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Light-harvesting complex

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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
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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,
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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
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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,
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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.
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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.
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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
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Brunisholz RA, Zuber H (1992). "Structure, function and organization of antenna polypeptides and antenna complexes from the three families of Rhodospirillaneae".
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The carotenoid molecules also serve a safeguarding function. Carotenoid molecules suppress damaging photochemical reactions, in particular those including
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The geometrical arrangement of a phycobilisome is very elegant and results in 95% efficiency of energy transfer. There is a central core of
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Light Harvesting by Phycobilisomes Annual Review of Biophysics and Biophysical Chemistry Vol. 14: 47-77 (Volume publication date June 1985)
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and carotenoids to gather light energy. These proteins are arranged in a ring-like fashion creating a cylinder that spans the membrane.
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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.
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while the LH2 complexes are arranged around the LH1 complexes and the reaction centre in a peripheral fashion.
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subunits at the periphery of these antennas appears at the reaction center in less than 100 ps.
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Liu et al. (2004) Crystal structure of spinach major light-harvesting complex at 2.72A° resolution.
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Ramos, Felipe Cardoso; Nottoli, Michele; Cupellini, Lorenzo; Mennucci, Benedetta (2019-10-30).
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Ramos, Felipe Cardoso; Nottoli, Michele; Cupellini, Lorenzo; Mennucci, Benedetta (2019-10-30).
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Ramos, Felipe Cardoso; Nottoli, Michele; Cupellini, Lorenzo; Mennucci, Benedetta (2019-10-30).
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MacColl (1998) Cyanobacterial Phycobilisomes. JOURNAL OF STRUCTURAL BIOLOGY 124(2-3): 311-34.
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that have alternating single and double bonds along their length. Such molecules are called
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Fassioli, Francesca; Dinshaw, Rayomond; Arpin, Paul C.; Scholes, Gregory D. (2014-03-06).
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Fassioli, Francesca; Dinshaw, Rayomond; Arpin, Paul C.; Scholes, Gregory D. (2014-03-06).
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Fassioli, Francesca; Dinshaw, Rayomond; Arpin, Paul C.; Scholes, Gregory D. (2014-03-06).
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Fassioli, Francesca; Dinshaw, Rayomond; Arpin, Paul C.; Scholes, Gregory D. (2014-03-06).
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Fassioli, Francesca; Dinshaw, Rayomond; Arpin, Paul C.; Scholes, Gregory D. (2014-03-06).
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Fassioli, Francesca; Dinshaw, Rayomond; Arpin, Paul C.; Scholes, Gregory D. (2014-03-06).
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where the process of charge separation can take place. when the energy of the captured
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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.
1197: 1148: 1143: 1130: 1100: 1081: 1076: 1063: 1033: 1014: 1009: 996: 966: 947: 942: 929: 899: 880: 876: 845: 804: 786: 745: 727: 686: 668: 627: 578: 529: 447: 398: 349: 239: 169: 1600: 1187: 1179: 1138: 1120: 1071: 1053: 1004: 986: 937: 919: 872: 835: 794: 776: 735: 717: 676: 658: 617: 609: 568: 560: 519: 511: 478: 437: 429: 388: 380: 339: 331: 226: 1272: 1449: 1374: 1312: 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: 235: 101: 24: 1572: 1440: 283: 32: 1686: 1646: 1510: 1472: 1435: 1277: 1134: 1067: 1000: 933: 790: 731: 672: 271: 266: 222: 208: 1125: 1058: 991: 924: 1430: 1201: 1183: 822:
Wagner-Huber R, Brunisholz RA, Bissig I, Frank G, Suter F, Zuber H (1992).
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Hu, Xiche; Damjanović, Ana; Ritz, Thorsten; Schulten, Klaus (1998-05-26).
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Hu, Xiche; Damjanović, Ana; Ritz, Thorsten; Schulten, Klaus (1998-05-26).
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Hu, Xiche; Damjanović, Ana; Ritz, Thorsten; Schulten, Klaus (1998-05-26).
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Hu, Xiche; Damjanović, Ana; Ritz, Thorsten; Schulten, Klaus (1998-05-26).
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between 400 and 500 nm more efficiently. Carotenoids are long linear
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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: 1358: 1353: 1348: 1333: 1328: 762: 703: 644: 161: 36: 1560: 1555: 1550: 595: 546: 497: 415: 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).
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Schematic layout of protein subunits in a phycobilisome.
