
3763:
3752:
3744:
3720:
3716:
3708:
3688:
3682:
3669:
3665:
3656:
3644:
3616:
3612:
3597:
3591:
3588:
3587:
3586:
3584:
3579:
3535:
3530:
3220:
3218:Further reading
3215:
3185:Materials Today
3176:
3159:
3122:
3107:
3076:(13): 2000181.
3060:
3049:
3016:
3007:
2976:
2972:
2914:
2910:
2863:
2859:
2818:
2814:
2783:
2779:
2728:
2724:
2709:
2683:
2679:
2664:
2642:
2638:
2622:
2621:
2601:
2597:
2593:
2539:
2535:
2524:
2520:
2515:
2511:
2488:
2484:
2474:
2472:
2442:
2438:
2413:
2406:
2375:(11): 836–847.
2359:
2352:
2345:
2331:
2327:
2296:
2292:
2288:
2278:Diselenides in
2269:
2261:dynamic modulus
2206:
2181:
2176:
2169:
2161:
2152:
2145:
2141:
2130:
2126:
2089:
2088:
2087:
2086:
2085:
2084:
2079:
2070:
2069:
2068:
2067:
2062:
2051:
2039:
2029:
2025:
2015:
2011:
2000:
1996:
1984:
1977:
1974:
1973:
1972:
1970:
1961:
1958:
1957:
1956:
1954:
1947:
1946:
1945:
1944:
1943:
1940:
1936:
1932:
1926:
1917:
1916:
1915:
1912:
1908:
1902:
1893:
1892:
1886:
1871:
1842:
1804:
1757:but not in the
1743:
1724:
1718:
1698:
1689:
1683:
1680:
1673:
1664:
1575:
1504:
1491:
1435:
1408:
1397:
1390:
1382:
1337:
1332:
1321:
1319:
1316:
1315:
1312:sulfenyl halide
1275:
1270:
1262:
1257:
1248:
1241:
1236:
1228:
1223:
1209:
1202:
1201:
1199:
1191:
1184:
1182:
1181:
1179:
1172:
1167:
1159:
1154:
1135:
1131:
1129:
1126:
1125:
1114:mercaptoethanol
1077:
1075:
1072:
1071:
1028:
1024:
1022:
1019:
1018:
999:
996:
975:
970:
962:
957:
942:
931:
917:
912:
904:
899:
891:
887:
885:
882:
881:
871:
868:
867:
865:
853:
849:
829:
825:
820:
805:
800:
789:
785:
780:
768:
761:
759:
756:
755:
748:
745:
695:
684:
674:
667:
666:
664:
656:
649:
647:
646:
644:
633:
622:
618:
616:
613:
612:
568:
564:
551:
547:
532:
519:
512:
511:
509:
501:
494:
492:
491:
489:
481:
479:
476:
475:
468:
457:
415:
410:
399:
397:
394:
393:
369:dihedral angles
364:
360:
335:
331:
320:
308:
304:
293:
289:
287:
284:
283:
275:and especially
268:
258:
252:
245:
232:
216:
202:
197:
196:
195:
194:
193:
190:
186:
182:
178:
174:
168:
159:
158:
157:
151:
142:
141:
140:
134:
125:
124:
118:
103:
72:or sometimes a
61:
58:
57:
56:
54:
43:
40:British English
24:
17:
12:
11:
5:
5979:
5969:
5968:
5963:
5958:
5953:
5948:
5931:
5930:
5927:
5926:
5924:
5923:
5917:
5915:
5894:
5887:
5886:
5883:
5882:
5880:
5879:
5873:
5871:
5857:
5856:
5854:
5853:
5846:
5844:
5830:
5829:
5827:
5826:
5819:
5817:
5800:
5793:
5792:
5789:
5788:
5786:
5785:
5779:
5777:
5767:
5766:
5764:
5763:
5757:
5755:
5745:
5744:
5742:
5741:
5735:
5733:
5723:
5722:
5720:
5719:
5714:
5712:Disulfide bond
5708:
5706:
5693:
5686:
5685:
5682:
5681:
5679:
5678:
5672:
5670:
5664:
5663:
5661:
5660:
5655:
5648:
5646:
5640:
5639:
5637:
5636:
5630:
5628:
5622:
5621:
5619:
5618:
5613:
5608:
5606:Citrullination
5602:
5600:
5594:
5593:
5591:
5590:
5585:
5583:Propionylation
5580:
5575:
5570:
5565:
5560:
5555:
5553:-glycosylation
5547:
5542:
5537:
5532:
5527:
5525:Ubiquitination
5522:
5517:
5512:
5507:
5502:
5496:
5494:
5488:
5487:
5485:
5484:
5478:
5476:
5470:
5469:
5467:
5466:
5461:
5455:
5453:
5447:
5446:
5444:
5443:
5438:
5433:
5428:
5423:
5417:
5415:
5409:
5408:
5406:
5405:
5400:
5394:
5392:
5386:
5385:
5383:
5382:
5377:
5375:Palmitoylation
5371:
5369:
5363:
5362:
5360:
5359:
5357:Detyrosination
5354:
5349:
5347:Flavin linkage
5344:
5339:
5334:
5329:
5324:
5319:
5313:
5311:
5305:
5304:
5302:
5301:
5296:
5288:
5283:
5278:
5272:
5270:
5257:
5250:
5249:
5247:
5246:
5244:Detyrosination
5241:
5236:
5231:
5225:
5223:
5217:
5216:
5214:
5213:
5210:Myristoylation
5207:
5202:
5197:
5192:
5187:
5181:
5179:
5173:
5172:
5170:
5169:
5167:N–O acyl shift
5164:
5159:
5154:
5149:
5143:
5141:
5137:
5136:
5125:
5124:
5117:
5110:
5102:
5093:
5092:
5090:
5089:
5088:
5087:
5082:
5070:
5063:
5057:
5054:
5053:
5051:
5050:
5048:Sulfinylamines
5045:
5040:
5035:
5030:
5028:Phosphoramides
5025:
5023:Isothiocyanate
5019:
5017:
5013:
5012:
5009:
5008:
5006:
5005:
5000:
4999:
4998:
4988:
4987:
4986:
4976:
4975:
4974:
4969:
4964:
4959:
4954:
4943:
4941:
4933:
4932:
4930:
4929:
4924:
4918:
4916:
4910:
4909:
4907:
4906:
4901:
4899:Selenenic acid
4896:
4894:Seleninic acid
4891:
4889:Selenonic acid
4886:
4880:
4878:
4872:
4871:
4869:
4868:
4863:
4857:
4855:
4849:
4848:
4846:
4845:
4840:
4835:
4830:
4825:
4820:
4815:
4810:
4805:
4800:
4795:
4790:
4785:
4780:
4775:
4770:
4769:
4768:
4758:
4752:
4750:
4744:
4743:
4741:
4740:
4735:
4730:
4725:
4724:
4723:
4713:
4708:
4703:
4698:
4697:
4696:
4686:
4685:
4684:
4682:Phosphodiester
4673:
4671:
4665:
4664:
4662:
4661:
4656:
4651:
4646:
4641:
4636:
4631:
4626:
4621:
4616:
4611:
4606:
4601:
4596:
4591:
4586:
4581:
4576:
4571:
4566:
4561:
4560:
4559:
4554:
4543:
4541:
4532:
4528:(one element,
4512:
4511:
4508:
4507:
4505:
4504:
4503:
4502:
4492:
4491:
4490:
4485:
4474:
4472:
4468:
4467:
4465:
4464:
4459:
4454:
4453:
4452:
4442:
4441:
4440:
4435:
4430:
4419:
4417:
4411:
4410:
4408:
4407:
4405:Methylenedioxy
4402:
4397:
4396:
4395:
4390:
4380:
4379:
4378:
4373:
4363:
4362:
4361:
4351:
4346:
4340:
4338:
4331:
4309:
4308:
4306:
4305:
4300:
4295:
4294:
4293:
4288:
4278:
4277:
4276:
4271:
4266:
4261:
4256:
4251:
4241:
4240:
4239:
4234:
4224:
4223:
4222:
4217:
4212:
4207:
4202:
4197:
4186:
4184:
4182:(only C and H)
4174:
4173:
4166:
4165:
4158:
4151:
4143:
4134:
4133:
4128:
4127:
4124:
4121:
4118:
4115:
4112:
4109:
4106:
4103:
4100:
4097:
4094:
4091:
4088:
4085:
4081:
4080:
4077:
4074:
4071:
4068:
4065:
4062:
4059:
4056:
4053:
4050:
4047:
4044:
4041:
4038:
4034:
4033:
4030:
4027:
4026:
4023:
4020:
4017:
4014:
4011:
4008:
4005:
4002:
3999:
3996:
3993:
3990:
3987:
3984:
3981:
3978:
3975:
3972:
3968:
3967:
3964:
3961:
3958:
3955:
3952:
3949:
3946:
3943:
3940:
3937:
3934:
3931:
3928:
3925:
3922:
3919:
3916:
3913:
3909:
3908:
3905:
3901:
3897:
3893:
3890:
3885:
3881:
3877:
3874:
3871:
3868:
3865:
3862:
3859:
3855:
3851:
3848:
3845:
3842:
3839:
3836:
3834:
3831:
3827:
3826:
3823:
3819:
3815:
3811:
3808:
3805:
3802:
3799:
3796:
3789:
3785:
3781:
3777:
3773:
3769:
3765:
3761:
3757:
3754:
3750:
3746:
3742:
3738:
3735:
3733:
3730:
3726:
3725:
3722:
3718:
3714:
3710:
3706:
3702:
3699:
3696:
3693:
3690:
3684:
3680:
3675:
3674:
3671:
3667:
3663:
3659:
3654:
3650:
3647:
3642:
3638:
3635:
3632:
3628:
3627:
3624:
3622:
3620:
3618:
3614:
3610:
3603:
3602:
3599:
3598:
3589:
3578:
3577:
3570:
3563:
3555:
3549:
3548:
3534:
3533:External links
3531:
3529:
3528:
3485:
3457:(3): 341–346.
3442:
3424:(1): 111–135.
3413:
3403:(4): 459–466.
3392:
3374:(2): 245–250.
3363:
3345:(2): 268–276.
3334:
3316:(1): 181–188.
3305:
3287:(2): 261–287.
3276:
3251:
3233:(2): 471–478.
3221:
3219:
3216:
3214:
3213:
3157:
3105:
3047:
3032:(3): 475–521.
3005:
2970:
2908:
2879:(4): 889–901.
