572:
316:
InChI=1/C49H59N4O6.Fe/c1-9-34-31(6)39-25-45-49(46(55)18-12-17-30(5)16-11-15-29(4)14-10-13-28(2)3)33(8)40(52-45)24-44-37(27-54)36(20-22-48(58)59)43(53-44)26-42-35(19-21-47(56)57)32(7)38(51-42)23-41(34)50-39;/h9,13,15,17,23-27,43,46,55H,1,10-12,14,16,18-22H2,2-8H3,(H4-,50,51,52,53,56,57,58,59);/q-1;+2/p-2/b29-15+,30-17+,42-26-;/rC49H57FeN4O6/c1-9-34-31(6)39-25-45-49(46(56)18-12-17-30(5)16-11-15-29(4)14-10-13-28(2)3)33(8)40-24-44-37(27-55)36(20-22-48(59)60)43-26-42-35(19-21-47(57)58)32(7)38-23-41(34)51(39)50(52(38)42,53(40)45)54(43)44/h9,13,15,17,23-27,43,46,56H,1,10-12,14,16,18-22H2,2-8H3,(H,57,58)(H,59,60)/q-1/b29-15+,30-17+
124:
283:
403:
115:
306:
InChI=1S/C49H59N4O6.Fe/c1-9-34-31(6)39-25-45-49(46(55)18-12-17-30(5)16-11-15-29(4)14-10-13-28(2)3)33(8)40(52-45)24-44-37(27-54)36(20-22-48(58)59)43(53-44)26-42-35(19-21-47(56)57)32(7)38(51-42)23-41(34)50-39;/h9,13,15,17,23-27,43,46,55H,1,10-12,14,16,18-22H2,2-8H3,(H4-,50,51,52,53,56,57,58,59);/q-1;+2/p-2/b29-15+,30-17+,42-26-;
613:. CCO is thought to be responsible for conserving the energy of dioxygen reduction by pumping protons into the inter-membrane mitochondrial space. Both the formyl and hydroxyethylfarnesyl groups of heme A are thought to play important roles in this critical process, as published by the influential group of S. Yoshikawa.
190:
700:
Battersby, Alan R.; McDonald, Edward; Thompson, Mervyn; Chaudhry, Irshad A.; Clezy, Peter S.; Fookes, Christopher J. R.; Hai, Ton That (1985). "Isolation, crystallisation, and synthesis of the dimethyl ester of porphyrin a, the iron-free prosthetic group of cytochrome c oxidase".
521:
group at position 8, still containing the methyl group. The correct structure of heme A, based upon NMR and IR experiments of the reduced, Fe(II) form of the heme, was published in 1975. The structure was confirmed by synthesis of the dimethyl ester of the iron-free form.
598:). In addition, this enzyme binds 3 copper, magnesium, zinc, and several potassium and sodium ions. The two heme A groups in CCO are thought to readily exchange electrons between each other, the copper ions and the closely associated protein cytochrome c.
546:
The final structural question of the exact geometric configuration about the first carbon at ring position 3 of ring I, the carbon bound to the hydroxyl group, has been shown to be the chiral S configuration.
585:
An example of a metalloprotein that contains heme A is cytochrome c oxidase. This very complicated protein contains heme A at two different sites, each with a different function. The iron of the heme A of
763:"Absolute configuration of the hydroxyfarnesylethyl group of heme A, determined by X-ray structural analysis of bovine heart cytochrome c oxidase using methods applicable at 2.8 Angstrom resolution"
571:
550:
Like heme B, heme A is often attached to the apoprotein through a coordinate bond between the heme iron and a conserved amino acid side-chain. In the important respiratory protein
416:
868:
Yoshikawa, S.; Shinzawa-Itoh, K.; Nakashima, R.; et al. (1998). "Redox-Coupled
Crystal Structural Changes in Bovine Heart Cytochrome c Oxidase".
