20:
229:. Complex III itself is composed of several subunits, one of which is a b-type cytochrome while another one is a c-type cytochrome. Both domains are involved in electron transfer within the complex. Complex IV contains a cytochrome a/a3-domain that transfers electrons and catalyzes the reaction of
923:
140:(550 nm). The ultra-violet (UV) to visible spectroscopic signatures of hemes are still used to identify heme type from the reduced bis-pyridine-ligated state, i.e., the pyridine hemochrome method. Within each class, cytochrome
193:
to be very mobile) surrounding an iron ion. The iron in cytochromes usually exists in a ferrous (Fe) and a ferric (Fe) state with a ferroxo (Fe) state found in catalytic intermediates. Cytochromes are, thus, capable of performing
927:
70:
964:
Murshudov, G.; Grebenko, A.; Barynin, V.; Dauter, Z.; Wilson, K.; Vainshtein, B.; Melik-Adamyan, W.; Bravo, J.; Ferrán, J.; Ferrer, J. C.; Switala, J.; Loewen, P. C.; Fita, I. (1996).
100:(Fe(III)) oxidation state of the iron found in the heme core. In addition to the classification by the IUBMB into four cytochrome classes, several additional classifications such as
124:
rediscovered these respiratory pigments and named them the cytochromes, or “cellular pigments”. He classified these heme proteins on the basis of the position of their lowest
1846:
594:
268:
hypothesis. The apparently constant evolution rate of cytochromes can be a helpful tool in trying to determine when various organisms may have diverged from a
457:
222:
1165:
510:"Nomenclature Committee of the International Union of Biochemistry (NC-IUB). Nomenclature of electron-transfer proteins. Recommendations 1989"
1077:
246:
125:
924:"Investigation of biological oxidation, oxidative phosphorylation and ATP synthesis. Inhibitor and Uncouplers of oxidative phosphorylation"
435:
570:
1110:
202:
by reduction or oxidation of their heme iron. The cellular location of cytochromes depends on their function. They can be found as
1128:
1158:
238:
214:
117:
1233:
1137:
951:
195:
55:
1070:
The brain's way of healing : remarkable discoveries and recoveries from the frontiers of neuroplasticity
1311:
1292:
1255:
380:
51:
361:
1151:
1866:
1436:
1422:
1408:
1394:
815:
731:
621:
409:
226:
101:
1702:
1672:
1596:
1238:
325:
257:
78:
473:
formed by absorbance of light at wavelengths near 450 nm when the heme iron is reduced (with
1686:
1368:
1050:
902:
700:
692:
588:
261:
1093:
Miller, Walter L.; Gucev, Zoran S. (2014), "Disorders in the
Initial Steps in Steroidogenesis",
1667:
1562:
1106:
1073:
1042:
1034:
999:
947:
894:
886:
851:
833:
784:
749:
657:
639:
576:
566:
539:
531:
474:
1572:
1531:
1461:
1143:
1098:
1026:
989:
878:
841:
823:
776:
739:
684:
647:
629:
521:
207:
203:
1826:
1681:
482:
478:
466:
265:
234:
105:
1030:
819:
735:
625:
1728:
1723:
1133:
1102:
486:
269:
242:
170:, with more recent examples designated by their reduced state R-band maximum, e.g. cyt
846:
803:
526:
1860:
1833:
1792:
1707:
1514:
1296:
1279:
1218:
704:
652:
609:
559:
426:
372:
334:
284:, exact structure of the heme group, inhibitor sensitivity, and reduction potential.
66:
1054:
906:
1821:
1762:
1638:
1624:
1610:
1500:
1475:
720:"On cytochrome, a respiratory pigment, common to animals, yeast, and higher plants"
451:
413:
357:
342:
313:
301:
281:
250:
218:
121:
82:
74:
1769:
1182:
376:
808:
Proceedings of the
National Academy of Sciences of the United States of America
1774:
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1200:
470:
1038:
890:
837:
753:
643:
535:
1757:
994:
965:
675:
Mac Munn, C. A. (1886). "Researches on
Myohaematin and the Histohaematins".