2857:
2812:
2777:
2722:
2707:
2677:
2662:
2636:
2605:Sulfur Reports
2595:
2592:
2591:
2568:
2540:
2533:
2518:
2509:
2482:
2436:
2404:
2382:10.1038/nrm954
2350:
2343:
2325:
2289:
2287:
2284:
2283:
2282:
2276:
2268:
2265:
2218:thiyl radicals
2205:
2202:
2180:
2177:
2175:
2172:
2167:
2159:
2151:
2148:
2143:
2139:
2128:
2124:
2092:Thiosulfoxides
2082:
2080:
2073:
2072:
2071:
2065:
2063:
2056:
2055:
2054:
2053:
2052:
2050:
2047:
2046:
2045:
2037:
2036:disulfide (FeS
2031:
2027:
2023:
2017:
2013:
2009:
1998:
1994:
1982:
1975:
1959:
1949:The disulfide
1938:
1934:
1927:
1920:
1919:
1918:
1910:
1903:
1896:
1895:
1894:
1890:
1889:
1888:
1887:
1885:
1882:
1870:
1867:
1859:permanent wave
1841:
1838:
1803:
1800:
1742:
1739:
1722:
1716:
1697:
1694:
1691:
1690:
1667:
1665:
1658:
1630:
1629:
1622:hydrogen bonds
1606:
1595:
1577:dihedral angle
1573:
1558:ribonuclease A
1503:
1500:
1490:
1487:
1462:dithiothreitol
1433:
1400:displaces one
1389:
1386:
1385:
1384:
1380:
1377:
1370:thiosulfonates
1366:thiosulfinates
1346:
1343:
1335:
1327:
1303:The reductant
1287:
1284:
1273:
1260:
1251:
1239:
1226:
1212:
1205:
1194:
1187:
1170:
1157:
1148:
1145:
1138:
1118:dithiothreitol
1095:
1089:
1083:
1058:
1051:
1048:
1041:
1038:
1031:
995:
992:
991:
990:
973:
960:
952:
948:
941:
937:
930:
926:
915:
902:
894:
851:
846:
845:
828:
823:
815:
811:
803:
796:
788:
783:
774:
767:
744:
741:
721:
720:
705:
698:
690:
677:
670:
659:
652:
639:
632:
625:
586:
585:
571:
562:
559:
554:
545:
542:
535:
522:
515:
504:
497:
484:
456:
453:
441:
440:
424:
421:
413:
405:
353:
352:
338:
330:
323:
316:
311:
303:
296:
265:polarizability
244:
241:
206:dihedral angle
201:
198:
188:
184:
180:
176:
169:
162:
161:
160:
152:
145:
144:
143:
135:
128:
127:
126:
122:
121:
120:
119:
117:
114:
59:
15:
9:
6:
4:
3:
2:
5978:
5967:
5964:
5962:
5959:
5957:
5954:
5952:
5949:
5947:
5944:
5943:
5941:
5922:
5919:
5918:
5916:
5914:
5910:
5906:
5902:
5898:
5895:
5893:
5888:
5878:
5875:
5874:
5872:
5870:
5866:
5862:
5858:
5852:(chromophore)
5851:
5848:
5847:
5845:
5843:
5839:
5835:
5831:
5825:(chromophore)
5824:
5821:
5820:
5818:
5816:
5812:
5808:
5804:
5801:
5799:
5794:
5784:
5781:
5780:
5778:
5776:
5772:
5768:
5762:
5759:
5758:
5756:
5754:
5750:
5746:
5740:
5737:
5736:
5734:
5732:
5731:Hydroxylysine
5728:
5724:
5718:
5715:
5713:
5710:
5709:
5707:
5705:
5701:
5697:
5694:
5692:
5687:
5677:
5674:
5673:
5671:
5669:
5665:
5659:
5658:Adenylylation
5656:
5653:
5650:
5649:
5647:
5645:
5641:
5635:
5634:Hydroxylation
5632:
5631:
5629:
5627:
5623:
5617:
5614:
5612:
5609:
5607:
5604:
5603:
5601:
5599:
5595:
5589:
5586:
5584:
5581:
5579:
5576:
5574:
5573:Succinylation
5571:
5569:
5568:Carbamylation
5566:
5564:
5561:
5559:
5556:
5554:
5552:
5548:
5546:
5543:
5541:
5538:
5536:
5533:
5531:
5528:
5526:
5523:
5521:
5520:Hydroxylation
5518:
5516:
5515:Adenylylation
5513:
5511:
5508:
5506:
5503:
5501:
5498:
5497:
5495:
5493:
5489:
5483:
5480:
5479:
5477:
5475:
5471:
5465:
5464:Glycosylation
5462:
5460:
5457:
5456:
5454:
5452:
5448:
5442:
5439:
5437:
5434:
5432:
5429:
5427:
5424:
5422:
5421:Carboxylation
5419:
5418:
5416:
5414:
5410:
5404:
5401:
5399:
5396:
5395:
5393:
5391:
5387:
5381:
5378:
5376:
5373:
5372:
5370:
5368:
5364:
5358:
5355:
5353:
5350:
5348:
5345:
5343:
5342:Adenylylation
5340:
5338:
5335:
5333:
5330:
5328:
5325:
5323:
5320:
5318:
5315:
5314:
5312:
5310:
5306:
5300:
5297:
5295:
5293:
5289:
5287:
5286:Glycosylation
5284:
5282:
5279:
5277:
5274:
5273:
5271:
5269:
5265:
5261:
5258:
5256:
5251:
5245:
5242:
5240:
5239:O-methylation
5237:
5235:
5232:
5230:
5227:
5226:
5224:
5222:
5218:
5211:
5208:
5206:
5203:
5201:
5198:
5196:
5193:
5191:
5190:Carbamylation
5188:
5186:
5183:
5182:
5180:
5178:
5174:
5168:
5165:
5163:
5160:
5158:
5155:
5153:
5150:
5148:
5145:
5144:
5142:
5138:
5134:
5130:
5123:
5118:
5116:
5111:
5109:
5104:
5103:
5100:
5086:
5083:
5081:
5078:
5077:
5076:
5075:
5071:
5069:
5068:
5064:
5059:
5058:
5055:
5049:
5046:
5044:
5041:
5039:
5036:
5034:
5031:
5029:
5026:
5024:
5021:
5020:
5018:
5014:
5004:
5001:
4997:
4994:
4993:
4992:
4989:
4985:
4982:
4981:
4980:
4977:
4973:
4970:
4968:
4965:
4963:
4960:
4958:
4955:
4953:
4950:
4949:
4948:
4945:
4944:
4942:
4940:
4939:
4934:
4928:
4927:Telluroketone
4925:
4923:
4920:
4919:
4917:
4915:
4911:
4905:
4902:
4900:
4897:
4895:
4892:
4890:
4887:
4885:
4882:
4881:
4879:
4877:
4873:
4867:
4864:
4862:
4859:
4858:
4856:
4854:
4850:
4844:
4841:
4839:
4836:
4834:
4831:
4829:
4826:
4824:
4821:
4819:
4816:
4814:
4813:Sulfonic acid
4811:
4809:
4806:
4804:
4803:Sulfinic acid
4801:
4799:
4798:Thiosulfonate
4796:
4794:
4791:
4789:
4788:Thiosulfinate
4786:
4784:
4783:Sulfenic acid
4781:
4779:
4776:
4774:
4771:
4767:
4764:
4763:
4762:
4759:
4757:
4754:
4753:
4751:
4749:
4745:
4739:
4738:Phosphaallene
4736:
4734:
4733:Phosphaalkyne
4731:
4729:
4728:Phosphaalkene
4726:
4722:
4719:
4718:
4717:
4714:
4712:
4709:
4707:
4704:
4702:
4699:
4695:
4692:
4691:
4690:
4687:
4683:
4680:
4679:
4678:
4675:
4674:
4672:
4670:
4666:
4660:
4657:
4655:
4652:
4650:
4647:
4645:
4642:
4640:
4637:
4635:
4632:
4630:
4627:
4625:
4622:
4620:
4617:
4615:
4612:
4610:
4607:
4605:
4602:
4600:
4597:
4595:
4592:
4590:
4587:
4585:
4582:
4580:
4577:
4575:
4572:
4570:
4567:
4565:
4562:
4558:
4555:
4553:
4550:
4549:
4548:
4545:
4544:
4542:
4540:
4536:
4533:
4513:
4501:
4498:
4497:
4496:
4493:
4489:
4486:
4484:
4481:
4480:
4479:
4476:
4475:
4473:
4469:
4463:
4460:
4458:
4455:
4451:
4448:
4447:
4446:
4443:
4439:
4436:
4434:
4431:
4429:
4426:
4425:
4424:
4421:
4420:
4418:
4416:
4412:
4406:
4403:
4401:
4400:Ethylenedioxy
4398:
4394:
4391:
4389:
4386:
4385:
4384:
4381:
4377:
4374:
4372:
4369:
4368:
4367:
4364:
4360:
4357:
4356:
4355:
4352:
4350:
4347:
4345:
4342:
4341:
4339:
4335:
4332:
4326:
4320:
4315:
4310:
4304:
4301:
4299:
4296:
4292:
4289:
4287:
4284:
4283:
4282:
4279:
4275:
4272:
4270:
4267:
4265:
4262:
4260:
4257:
4255:
4252:
4250:
4247:
4246:
4245:
4242:
4238:
4235:
4233:
4230:
4229:
4228:
4225:
4221:
4218:
4216:
4213:
4211:
4208:
4206:
4203:
4201:
4198:
4196:
4193:
4192:
4191:
4188:
4187:
4185:
4179:
4175:
4171:
4164:
4159:
4157:
4152:
4150:
4145:
4144:
4141:
4125:
4122:
4119:
4116:
4113:
4110:
4107:
4104:
4101:
4098:
4095:
4092:
4089:
4086:
4083:
4082:
4078:
4075:
4072:
4069:
4066:
4063:
4060:
4057:
4054:
4051:
4048:
4045:
4042:
4039:
4036:
4035:
4028:
4024:
4021:
4018:
4015:
4012:
4009:
4006:
4003:
4000:
3997:
3994:
3991:
3988:
3985:
3982:
3979:
3976:
3973:
3970:
3969:
3965:
3962:
3959:
3956:
3953:
3950:
3947:
3944:
3941:
3938:
3935:
3932:
3929:
3926:
3923:
3920:
3917:
3914:
3911:
3910:
3906:
3904:
3894:
3891:
3888:
3878:
3875:
3872:
3869:
3866:
3863:
3860:
3858:
3852:
3849:
3846:
3843:
3840:
3837:
3835:
3832:
3829:
3828:
3824:
3822:
3812:
3809:
3806:
3803:
3800:
3797:
3794:
3790:
3788:
3782:
3780:
3774:
3772:
3766:
3764:
3758:
3755:
3753:
3747:
3745:
3739:
3736:
3734:
3731:
3728:
3727:
3723:
3721:
3711:
3709:
3703:
3700:
3697:
3694:
3691:
3689:
3687:
3677:
3676:
3672:
3670:
3660:
3658:
3651:
3648:
3646:
3639:
3636:
3633:
3630:
3629:
3625:
3619:
3617:
3607:
3606:
3600:
3583:
3576:
3571:
3569:
3564:
3562:
3557:
3556:
3553:
3546:
3541:
3537:
3536:
3525:
3521:
3516:
3511:
3507:
3503:
3499:
3495:
3491:
3486:
3482:
3478:
3473:
3468:
3464:
3460:
3456:
3452:
3448:
3443:
3439:
3435:
3431:
3427:
3423:
3419:
3414:
3410:
3406:
3402:
3398:
3397:Plant Science
3393:
3389:
3385:
3381:
3377:
3373:
3369:
3364:
3360:
3356:
3352:
3348:
3344:
3340:
3335:
3331:
3327:
3323:
3319:
3315:
3311:
3306:
3302:
3298:
3294:
3290:
3286:
3282:
3277:
3273:
3269:
3265:
3261:
3257:
3252:
3248:
3244:
3240:
3236:
3232:
3228:
3223:
3222:
3209:
3205:
3200:
3195:
3191:
3187:
3186:
3181:
3174:
3172:
3170:
3168:
3166:
3164:
3162:
3153:
3149:
3145:
3141:
3137:
3133:
3132:
3127:
3120:
3118:
3116:
3114:
3112:
3110:
3101:
3097:
3093:
3089:
3084:
3079:
3075:
3071:
3070:
3065:
3058:
3056:
3054:
3052:
3043:
3039:
3035:
3031:
3027:
3026:
3021:
3014:
3012:
3010:
3001:
2997:
2993:
2989:
2985:
2981:
2974:
2966:
2962:
2957:
2952:
2947:
2942:
2938:
2934:
2930:
2926:
2925:
2920:
2912:
2904:
2900:
2896:
2892:
2887:
2882:
2878:
2874:
2873:
2868:
2861:
2853:
2849:
2845:
2841:
2837:
2833:
2829:
2825:
2824:
2823:Extremophiles
2816:
2808:
2804:
2800:
2796:
2792:
2788:
2781:
2773:
2769:
2764:
2759:
2754:
2749:
2745:
2741:
2737:
2735:
2726:
2718:
2714:
2710:
2708:9780121821524
2704:
2700:
2696:
2692:
2688:
2681:
2673:
2669:
2665:
2663:9780470123096
2659:
2655:
2651:
2647:
2640:
2632:
2626:
2618:
2614:
2610:
2606:
2599:
2588:
2584:
2580:
2576:
2575:
2569:
2565:
2561:
2557:
2553:
2552:
2547:
2542:
2541:
2537:
2531:
2527:
2522:
2513:
2505:
2501:
2497:
2493:
2486:
2471:
2467:
2463:
2459:
2455:
2451:
2447:
2440:
2432:
2428:
2424:
2420:
2419:
2411:
2409:
2400:
2396:
2392:
2388:
2383:
2378:
2374:
2370:
2369:
2364:
2357:
2355:
2346:
2344:0-471-95512-4
2340:
2336:
2329:
2321:
2317:
2313:
2309:
2305:
2301:
2294:
2290:
2281:
2277:
2274:
2273:Thiosulfinate
2271:
2270:
2264:
2262:
2258:
2253:
2249:
2245:
2240:
2239:thermoplastic
2236:
2235:recyclability
2231:
2228:
2223:
2219:
2215:
2211:
2201:
2199:
2194:
2190:
2186:
2185:vulcanization
2171:
2165:
2157:
2147:
2136:
2134:
2122:
2118:
2116:
2112:
2108:
2104:
2100:
2095:
2093:
2077:
2060:
2043:
2035:
2032:
2021:
2018:
2007:
2004:
2003:
2002:
1992:
1988:
1968:
1952:
1930:
1924:
1906:
1900:
1881:
1879:
1875:
1866:
1864:
1860:
1855:
1851:
1847:
1837:
1834:
1829:
1826:degradation,
1825:
1821:
1817:
1816:photosystem I
1813:
1809:
1799:
1797:
1793:
1790:
1786:
1781:
1778:
1777:
1772:
1766:
1764:
1760:
1756:
1752:
1748:
1741:In eukaryotes
1738:
1736:
1732:
1729:and kill the
1728:
1721:
1715:
1711:
1707:
1703:
1687:
1684:November 2023
1677:
1671:
1668:This section
1666:
1662:
1657:
1656:
1653:
1651:
1646:
1644:
1639:
1635:
1627:
1624:and break up
1623:
1619:
1615:
1611:
1607:
1604:
1600:
1596:
1593:
1589:
1585:
1584:
1583:
1580:
1578:
1572:
1568:
1564:
1559:
1555:
1551:
1547:
1543:
1535:
1531:
1527:
1523:
1521:
1517:
1513:
1509:
1495:
1486:
1483:
1479:
1475:
1470:
1467:
1463:
1459:
1455:
1451:
1447:
1443:
1438:
1436:
1432:
1426:
1416:
1412:
1406:
1403:
1395:
1378:
1375:
1374:
1373:
1371:
1367:
1362:
1344:
1333:
1325:
1313:
1308:
1306:
1285:
1282:
1271:
1258:
1249:
1237:
1224:
1203:
1192:
1168:
1155:
1146:
1143:
1136:
1123:
1119:
1115:
1110:
1093:
1081:
1056:
1049:
1039:
1036:
1029:
1016:
1012:
1007:
1005:
971:
958:
950:
946:
935:
928:
913:
900:
880:
879:
878:
863:
859:
826:
821:
813:
809:
801:
786:
781:
772:
765:
754:
753:
752:
740:
737:
733:
729:
724:
703:
696:
688:
668:
657:
637:
630:
623:
611:
610:
609:
607:
603:
599:
595:
594:sulfenic acid
591:
569:
560:
557:
552:
543:
540:
533:
513:
502:
482:
474:
473:
472:
466:
462:
452:
450:
446:
422:
411:
403:
392:
391:
390:
388:
387:hydrogenation
385:Although the
383:
381:
377:
372:
370:
358:
336:
328:
321:
309:
301:
294:
282:
281:
280:
278:
274:
273:electrophiles
266:
261:
255:
250:
240:
238:
230:
226:
223:(also called
222:
213:
211:
207:
172:
166:
155:
149:
138:
132:
113:
111:
110:
100:
98:
94:
90:
86:
81:
79:
75:
71:
67:
52:
47:
41:
37:
33:
29:
22:
5588:Butyrylation
5550:
5291:
5162:Racemization
5147:Peptide bond
5072:
5065:
4979:Vinyl halide
4936:
4866:Borinic acid
4861:Boronic acid
4838:Thioxanthate
4777:
4178:Hydrocarbons
3685:
3640:
3581:
3500:(1): 28–32.
3497:
3494:EMBO Reports
3493:
3454:
3450:
3421:
3417:
3400:
3396:
3371:
3367:
3342:
3338:
3313:
3309:
3284:
3280:
3255:
3230:
3226:
3189:
3183:
3135:
3129:
3073:
3067:
3040:– via
3029:
3023:
2983:
2979:
2973:
2928:
2922:
2911:
2876:
2872:Cell Reports
2870:
2860:
2830:(1): 29–38.
2827:
2821:
2815:
2790:
2787:Biochemistry
2786:
2780:
2743:
2739:
2733:
2725:
2686:
2680:
2645:
2639:
2625:cite journal
2608:
2604:
2598:
2578:
2572:
2555:
2549:
2545:
2536:
2521:
2512:
2495:
2491:
2485:
2473:. Retrieved
2453:
2449:
2439:
2422:
2416:
2372:
2366:
2334:
2328:
2303:
2299:
2293:
2232:
2222:self-healing
2207:
2182:
2174:Applications
2153:
2137:
2133:thiocarbonyl
2119:
2103:thioselenide
2096:
2090:
2001:. Examples:
1948:
1872:
1843:
1832:
1808:chloroplasts
1805:
1782:
1774:
1767:
1744:
1699:
1681:
1669:
1647:
1637:
1633:
1631:
1617:
1613:
1609:
1587:
1581:
1570:
1539:
1522:is present.
1505:
1473:
1471:
1465:
1453:
1449:
1439:
1430:
1422:
1391:
1363:
1309:
1111:
1008:
997:
847:
746:
732:polysulfides
725:
722:
587:
458:
442:
384:
373:
354:
277:nucleophiles
246:
228:
224:
220:
214:
203:
107:
101:
89:biochemistry
82:
73:
69:
45:
35:
31:
25:
5652:Diphthamide
5611:Methylation
5578:Lactylation
5540:Deamination
5530:Sumoylation
5505:Acetylation
5500:Methylation
5459:Deamidation
5431:Methylation
5380:Prenylation
5205:Methylation
5195:Formylation
5185:Acetylation
5157:Proteolysis
5043:Thiocyanate
5038:Sulfonamide
5003:Perchlorate
4991:Acyl halide
4952:Fluoroethyl
4833:Thionoester
4721:Phosphonium
4706:Phosphinate
4701:Phosphonous
4689:Phosphonate
4388:Hydroperoxy
4210:Cyclopropyl
3192:: 586–625.
2611:: 223–240.
1763:glutathione
1708:reactions.
1650:thioredoxin
1478:thioredoxin
1458:glutathione
862:Bunte salts
858:phthalimido
449:ferrodoxins
156:, a vitamin
154:lipoic acid
109:persulfides
5940:Categories
5775:Tryptophan
5771:Tryptophan
5727:Methionine
5668:Tryptophan
5451:Asparagine
5221:C terminus
5177:N terminus
4947:Haloalkane
4818:Thioketone
4773:Persulfide
4669:Phosphorus
4634:Isocyanate
4624:Isonitrile
4525:or oxygen
4523:hydrogen,
4519:not being
4500:Orthoester
4393:Dioxiranes
4371:Enol ether
4259:1-Propenyl
3582:Disulfides
3545:Disulfides
2746:(67): 67.
2492:Org. Synth
2286:References
2200:material.
