85:, and the rate depends strongly on the distance between the energy donor and energy acceptor molecules. Before an excited molecule can transition back to its ground state, energy needs to be harvested. This excitation is transferred among chromophores where it is delivered to the reaction centre. Light-harvesting complexes have their pigments specifically positioned to optimize these rates.
214:
75:
Photosynthesis is a process where light is absorbed or harvested by pigment protein complexes which are able to turn sunlight into energy. Absorption of a photon by a molecule takes place when pigment protein complexes harvest sunlight leading to electronic excitation delivered to the reaction centre
80:
matches that of an electronic transition. The fate of such excitation can be a return to the ground state or another electronic state of the same molecule. When the excited molecule has a nearby neighbour molecule, the excitation energy may also be transferred, through electromagnetic interactions,
233:
is known as the phycobilisome which is composed of linear tetrapyrrole pigments. Pigment-protein complexes referred to as R-phycoerythrin are rod-like in shape and make up the rods and core of the phycobilisome. Little light reaches algae that reside at a depth of one meter or more in seawater, as
99:
Purple bacteria is a type of photosynthetic organism with a light harvesting complex consisting of two pigment protein complexes referred to as LH1 and LH2. Within the photosynthetic membrane, these two complexes differ in terms of their arrangement. The LH1 complexes surround the reaction centre,
269:
subunits that radiate out from this center like thin tubes. This increases the surface area of the absorbing section and helps focus and concentrate light energy down into the reaction center to form chlorophyll. The energy transfer from excited electrons absorbed by pigments in the
242:, are the chromophores that bind through a covalent thioether bond to their apoproteins at cystein residues. The apoprotein with its chromophore is called phycocyanin, phycoerythrin, and allophycocyanin, respectively. They often occur as hexamers of α and β subunits (α
122:
The main light harvesting complex in Green bacteria is known as the chlorosome. The chlorosome is equipped with rod-like BChl c aggregates with protein embedded lipids surrounding it. Chlorosomes are found outside of the membrane which covers the reaction centre.
47:
alone. The light which is captured by the chromophores is capable of exciting molecules from their ground state to a higher energy state, known as the excited state. This excited state does not last very long and is known to be short-lived.
1248:
Lokstein (1994)The role of light-harvesting complex II energy dissipation: an in-vivo fluorescence in excess excitation study on the origin of high-energy quenching. Journal of
Photochemistry and Photobiology 26:
184:. These molecules also absorb light most efficiently in the 400 – 500 nm range. Due to their absorption region, carotenoids appear red and yellow and provide most of the red and yellow colours present in
824:"The primary structure of the antenna polypeptides of Ectothiorhodospira halochloris and Ectothiorhodospira halophila. Four core-type antenna polypeptides in E. halochloris and E. halophila"
51:
Light-harvesting complexes are found in a wide variety among the different photosynthetic species, with no homology among the major groups. The complexes consist of proteins and
863:
Brunisholz RA, Zuber H (1992). "Structure, function and organization of antenna polypeptides and antenna complexes from the three families of
Rhodospirillaneae".
195:
The carotenoid molecules also serve a safeguarding function. Carotenoid molecules suppress damaging photochemical reactions, in particular those including
1605:
257:
The geometrical arrangement of a phycobilisome is very elegant and results in 95% efficiency of energy transfer. There is a central core of
1214:
Light
Harvesting by Phycobilisomes Annual Review of Biophysics and Biophysical Chemistry Vol. 14: 47-77 (Volume publication date June 1985)
108:
and carotenoids to gather light energy. These proteins are arranged in a ring-like fashion creating a cylinder that spans the membrane.
1590:
1388:
1299:
140:
152:
are important in light-harvesting complexes present in plants. Chlorophyll b is almost identical to chlorophyll a, except it has a
293:
765:"The molecular mechanisms of light adaption in light-harvesting complexes of purple bacteria revealed by a multiscale modeling"
706:"The molecular mechanisms of light adaption in light-harvesting complexes of purple bacteria revealed by a multiscale modeling"
647:"The molecular mechanisms of light adaption in light-harvesting complexes of purple bacteria revealed by a multiscale modeling"
1338:
199:, which exposure to sunlight can cause. Plants that lack carotenoid molecules quickly die upon exposure to oxygen and light.
254:. They enhance the amount and spectral window of light absorption and fill the "green gap", which occurs in higher plants.
64:
1595:
1636:
1641:
1697:
1656:
131:
use ellipsoidal complexes known as the chlorosome to capture light. Their form of bacteriochlorophyll is green.
1383:
1292:
288:
100:
while the LH2 complexes are arranged around the LH1 complexes and the reaction centre in a peripheral fashion.
56:
44:
1262:
1453:
1498:
1666:
1467:
1320:
1565:
1285:
274:
subunits at the periphery of these antennas appears at the reaction center in less than 100 ps.
94:
82:
40:
1241:
Liu et al. (2004) Crystal structure of spinach major light-harvesting complex at 2.72A° resolution.
1457:
1266:
298:
1692:
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1545:
1493:
1661:
763:
Ramos, Felipe
Cardoso; Nottoli, Michele; Cupellini, Lorenzo; Mennucci, Benedetta (2019-10-30).