634:
580:
199:
62:
1046:
898:
855:
788:
744:
719:
688:
1003:
828:
661:
543:
19:
190:
767:
Reedy, C. J.; Gibney, B. R. (February 2004). "Heme protein assemblies".
287:
Four types of cytochromes are distinguished by their prosthetic groups:
1174:
509:
93:
39:
780:
696:
1191:
869:
Kumar, Sudhir (2005). "Molecular clocks: four decades of evolution".
347:
330:
318:
306:
230:
97:
882:
120:
as respiratory pigments (myohematin or histohematin). In the 1920s,
16:
Redox-active proteins containing a heme with a Fe atom as a cofactor
1243:
1017:
Bendall, Derek S. (2004). "The
Unfinished Story of Cytochrome f".
89:
59:
1352:
1340:
1335:
1267:
1178:
186:
47:
43:
1147:
1582:
1323:
412:("Complex IV") with electrons delivered to complex by soluble
280:
Several kinds of cytochrome exist and can be distinguished by
221:
is involved in the electron transfer from the membrane-bound
65:. They are classified according to the type of heme and its
189:
group is a highly conjugated ring system (which allows its
677:
152:, early cytochromes are numbered consecutively, e.g. cyt
71:
610:"The heme groups of cytochrome o from Escherichia coli"
1809:
1783:
1748:
1741:
1716:
1695:
1660:
1553:
1493:
1454:
1387:
1376:
1367:
1290:
1215:
1208:
1199:
1190:
558:
804:"Primary Structure and Evolution of Cytochrome C"
116:Cytochromes were initially described in 1884 by
88:Cytochrome function is linked to the reversible
614:Proceedings of the National Academy of Sciences
1159:
8:
593:: CS1 maint: multiple names: authors list (
565:(3rd ed.). New York: Worth Publishers.
1745:
1384:
1373:
1212:
1205:
1196:
1166:
1152:
1144:
608:Puustinen, A.; Wikström, M. (1991-07-15).
481:. These enzymes are primarily involved in
379:, these cytochromes are often combined in
1847:disorders of globin and globulin proteins
1136:at the U.S. National Library of Medicine
993:
950:at the U.S. National Library of Medicine
845:
827:
743:
651:
633:
525:
469:family, so named for the characteristic
465:A distinct family of cytochromes is the
385:
289:
108:can be found in biochemical literature.
18:
498:
128:in their reduced state, as cytochromes
69:. Four varieties are recognized by the
586:
7:
918:
916:
561:Lehninger Principles of Biochemistry
504:
502:
233:to water. Photosystem II, the first
1129:Scripps Database of Metalloproteins
982:The Journal of Biological Chemistry
458:Plastoquinol—plastocyanin reductase
436:Coenzyme Q - cytochrome c reductase
245:, contains a cytochrome b subunit.
1103:10.1016/b978-0-12-416006-4.00011-9
1031:10.1023/b:pres.0000030454.23940.f9
368:of plants is a c-type cytochrome.
14:
383:and related metabolic pathways:
356:There is no "cytochrome e," but
260:of cytochromes was suggested by
514:Journal of Biological Chemistry
1097:, Elsevier, pp. 145–164,
1072:. Penguin Group. p. 173.
557:L., Lehninger, Albert (2000).
1:
527:10.1016/S0021-9258(18)48544-4
350:(Heme B with γ-spirolactone)
256:In the early 1960s, a linear
253:, is a cytochrome b protein.
50:(Fe) atom at its core, as a
196:electron transfer reactions
54:. They are involved in the
1883:
520:(1): 665–677. 1992-01-05.
1842:
1095:Genetic Steroid Disorders
718:Keilin, D. (1925-08-01).
239:light-dependent reactions
215:oxidative phosphorylation
118:Charles Alexander MacMunn
1138:Medical Subject Headings
952:Medical Subject Headings
871:Nature Reviews. Genetics
249:, an enzyme involved in
73:(IUBMB), cytochromes a,
56:electron transport chain
1068:Doidge, Norman (2015).