2115:sulfoxides
2107:diselenide
1878:cysteamine
1874:Cystinosis
1869:In disease
1785:protamines
1747:eukaryotic
1554:methionine
1544:groups of
1116:(β-ME) or
728:alkylation
465:sulfhydryl
243:Properties
36:disulphide
5921:Desmosine
5834:Histidine
5654:formation
5644:Histidine
5563:Glycation
5510:Acylation
5474:Glutamine
5413:Glutamate
5390:Aspartate
5332:Sulfation
5268:Threonine
5229:Amidation
5200:Glycation
5080:inorganic
4914:Tellurium
4828:Thioester
4793:Sulfoxide
4778:Disulfide
4766:Sulfonium
4716:Phosphine
4694:Phosphite
4677:Phosphate
4609:Carbamate
4584:Hydrazone
4517:element,
4515:Only one
4488:Anhydride
4227:Methylene
3208:237649642
3152:234925061
3100:218975603
2895:2211-1247
2530:Interchim
2418:Synthesis
2248:toughness
2198:thermoset
2150:Misnomers
1993:such as H
1991:peroxides
1798:species.
1796:mammalian
1792:chromatin
1731:bacterium
1706:oxidation
1676:talk page
1614:increases
1534:cysteines
1368:and then
1342:⟶
1250:−
1211:⇀
1204:−
1193:−
1186:↽
1137:−
1088:⟶
1047:⟶
1030:−
994:Reactions
940:⟶
802:−
795:⟶
697:−
676:⇀
669:−
658:−
651:↽
624:−
602:complexes
570:−
534:−
521:⇀
514:−
503:−
496:↽
461:oxidation
455:Synthesis
420:⟶
337:−
322:−
315:⟶
310:−
295:−
200:Structure
112:instead.
80:groups.
32:disulfide
28:chemistry
21:Bisulfide
5909:Allysine
5905:Allysine
5901:Allysine
5838:Tyrosine
5811:Tyrosine
5753:Tyrosine
5704:Cysteine
5700:Cysteine
5598:Arginine
5367:Cysteine
5309:Tyrosine
5061:See also
4996:Chloride
4922:Tellurol
4876:Selenium
4843:Xanthate
4557:Ammonium
4539:Nitrogen
4521:carbon,
4478:Carboxyl
4445:Aldehyde
4433:Acryloyl
4415:carbonyl
4319:hydrogen
4274:Cumulene
3524:15643448
3481:14757749
3438:12524212
3388:10920260
3247:14444674
3092:32462759
3000:23416144
2965:32354997
2903:23041318
2852:11491989
2844:17508126
2807:11009618
2772:20836848
2470:28260381
2391:12415301
2267:See also
2244:strength
2227:aromatic
2193:rheology
2099:peroxide
1967:chlorine
1854:Feathers
1850:keratins
1794:of many
1776:Vaccinia
1702:bacteria
1567:cysteine
1546:cysteine
1454:in vitro
1446:cysteine
1394:thiolate
947:′
936:′
827:″
810:′
787:″
773:′
689:′
638:′
97:proteins
93:cysteine
5869:Glycine
5861:Alanine
5842:Glycine
5815:Glycine
5626:Proline
5294:-GlcNAc
5140:General
5085:organic
4884:Selenol
4808:Sulfone
4761:Sulfide
4659:NONOate
4654:Nitroso
4644:Nitrite
4639:Nitrate
4629:Cyanate
4619:Nitrile
4604:Amidine
4599:Imidate
4569:Nitrene
4564:Hydrazo
4552:Enamine
4483:Acetoxy
4471:carboxy
4438:Benzoyl
4376:Epoxide
4359:Methoxy
4349:Alcohol
4303:Carbene
4237:Methine
4032:
3515:1299221
3472:2172237
3359:9570840
3330:6547275
3301:7338898
2956:7245129
2933:Bibcode
2763:2946281
2734:E. coli
2717:7651233
2672:2407068
2528:, from
2498:: 147.
2399:2885059
2308:Bibcode
2142:S−S−SCH
2135:group.
1787:in the
1759:cytosol
1735:Archaea
1592:entropy
1563:cystine
1530:Cystine
1516:cytosol
1482:vicinal
1474:in vivo
1442:protein
860:group.
856:is the
237:cystine
137:cystine
104:R−S−S−H
70:SS-bond
53:or the
5961:Sulfur
5913:Lysine
5865:Serine
5807:Serine
5749:Lysine
5492:Lysine
5264:Serine
4984:Iodide
4904:Selone
4748:Sulfur
4457:Ketone
4450:Ketene
4428:Acetyl
4383:Peroxy
4354:Alkoxy
4344:Acetal
4325:oxygen
4314:carbon
4298:Alkyne
4291:Benzyl
4286:Phenyl
4269:Allene
4264:Crotyl
4244:Alkene
4232:Bridge
4220:Pentyl
4205:Propyl
4195:Methyl
3522:
3512:
3479:
3469:
3436:
3386:
3357:
3328:
3299:
3272:927170
3270:
3245:
3206:
3150:
3098:
3090:
2998:
2963:
2953:
2901:
2893:
2850:
2842:
2805:
2770:
2760:
2715:
2705:
2670:
2660:
2581:: 62.
2558:: 45.