704:
Ramos, Felipe
Cardoso; Nottoli, Michele; Cupellini, Lorenzo; Mennucci, Benedetta (2019-10-30).
645:
Ramos, Felipe
Cardoso; Nottoli, Michele; Cupellini, Lorenzo; Mennucci, Benedetta (2019-10-30).
124:
52:
1522:
1252:
MacColl (1998) Cyanobacterial
Phycobilisomes. JOURNAL OF STRUCTURAL BIOLOGY 124(2-3): 311-34.
172:
that have alternating single and double bonds along their length. Such molecules are called
1631:
1527:
1112:
1045:
978:
911:
596:
Fassioli, Francesca; Dinshaw, Rayomond; Arpin, Paul C.; Scholes, Gregory D. (2014-03-06).
547:
Fassioli, Francesca; Dinshaw, Rayomond; Arpin, Paul C.; Scholes, Gregory D. (2014-03-06).
498:
Fassioli, Francesca; Dinshaw, Rayomond; Arpin, Paul C.; Scholes, Gregory D. (2014-03-06).
416:
Fassioli, Francesca; Dinshaw, Rayomond; Arpin, Paul C.; Scholes, Gregory D. (2014-03-06).
367:
Fassioli, Francesca; Dinshaw, Rayomond; Arpin, Paul C.; Scholes, Gregory D. (2014-03-06).
318:
Fassioli, Francesca; Dinshaw, Rayomond; Arpin, Paul C.; Scholes, Gregory D. (2014-03-06).
8:
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where the process of charge separation can take place. when the energy of the captured
1234:
Govindjee & Shevela (2011) Adventures with cyanobacteria: a personal perspective.
1168:"The phycobilisomes: an early requisite for efficient photosynthesis in cyanobacteria"
483:
466:
1227:
Caffarri (2009)Functional architecture of higher plantphotosystem II supercomplexes.
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1101:"Architecture and mechanism of the light-harvesting apparatus of purple bacteria"
1034:"Architecture and mechanism of the light-harvesting apparatus of purple bacteria"
967:"Architecture and mechanism of the light-harvesting apparatus of purple bacteria"
900:"Architecture and mechanism of the light-harvesting apparatus of purple bacteria"
258:
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24:
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Wagner-Huber R, Brunisholz RA, Bissig I, Frank G, Suter F, Zuber H (1992).
808:
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384:
353:
335:
157:
153:
128:
1152:
1099:
Hu, Xiche; Damjanović, Ana; Ritz, Thorsten; Schulten, Klaus (1998-05-26).
1085:
1032:
Hu, Xiche; Damjanović, Ana; Ritz, Thorsten; Schulten, Klaus (1998-05-26).
1018:
965:
Hu, Xiche; Damjanović, Ana; Ritz, Thorsten; Schulten, Klaus (1998-05-26).
951:
898:
Hu, Xiche; Damjanović, Ana; Ritz, Thorsten; Schulten, Klaus (1998-05-26).
884:
849:
213:
168:
between 400 and 500 nm more efficiently. Carotenoids are long linear
1610:
1462:
1378:
262:
165:
149:
145:
28:
781:
722:
663:
117:
1651:
1615:
230:
43:
to collect more of the incoming light than would be captured by the
181:
177:
173:
1308:
821:
189:
60:
467:"Structure and function of bacterial light-harvesting complexes"
1423:
1418:
1413:
1408:
1403:
1398:
1393:
261:, which sits above a photosynthetic reaction center. There are
196:
185:
77:
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1328:
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644:
161:
36:
1560:
1555:
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366:
317:
1165:
598:"Photosynthetic light harvesting: excitons and coherence"
549:"Photosynthetic light harvesting: excitons and coherence"
500:"Photosynthetic light harvesting: excitons and coherence"
418:"Photosynthetic light harvesting: excitons and coherence"
369:"Photosynthetic light harvesting: excitons and coherence"
320:"Photosynthetic light harvesting: excitons and coherence"
1166:
Singh, NK; Sonani, RR; Rastogi, RP; Madamwar, D (2015).
1098:
1031:
964:
897:
217:
Schematic layout of protein subunits in a phycobilisome.
59:
to focus energy, attained from photons absorbed by the
23:
consists of a number of chromophores which are complex
234:
light is absorbed by seawater. The pigments, such as
81:
from one molecule to another. This process is called
160:. This small difference makes chlorophyll b absorb
1684:
27:that may be part of a larger super complex of a
1105:Proceedings of the National Academy of Sciences
1038:Proceedings of the National Academy of Sciences
971:Proceedings of the National Academy of Sciences
904:Proceedings of the National Academy of Sciences
862:
221:The antenna-shaped light harvesting complex of
1307:
134:
1293:
856:
815:
1389:Insulin-like growth factor binding protein
1300:
1286:
464:
141:Light-harvesting complexes of green plants
1265:at the U.S. National Library of Medicine
1191:
1142:
1124:
1075:
1057:
1008:
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780:
739:
721:
680:
662:
621:
572:
523:
482:
441:
392:
343:
212:
294:Photosystem II light-harvesting protein
1685:
602:Journal of the Royal Society Interface
553:Journal of the Royal Society Interface
504:Journal of the Royal Society Interface
422:Journal of the Royal Society Interface
373:Journal of the Royal Society Interface
324:Journal of the Royal Society Interface
1281:
1273:Photosynthesis and all sub categories
88:
111:
63:, toward the reaction center using
13:
1263:Light-harvesting+protein+complexes
1221:
841:10.1111/j.1432-1033.1992.tb16858.x
176:. Two examples of carotenoids are
14:
1709:
1642:Cholesterylester transfer protein
1256:
65:Förster resonance energy transfer
465:KĂĽhlbrandt, Werner (June 1995).