1019:Photosynthesis Research
995:10.1074/jbc.271.15.8863
966:"Structure of the heme
802:Margoliash, E. (1963).
635:10.1073/pnas.88.14.6122
745:10.1098/rspb.1925.0039
689:10.1098/rstl.1886.0007
181:Structure and function
126:energy absorption band
32:
829:10.1073/pnas.50.4.672
724:Proc. R. Soc. Lond. B
219:cytochrome cc protein
22:
410:Cytochrome c oxidase
136:(≈565 nm), and
1703:Glycated hemoglobin
1673:Carbaminohemoglobin
820:1963PNAS...50..672M
736:1925RSPSB..98..312K
626:1991PNAS...88.6122P
477:) and complexed to
972:Penicillium vitale
948:Cytochrome+c+Group
381:electron transport
262:Emanuel Margoliash
213:In the process of
33:
1854:
1853:
1805:
1804:
1801:
1800:
1737:
1736:
1668:Carboxyhemoglobin
1656:
1655:
1549:
1548:
1363:
1362:
1079:978-0-698-19143-3
988:(15): 8863–8868.
781:10.1021/cr0206115
620:(14): 6122–6126.
475:sodium dithionite
463:
462:
416:(hence the name)
354:
353:
296:Prosthetic group
208:membrane proteins
204:globular proteins
46:, with a central
38:are redox-active
1874:
1746:
1385:
1374:
1213:
1206:
1197:
1168:
1161:
1154:
1145:
1116:
1115:
1090:
1084:
1083:
1065:
1059:
1058:
1025:(1–3): 265–276.
1014:
1008:
1007:
997:
976:Escherichia coli
961:
955:
945:
939:
938:
936:
935:
926:. Archived from
920:
911:
910:
866:
860:
859:
849:
831:
799:
793:
792:
764:
758:
757:
747:
730:(690): 312–339.
715:
709:
708:
672:
666:
665:
655:
637:
605:
599:
598:
592:
584:
564:
554:
548:
547:
529:
506:
438:("Complex III")
386:
335:covalently bound
290:
264:that led to the
247:Cyclooxygenase 2
96:(Fe(II)) to the
1882:
1881:
1877:
1876:
1875:
1873:
1872:
1871:
1857:
1856:
1855:
1850:
1838:
1827:Cytochrome P450
1797:
1779:
1733:
1712:
1691:
1682:Deoxyhemoglobin
1652:
1648:
1644:
1634:
1630:
1620:
1616:
1606:
1602:
1592:
1588:
1578:
1568:
1545:
1541:
1537:
1527:
1523:
1518:
1510:
1506:
1489:
1485:
1481:
1471:
1467:
1450:
1446:
1442:
1437:HbE Portland II
1432:
1428:
1418:
1414:
1404:
1400:
1379:
1359:
1286:
1217:Alpha locus on
1186:
1172:
1125:
1120:
1119:
1113:
1092:
1091:
1087:
1080:
1067:
1066:
1062:
1016:
1015:
1011:
963:
962:
958:
946:
942:
933:
931:
922:
921:
914:
883:10.1038/nrg1659
868:
867:
863:
801:
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796:
766:
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761:
717:
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674:
673:
669:
607:
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602:
585:
573:
556:
555:
551:
508:
507:
500:
495:
483:steroidogenesis
479:carbon monoxide
467:cytochrome P450
447:
430:
405:
365:
360:, found in the
278:
270:common ancestor
266:molecular clock
235:protein complex
183:
175:
168:
161:
132:(605 nm),
114:
106:cytochrome P450
67:mode of binding
17:
12:
11:
5:
1880:
1878:
1870:
1869:
1859:
1858:
1852:
1851:
1843:
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1839:
1837:
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1824:
1813:
1811:
1807:
1806:
1803:
1802:
1799:
1798:
1796:
1795:
1789:
1787:
1781:
1780:
1778:
1777:
1772:
1767:
1766:
1765:
1754:
1752:
1743:
1739:
1738:
1735:
1734:
1732:
1731:
1729:Erythrocruorin
1726:
1720:
1718:
1714:
1713:
1711:
1710:
1705:
1699:
1697:
1693:
1692:
1690:
1689:
1687:Sulfhemoglobin
1684:
1675:
1670:
1664:
1662:
1658:
1657:
1654:
1653:
1651:
1650:
1646:
1642:
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1559:
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1516:
1512:
1508:
1504:
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1469:
1465:
1458:
1456:
1452:
1451:
1449:
1448:
1444:
1440:
1434:
1430:
1426:
1423:HbE Portland I
1420:
1416:
1412:
1406:
1402:
1398:
1391:
1389:
1382:
1371:
1365:
1364:
1361:
1360:
1358:
1357:
1356:
1355:
1345:
1344:
1343:
1338:
1328:
1327:
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1316:
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1303:
1301:
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1283:
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1272:
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1260:
1259:
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1203:
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1123:External links
1121:
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877:(8): 654–662.