2475:31 May
2468:
2397:
2389:
2341:
2259:, and
2189:rubber
2105:, and
2042:pyrite
2040:), or
1987:Oxygen
1905:Pyrite
1824:starch
1618:lowers
1402:sulfur
1396:group
1323:ArSSAr
1011:thiols
848:where
598:iodine
279:(Nu):
5212:(Gly)
5016:Other
4853:Boron
4823:Thial
4756:Thiol
4649:Nitro
4614:Imide
4594:Amide
4579:Oxime
4574:Imine
4547:Amine
4495:Ester
4462:Ynone
4366:Ether
4337:R-O-R
4312:Only
4254:Allyl
4249:Vinyl
4215:Butyl
4200:Ethyl
4190:Alkyl
3204:S2CID
3148:S2CID
3096:S2CID
2848:S2CID
2395:S2CID
2252:creep
2166:, MoS
2127:NCSS)
1951:anion
1789:sperm
1771:redox
1610:links
1542:thiol
1419:bond.
1409:−S−S−
1349:ArSCl
233:RSSR'
78:thiol
66:anion
5131:and
4938:Halo
4423:Acyl
4323:and
4281:Aryl
3520:PMID
3477:PMID
3434:PMID
3384:PMID
3355:PMID
3326:PMID
3297:PMID
3268:PMID
3243:PMID
3088:PMID
2996:PMID
2961:PMID
2899:PMID
2891:ISSN
2840:PMID
2803:PMID
2768:PMID
2713:PMID
2703:ISBN
2668:PMID
2658:ISBN
2631:link
2477:2021
2466:PMID
2423:2008
2387:PMID
2339:ISBN
2183:The
2158:, CS
2034:Iron
1846:hair
1472:The
1405:atom
1221:HOCH
1152:HOCH
1097:NaCl
1079:NaSR
1054:NaSR
944:RSSR
933:NaSR
866:RSSO
726:The
401:RSSR
378:and
257:and
239:.
217:RSSR
34:(or
30:, a
5892:AAs
5798:AAs
5691:AAs
5255:AAs
4589:Azo
4126:No
4123:Md
4120:Fm
4117:Es
4114:Cf
4111:Bk
4108:Cm
4105:Am
4102:Pu
4099:Np
4093:Pa
4090:Th
4087:Ac
4084:**
4079:Yb
4076:Tm
4073:Er
4070:Ho
4067:Dy
4064:Tb
4061:Gd
4058:Eu
4055:Sm
4052:Pm
4049:Nd
4046:Pr
4043:Ce
4040:La
4025:Og
4022:Ts
4019:Lv
4016:Mc
4013:Fl
4010:Nh
4007:Cn
4004:Rg
4001:Ds
3998:Mt
3995:Hs
3992:Bh
3989:Sg
3986:Db
3983:Rf
3980:Lr
3977:**
3974:Ra
3971:Fr
3966:Rn
3963:At
3960:Po
3957:Bi
3954:Pb
3951:Tl
3948:Hg
3945:Au
3942:Pt
3939:Ir
3936:Os
3933:Re
3927:Ta
3924:Hf
3921:Lu
3915:Ba
3912:Cs
3907:Xe
3892:Te
3876:Sn
3873:In
3870:Cd
3867:Ag
3864:Pd
3861:Rh
3854:RuS
3850:Tc
3847:Mo
3844:Nb
3841:Zr
3833:Sr
3830:Rb
3825:Kr
3810:Se
3807:As
3804:Ge
3801:Ga
3798:Zn
3793:CuS
3784:NiS
3776:CoS
3768:FeS
3760:MnS
3756:Cr
3741:TiS
3737:Sc
3732:Ca
3724:Ar
3698:Si
3695:Al
3692:Mg
3673:Ne
3634:Be
3631:Li
3626:He
3510:PMC
3502:doi
3467:PMC
3459:doi
3455:164
3426:doi
3405:doi
3401:175
3376:doi
3372:128
3347:doi
3343:258
3318:doi
3314:138
3289:doi
3285:151
3260:doi
3235:doi
3194:doi
3140:doi
3078:doi
3034:doi
2988:doi
2951:PMC
2941:doi
2929:117
2881:doi
2832:doi
2795:doi
2758:PMC
2748:doi
2695:doi
2650:doi
2613:doi
2583:doi
2560:doi
2500:doi
2458:doi
2427:doi
2377:doi
2316:doi
2187:of
2081:MoS
1953:is
1909:FeS
1828:ATP
1751:RER
1745:In
1727:DNA
1290:RSH
1255:SCH
1091:HSR
1085:HCl
1000:S−S
818:HNR
778:SNR
763:RSH
707:RSH
487:RSH
469:−SH
463:of
427:RSH
365:S−S
361:C−C
269:S−S
260:C−H
254:C−C
227:or
99:.
83:In
48:−R′
46:S−S
38:in
26:In
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4321:,
4316:,
4096:U
4037:*
3930:W
3918:*
3889:?
3880:Sb
3838:Y
3818:Br
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3749:VS
3729:K
3717:Cl
3701:P
3679:Na
3649:N
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3641:RS
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1632:A
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1460:,
1425:pH
1398:−S
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1330:Cl
1280:OH
1268:CH
1234:CH
1177:SH
1165:CH
1141:SR
1133:RS
1044:Na
1034:SR
1026:RS
968:SO
955:Na
889:Na
875:Na
850:R″
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701:SR
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628:SR
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538:SR
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326:Nu
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306:Nu
299:SR
291:RS
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1960:2
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