332:
1200:
1063:
1059:
992:
466:
and is produced naturally by many organisms. Heme A, often appears a dichroic green/red when in solution, is a structural relative of
726:
554:(CCO) this ligand 5 for the heme A at the oxygen reaction center is a histidyl group. Histidine is a common ligand for many
340:
OC(=O)CC/c6c(\C)c3n7c6cc2c(/CCC(O)=O)c(/C=O)c1cc5n8c(cc4n(78n12)c(c=3)c(C=C)c4c)c(\C(O)CC\C=C(/C)CC\C=C(/C)CC\C=C(C)/C)c5\C
88:
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37:
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84:
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61:
26:
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227:
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side chain are thought to play important roles in conservation of the energy of oxygen reduction by
278:
1272:
767:
221:
123:
1285:
1004:
594:
is sometimes bound by 5 other atoms leaving the sixth site available to bind dioxygen (molecular
806:"The low-spin heme of cytochrome c oxidase as the driving element of the proton-pumping process"
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1185:
1027:
68:
33:
210:
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1190:
1037:
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1103:
928:
819:
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610:
551:
447:
166:
8:
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1083:
156:
53:
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823:
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282:
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517:, in that both have this farnesyl addition at position 2 but heme O does not have the
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21:
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590:
is hexacoordinated, that is bound with 6 other atoms. The iron of the heme A of
657:
Caughey, W.S.; Smythe, G.A.; O'Keefe, D.H.; Maskasky, J.E.; Smith, M.L. (1975).
1149:
739:
535:
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591:
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in 1951 and shown by him to be the active component of the integral membrane
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Heme A in the cytochrome a portion of cytochrome c oxidase, bound by two
506:
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1210:
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201:
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Except where otherwise noted, data are given for materials in their
970:
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915:"The proton pumping pathway of bovine heart cytochrome c oxidase"
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487:
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467:
179:
724:
Warburg, O; Gewitz H S. (1951). "Cytohämin aus
Herzmuskel".
266:
1342:
1317:
1230:
919:
810:
622:
510:
443:
804:
Tsukihara T, Shimokata K, Katayama Y, et al. (2003).
760:
913:
Shimokata K, Katayama Y, Murayama H, et al. (2007).
114:
509:
side chain at ring position 2 of the iron tetrapyrrole
703:
Journal of the
Chemical Society, Perkin Transactions 1
723:
530:Heme A was first isolated by the German biochemist
761:Yamashita E, Aoyama H, Yao M, et al. (2005).
91:| Latest revision (diff) | Newer revision → (diff)
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60:Revision as of 08:03, 10 November 2023 by
950:
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47:
277:
226:
14:
1385:
144:Iron cytoporphyrin IX, formilporphyrin
78:(so text won't be offset so much)
49:(so text won't be offset so much)
974:
727:Zeitschrift für Physiologische Chemie
309:Key: RRRJRRNGYOECDS-ZHOBENDVSA-L
44:
25:
1000:
493:at ring position 8 is oxidized to a
319:Key: RRRJRRNGYOECDS-DRKRPJRXBB
239:
97:
82:
541:
122:
113:
98:
1409:
52:. The present address (URL) is a
659:"Heme A of Cytochrome c Oxidase"
570:
505:chain, has been attached to the
401:
664:Journal of Biological Chemistry
397:(at 25 °C , 100 kPa).
906:
797:
754:
717:
693:
650:
13:
1:
884:10.1126/science.280.5370.1723
678:10.1016/S0021-9258(19)40860-0
643:
474:, the red pigment in blood.
7:
616:
478:Relationship to other hemes
109:
24:of this page, as edited by
10:
1414:
740:10.1515/bchm2.1951.288.1.1
525:
499:hydroxyethylfarnesyl group
462:an iron atom. Heme A is a
1355:
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1176:
1018:
1011:
782:10.1107/S0907444905023358
582:residues (shown in pink)
391:
348:
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149:
141:
136:
108:
768:Acta Crystallographica D
942:10.1073/pnas.0611627104
833:10.1073/pnas.2635097100
513:. Heme A is similar to
45:08:03, 10 November 2023
538:cytochrome c oxidase.