861:
814:(4): 672–679.
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572:978-1572591530
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487:detoxification
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2:
1879:
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1835:
1834:Methemalbumin
1832:
1828:
1825:
1823:
1820:
1819:
1818:
1815:
1814:
1812:
1808:
1794:
1793:Leghemoglobin
1791:
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1776:
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1759:
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1740:
1730:
1727:
1725:
1724:Chlorocruorin
1722:
1721:
1719:
1715:
1709:
1708:Methemoglobin
1706:
1704:
1701:
1700:
1698:
1694:
1688:
1685:
1683:
1679:
1678:Oxyhemoglobin
1676:
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1177:that contain
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987:
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930:on 2020-06-28
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775:(2): 617–49.
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80:
79:cytochromes c
76:
75:cytochromes b
72:
68:
64:
61:
57:
53:
49:
45:
42:containing a
41:
37:
30:
26:
21:
1844:
1822:Cytochrome b
1816:
1784:
1763:Metmyoglobin
1749:
1554:
1380:development:
1377:
1347:
1330:
1318:
1306:
1291:
1274:
1262:
1250:
1228:
1216:
1183:hemoproteins
1094:
1088:
1069:
1063:
1022:
1018:
1012:
985:
981:
975:
971:
967:
959:
943:
932:. Retrieved
928:the original
874:
870:
864:
811:
807:
797:
772:
768:
762:
727:
723:
713:
680:
676:
670:
617:
613:
603:
560:
552:
517:
513:
464:
450:
443:
425:
421:
414:cytochrome c
401:
397:
392:Combination
377:chloroplasts
373:mitochondria
370:
362:cytochrome b
358:cytochrome f
355:
343:Cytochrome d
326:Cytochrome c
314:Cytochrome b
302:Cytochrome a
286:
282:spectroscopy
279:
255:
251:inflammation
241:of oxygenic
212:
184:
171:
164:
157:
153:
149:
145:
141:
137:
133:
129:
115:
102:cytochrome o
92:change from
87:
83:cytochrome d
35:
34:
28:
24:
1867:Cytochromes
1770:Neuroglobin
1696:Other human
1409:HbE Gower 2
1395:HbE Gower 1
1134:Cytochromes
683:: 267–298.
389:Cytochromes
223:complex III
36:Cytochromes
23:Cytochrome
1817:Cytochrome
1775:Cytoglobin
1555:pathology:
1378:stages of
1293:Beta locus
1201:Hemoglobin
978:catalases"
934:2020-02-02
493:References
471:Soret peak
227:complex IV
163:, and cyt
27:with heme
1845:see also
1758:Myoglobin
1661:Compounds
1532:HbF/Fetal
1462:HbF/Fetal
1388:Embryonic
1369:Tetramers
1039:0166-8595
891:1471-0056
838:0027-8424
754:0950-1193
705:110335335
644:0027-8424
589:cite book
536:0021-9258
366:f complex
258:evolution
200:catalysis
191:electrons
63:catalysis
1861:Category
1717:Nonhuman
1209:Subunits
1175:Proteins
1055:16716904
1047:16328825
907:14261833
899:16136655
856:14077496
789:14871137
769:Chem Rev
581:42619569
337:heme b)
52:cofactor
40:proteins
1192:Globins
1004:8621527
954:(MeSH).