202:
1657:Latent TGF-beta binding protein
1606:Photosynthetic Reaction Centers
1208:
1159:
1092:
1025:
958:
891:
756:
1591:Plant Light-Harvesting Complex
1384:Growth hormone binding protein
697:
638:
589:
540:
491:
458:
409:
360:
311:
289:Photosynthetic reaction center
57:photosynthetic reaction center
45:photosynthetic reaction center
1:
484:10.1016/S0969-2126(01)00184-8
304:
1454:Sex hormone binding globulin
877:10.1016/1011-1344(92)87010-7
7:
1499:Calmodulin-binding proteins
277:
135:In cyanobacteria and plants
70:
10:
1714:
1667:Membrane transport protein
1468:Thyroxine-binding globulin
1236:Frontiers in Plant Science
865:J. Photochem. Photobiol. B
206:
138:
115:
92:
1624:
1596:Orange Carotenoid Protein
1581:
1538:
1481:
1367:
1319:
95:Bacterial antenna complex
83:resonance energy transfer
31:, the functional unit in
1458:Androgen binding protein
1267:Medical Subject Headings
299:Light harvesting pigment
21:light-harvesting complex
1672:Odorant binding protein
1546:Retinol binding protein
1494:Calcium-binding protein
1126:10.1073/pnas.95.11.5935
1059:10.1073/pnas.95.11.5935
992:10.1073/pnas.95.11.5935
925:10.1073/pnas.95.11.5935
53:photosynthetic pigments
41:photosynthetic bacteria
16:Protein-pigment complex
1698:Transmembrane proteins
1662:Major urinary proteins
1184:10.17179/excli2014-723
614:10.1098/rsif.2013.0901
565:10.1098/rsif.2013.0901
516:10.1098/rsif.2013.0901
434:10.1098/rsif.2013.0901
385:10.1098/rsif.2013.0901
336:10.1098/rsif.2013.0901
218:
125:Green sulphur bacteria
1523:Iron-binding proteins
216:
1632:Acyl carrier protein
1528:Transferrin receptor
1652:GTP-binding protein
1117:1998PNAS...95.5935H
1050:1998PNAS...95.5935H
983:1998PNAS...95.5935H
916:1998PNAS...95.5935H
106:bacteriochlorophyll
782:10.1039/C9SC02886B
723:10.1039/C9SC02886B
664:10.1039/C9SC02886B
219:
89:In purple bacteria
1680:
1679:
1111:(11): 5935–5941.
1044:(11): 5935–5941.
977:(11): 5935–5941.
910:(11): 5935–5941.
775:(42): 9650–9662.
716:(42): 9650–9662.
657:(42): 9650–9662.
240:phycoerythrobilin
170:organic molecules
112:In green bacteria
1705:
1601:Phycobiliprotein
1313:carrier proteins
1302:
1295:
1288:
1279:
1278:
1229:The EMBO Journal
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651:Chemical Science
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608:(92): 20130901.
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510:(92): 20130901.
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379:(92): 20130901.
364:
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330:(92): 20130901.
315:
227:glaucocystophyta
35:. It is used by
25:subunit proteins
1713:
1712:
1708:
1707:
1706:
1704:
1703:
1702:
1683:
1682:
1681:
1676:
1637:Adaptor protein
1620:
1577:
1534:
1477:
1450:steroid hormone
1375:peptide hormone
1363:
1315:
1306:
1259:
1224:
1222:Further reading
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259:allophycocyanin
253:
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236:phycocyanobilin
211:
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143:
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120:
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102:Purple bacteria
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91:
73:
55:and surround a
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1693:Photosynthesis
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1573:Transcobalamin
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1257:External links
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284:Photosynthesis
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156:in place of a
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1511:Ceruloplasmin
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1482:Metal/element
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1473:Transthyretin
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1463:Transcortin
1379:Follistatin
263:phycocyanin
166:wavelengths
150:carotenoids
29:photosystem
1687:Categories
1321:Fatty acid
1178:: 268–89.
305:References
182:β-carotene
118:Chlorosome
1616:Rhodopsin
1135:0027-8424
1068:0027-8424
1001:0027-8424
934:0027-8424
791:2041-6539
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231:red algae
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278:See also
178:lycopene
174:polyenes
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1583:Pigment
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1368:Hormone
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1193:4553884
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162:light
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