127:
118:
387:852.837
126:
117:
711:10.1039/P19850000135
637:cellular respiration
633:Cytochrome c oxidase
611:cytochrome c oxidase
552:cytochrome c oxidase
482:Heme A differs from
448:coordination complex
933:2007PNAS..104.4200S
878:(5370): 1723–1729.
824:2003PNAS..10015304T
818:(26): 15304–15309.
105:
89:← Previous revision
424:Infobox references
128:
119:
103:
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1351:
1350:
927:(10): 4200–4205.
775:(10): 1373–1377.
671:(19): 7602–7622.
470:, a component of
432:Chemical compound
430:
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262:CompTox Dashboard
191:Interactive image
132:
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100:Chemical compound
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450:consisting of a
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56:to this version.
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54:permanent link
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1393:Tetrapyrroles
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1263:Molybdopterin
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1216:Cofactor F430
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1175:
1169:
1168:Coenzyme F420
1166:
1159:
1151:
1150:Phylloquinone
1148:
1145:
1144:Ascorbic acid
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592:cytochrome a3
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1398:Biomolecules
1368:
1362:
1268:Mycofactocin
1258:Methanofuran
1234:
1178:non-vitamins
1012:Active forms
924:
918:
908:
875:
869:
815:
809:
799:
772:
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719:
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695:
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588:cytochrome a
584:
577:
556:hemeproteins
549:
545:
532:Otto Warburg
529:
497:group and a
481:
439:
435:
434:
150:Identifiers
142:Other names
63:Alfa-ketosav
28:Alfa-ketosav
20:This is the
19:
18:
1253:Lipoic Acid
1231:Heme / Haem
1158:Menaquinone
628:Hemoprotein
464:biomolecule
452:macrocyclic
349:Properties
1387:Categories
1356:Base forms
1300:metal ions
1226:Coenzyme Q
1221:Coenzyme M
1211:Coenzyme B
1074:Coenzyme A
1028:TPP / ThDP
734:(1): 1–4.
644:References
607:isoprenoid
560:hemoglobin
558:including
503:isoprenoid
491:side chain
486:in that a
472:hemoglobin
383:Molar mass
202:ChemSpider
178:3D model (
167:18535-39-2
157:CAS Number
1286:THMPT / H
1084:PLP / P5P
1005:cofactors
601:Both the
580:histidine
564:myoglobin
460:chelating
456:porphyrin
377:Fe
1371:vitamins
1364:vitamins
1278:THB / BH
1112:DHFA / H
1104:THFA / H
1020:vitamins
961:17360500
900:37147458
852:14673090
791:16204889
748:14860765
617:See also
211:21106444
73:contribs
38:contribs
952:1820732
929:Bibcode
892:9624044
871:Science
820:Bibcode
705:: 135.
526:History
442:) is a
417:what is
415: (
250:5288529
237:PubChem
104:Heme A
1318:Fe, Fe
1130:AdoCbl
1094:Biotin
1002:Enzyme
959:
949:
898:
890:
850:
843:307562
840:
789:
746:
687:170266
685:
603:formyl
596:oxygen
519:formyl
515:heme o
495:formyl
488:methyl
484:heme B
468:heme B
440:haem A
436:Heme A
412:verify
409:
333:SMILES
228:Heme+a
137:Names
1134:MeCbl
1064:NADPH
896:S2CID
507:vinyl
501:, an
298:InChI
180:JSmol
1369:see
1201:PAPS
1196:SAMe
1120:MTHF
1060:NADP
1056:NADH
957:PMID
920:PNAS
888:PMID
848:PMID
811:PNAS
787:PMID
744:PMID
683:PMID
623:Heme
562:and
511:heme
446:, a
444:heme
438:(or
222:MeSH
85:diff
69:talk
34:talk
1290:MPT
1273:PQQ
1206:GSH
1191:CTP
1186:ATP
1156:),
1146:(C)
1052:NAD
1042:FAD
1038:FMN
947:PMC
937:doi
925:104
880:doi
876:280
838:PMC
828:doi
816:100
777:doi
736:doi
732:288
707:doi
673:doi
669:250
267:EPA
240:CID
43:at
1389::
1367::
1343:Zn
1338:Ni
1333:Mo
1328:Mn
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