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to focus energy, attained from photons absorbed by the
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consists of a number of chromophores which are complex
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light is absorbed by seawater. The pigments, such as
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from one molecule to another. This process is called
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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: 990: 941: 923: 839: 798: 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 1215: 1212: 1206: 1205: 1195: 1163: 1157: 1156: 1146: 1128: 1096: 1090: 1089: 1079: 1061: 1029: 1023: 1022: 1012: 994: 962: 956: 955: 945: 927: 895: 889: 888: 860: 854: 853: 843: 819: 813: 812: 802: 784: 769:Chemical Science 760: 754: 753: 743: 725: 710:Chemical Science 701: 695: 694: 684: 666: 651:Chemical Science 642: 636: 635: 625: 608:(92): 20130901. 593: 587: 586: 576: 559:(92): 20130901. 544: 538: 537: 527: 510:(92): 20130901. 495: 489: 488: 486: 462: 456: 455: 445: 428:(92): 20130901. 413: 407: 406: 396: 379:(92): 20130901. 364: 358: 357: 347: 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 1219: 1218: 1213: 1209: 1164: 1160: 1097: 1093: 1030: 1026: 963: 959: 896: 892: 861: 857: 828:Eur. J. Biochem 820: 816: 761: 757: 702: 698: 643: 639: 594: 590: 545: 541: 496: 492: 463: 459: 414: 410: 365: 361: 316: 312: 307: 280: 259:allophycocyanin 253: 249: 245: 236:phycocyanobilin 211: 205: 143: 137: 120: 114: 102:Purple bacteria 97: 91: 73: 55:and surround a 17: 12: 11: 5: 1711: 1701: 1700: 1695: 1693:Photosynthesis 1678: 1677: 1675: 1674: 1669: 1664: 1659: 1654: 1649: 1644: 1639: 1634: 1628: 1626: 1622: 1621: 1619: 1618: 1613: 1608: 1603: 1598: 1593: 1587: 1585: 1579: 1578: 1576: 1575: 1573:Transcobalamin 1570: 1569: 1568: 1563: 1558: 1553: 1542: 1540: 1536: 1535: 1533: 1532: 1531: 1530: 1525: 1515: 1514: 1513: 1503: 1502: 1501: 1496: 1485: 1483: 1479: 1478: 1476: 1475: 1470: 1465: 1460: 1446: 1445: 1444: 1443: 1438: 1428: 1427: 1426: 1421: 1416: 1411: 1406: 1401: 1396: 1386: 1381: 1371: 1369: 1365: 1364: 1362: 1361: 1356: 1351: 1346: 1341: 1336: 1331: 1325: 1323: 1317: 1316: 1305: 1304: 1297: 1290: 1282: 1276: 1275: 1270: 1258: 1257:External links 1255: 1254: 1253: 1250: 1246: 1239: 1232: 1223: 1220: 1217: 1216: 1207: 1158: 1091: 1024: 957: 890: 871:(1): 113–140. 855: 834:(3): 917–925. 814: 755: 696: 637: 588: 539: 490: 477:(6): 521–525. 457: 408: 359: 309: 308: 306: 303: 302: 301: 296: 291: 286: 284:Photosynthesis 279: 276: 251: 247: 243: 207:Main article: 204: 201: 156:in place of a 139:Main article: 136: 133: 116:Main article: 113: 110: 93:Main article: 90: 87: 72: 69: 33:photosynthesis 15: 9: 6: 4: 3: 2: 1710: 1699: 1696: 1694: 1691: 1690: 1688: 1673: 1670: 1668: 1665: 1663: 1660: 1658: 1655: 1653: 1650: 1648: 1647:F-box protein 1645: 1643: 1640: 1638: 1635: 1633: 1630: 1629: 1627: 1623: 1617: 1614: 1612: 1609: 1607: 1604: 1602: 1599: 1597: 1594: 1592: 1589: 1588: 1586: 1584: 1580: 1574: 1571: 1567: 1564: 1562: 1559: 1557: 1554: 1552: 1549: 1548: 1547: 1544: 1543: 1541: 1537: 1529: 1526: 1524: 1521: 1520: 1519: 1516: 1512: 1511:Ceruloplasmin 1509: 1508: 1507: 1504: 1500: 1497: 1495: 1492: 1491: 1490: 1487: 1486: 1484: 1482:Metal/element 1480: 1474: 1473:Transthyretin 1471: 1469: 1466: 1464: 1461: 1459: 1455: 1451: 1448: 1447: 1442: 1439: 1437: 1436:Neurophysin I 1434: 1433: 1432: 1429: 1425: 1422: 1420: 1417: 1415: 1412: 1410: 1407: 1405: 1402: 1400: 1397: 1395: 1392: 1391: 1390: 1387: 1385: 1382: 1380: 1376: 1373: 1372: 1370: 1366: 1360: 1357: 1355: 1352: 1350: 1347: 1345: 1342: 1340: 1337: 1335: 1332: 1330: 1327: 1326: 1324: 1322: 1318: 1314: 1310: 1303: 1298: 1296: 1291: 1289: 1284: 1283: 1280: 1274: 1271: 1268: 1264: 1261: 1260: 1251: 1247: 1245:428: 287–292. 