816:Bibcode
732:Bibcode
662:2068092
622:Bibcode
544:1309757
237:in the
112:History
94:ferrous
1785:plant:
1750:human:
1244:pseudo
1140:(MeSH)
1109:
1076:
1053:
1045:
1037:
1002:
905:
897:
889:
854:
847:221244
844:
836:
787:
752:
703:
697:109482
695:
660:
650:
642:
579:
569:
542:
534:
348:heme D
331:heme C
319:heme B
307:heme A
231:oxygen
156:, cyt
122:Keilin
98:ferric
1810:Other
1742:Other
1573:Barts
1494:Adult
1455:Fetal
1051:S2CID
903:S2CID
701:S2CID
693:JSTOR
653:52034
276:Types
148:, or
90:redox
60:redox
1353:HBE1
1341:HBG2
1336:HBG1
1268:HBQ1
1239:HBA2
1234:HBA1
1179:heme
1107:ISBN
1074:ISBN
1043:PMID
1035:ISSN
1000:PMID
974:and
895:PMID
887:ISSN
852:PMID
834:ISSN
785:PMID
750:ISSN
658:PMID
640:ISSN
595:link
577:OCLC
567:ISBN
540:PMID
532:ISSN
485:and
449:and
424:and
400:and
375:and
293:Type
206:and
198:and
187:heme
185:The
104:and
85:.
81:and
58:and
48:iron
44:heme
1639:HbO
1625:HbE
1611:HbC
1597:HbS
1583:HbD
1563:HbH
1515:HbA
1501:HbA
1476:HbA
1324:HBD
1312:HBB
1295:on
1280:HBM
1256:HBZ
1099:doi
1027:doi
990:doi
986:271
970:of
879:doi
842:PMC
824:doi
777:doi
773:104
740:doi
685:doi
681:177
648:PMC
630:doi
522:doi
518:267
371:In
225:to
174:559
1863::
1641:(α
1627:(α
1613:(α
1599:(α
1585:(α
1575:(γ
1565:(β
1534:(α
1520:(α
1503:(α
1478:(α
1464:(α
1439:(ζ
1425:(ζ
1411:(α
1397:(ζ
1297:11
1219:16
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1049:.
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591:}}
587:{{
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538:.
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516:.
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272:.
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1633:2
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1629:2
1621:)
1619:2
1617:β
1615:2
1607:)
1605:2
1603:β
1601:2
1593:)
1591:2
1589:β
1587:2
1579:)
1577:4
1569:)
1567:4
1542:)
1540:2
1538:γ
1536:2
1528:)
1526:2
1524:δ
1522:2
1517:2
1511:)
1509:2
1507:β
1505:2
1486:)
1484:2
1482:β
1480:2
1472:)
1470:2
1468:γ
1466:2
1447:)
1445:2
1443:β
1441:2
1433:)
1431:2
1429:γ
1427:2
1419:)
1417:2
1415:ε
1413:2
1405:)
1403:2
1401:ε
1399:2
1348:ε
1331:γ
1319:δ
1307:β
1299::
1275:μ
1263:θ
1251:ζ
1229:α
1221::
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1181:(
1167:e
1160:t
1153:v
1101::
1082:.
1057:.
1029::
1006:.
992::
968:d
937:.
909:.
881::
875:6
858:.
826::
818::
791:.
779::
756:.
742::
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707:.
687::
664:.
632::
624::
597:)
583:.
546:.
524::
452:f
446:6
444:b
429:1
427:c
422:b
404:3
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398:a
364:6
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172:c
167:2
165:c
160:1
158:c
154:c
150:c
146:b
142:a
138:c
134:b
130:a
31:.
29:c
25:c
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