1244: 1240: 1237: 1233: 1231:28: 3052–3063 1230: 1226: 1225: 1211: 1203: 1199: 1194: 1189: 1185: 1181: 1177: 1173: 1172:EXCLI Journal 1169: 1162: 1154: 1150: 1145: 1140: 1136: 1132: 1127: 1122: 1118: 1114: 1110: 1106: 1102: 1095: 1087: 1083: 1078: 1073: 1069: 1065: 1060: 1055: 1051: 1047: 1043: 1039: 1035: 1028: 1020: 1016: 1011: 1006: 1002: 998: 993: 988: 984: 980: 976: 972: 968: 961: 953: 949: 944: 939: 935: 931: 926: 921: 917: 913: 909: 905: 901: 894: 886: 882: 878: 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1368:Hormone 1249:175-184 1193:4553884 1153:9600895 1113:Bibcode 1086:9600895 1046:Bibcode 1019:9600895 979:Bibcode 952:9600895 912:Bibcode 885:1460542 850:1577009 800:6988754 741:6988754 682:6988754 623:3899860 574:3899860 525:3899860 443:3899860 394:3899860 345:3899860 190:flowers 61:pigment 1506:copper 1424:IGFBP7 1419:IGFBP6 1414:IGFBP5 1409:IGFBP4 1404:IGFBP3 1399:IGFBP2 1394:IGFBP1 1269:(MeSH) 1243:Nature 1200:  1190:  1151:  1141:  1133:  1084:  1074:  1066:  1017:  1007:  999:  950:  940:  932:  883:  848:  807:  797:  789:  748:  738:  730:  689:  679:  671:  630:  620:  581:  571:  532:  522:  450:  440:  401:  391:  352:  342:  229:, and 197:oxygen 186:fruits 78:photon 37:plants 1625:Other 1359:FABP7 1354:FABP6 1349:FABP5 1344:FABP4 1339:FABP3 1334:FABP2 1329:FABP1 1144:34498 1077:34498 1010:34498 943:34498 164:with 162:light 1518:iron 1198:PMID 1149:PMID 1131:ISSN 1082:PMID 1064:ISSN 1015:PMID 997:ISSN 948:PMID 930:ISSN 881:PMID 846:PMID 805:PMID 787:ISSN 746:PMID 728:ISSN 687:PMID 669:ISSN 628:PMID 579:PMID 530:PMID 448:PMID 399:PMID 350:PMID 265:and 238:and 188:and 180:and 148:and 104:use 39:and 1188:PMC 1180:doi 1139:PMC 1121:doi 1072:PMC 1054:doi 1005:PMC 987:doi 938:PMC 920:doi 873:doi 836:doi 832:205 795:PMC 777:doi 736:PMC 718:doi 677:PMC 659:doi 618:PMC 610:doi 569:PMC 561:doi 520:PMC 512:doi 479:doi 438:PMC 430:doi 389:PMC 381:doi 340:PMC 332:doi 1689:: 1452:: 1441:II 1377:: 1311:: 1196:. 1186:. 1176:14 1174:. 1170:. 1147:. 1137:. 1129:. 1119:. 1109:95 1107:. 1103:. 1080:. 1070:. 1062:. 1052:. 1042:95 1040:. 1036:. 1013:. 1003:. 995:. 985:. 975:95 973:. 969:. 946:. 936:. 928:. 918:. 908:95 906:. 902:. 879:. 869:15 867:. 844:. 830:. 826:. 803:. 793:. 785:. 773:10 771:. 767:. 744:. 734:. 726:. 714:10 712:. 708:. 685:. 675:. 667:. 655:10 653:. 649:. 626:. 616:. 606:11 604:. 600:. 577:. 567:. 557:11 555:. 551:. 528:. 518:. 508:11 506:. 502:. 473:. 469:. 446:. 436:. 426:11 424:. 420:. 397:. 387:. 377:11 375:. 371:. 348:. 338:. 328:11 326:. 322:. 225:, 192:. 67:. 19:A 1566:4 1561:3 1556:2 1551:1 1456:/ 1301:e 1294:t 1287:v 1238:. 1204:. 1182:: 1155:. 1123:: 1115:: 1088:. 1056:: 1048:: 1021:. 989:: 981:: 954:. 922:: 914:: 887:. 875:: 852:. 838:: 811:. 779:: 752:. 720:: 693:. 661:: 634:. 612:: 585:. 563:: 536:. 514:: 487:. 481:: 475:3 454:. 432:: 405:. 383:: 356:. 334:: 252:2 250:) 248:3 246:β 244:3

Index

subunit proteins
photosystem
photosynthesis
plants
photosynthetic bacteria
photosynthetic reaction center
photosynthetic pigments
photosynthetic reaction center
pigment
Förster resonance energy transfer
photon
resonance energy transfer
Bacterial antenna complex
Purple bacteria
bacteriochlorophyll
Chlorosome
Green sulphur bacteria
Chloroflexia
Light-harvesting complexes of green plants
Chlorophylls
carotenoids
formyl group
methyl group
light
wavelengths
organic molecules
polyenes
lycopene
β-carotene
fruits

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