26:
477:
are known. The fold belongs to the α+β class, with two hydrophobic cores on each side of a β-sheet. The larger hydrophobic core constitutes the heme-binding pocket, closed off on each side by a pair of helices connected by a turn. The smaller hydrophobic core may have only a structural role and is
308:
482:
residues provide the fifth and sixth heme ligands, and the propionate edge of the heme group lies at the opening of the heme crevice. Two isomers of cytochrome
79:
778:
Napier JA, Michaelson LV, Sayanova O (February 2003). "The role of cytochrome b5 fusion desaturases in the synthesis of polyunsaturated fatty acids".
811:(December 1992). "Gene synthesis, bacterial expression, and 1H NMR spectroscopic studies of the rat outer mitochondrial membrane cytochrome b5".
489:, referred to as the A (major) and B (minor) forms, differ by a 180° rotation of the heme about an axis defined by the α- and γ-meso carbons.
961:
589:
935:
550:
103:
91:
84:
328:
639:
718:
671:
633:
583:
540:
504:
442:
435:
428:
421:
414:
316:
727:
510:
31:
402:
itself) hemoprotein domains covalently associated with other redox domains in flavocytochrome cytochrome
96:
732:
161:
312:
966:
264:
350:
914:
895:
876:
857:
828:
795:
766:
385:
303:
115:
44:
849:
820:
787:
758:
156:
295:
369:
185:
165:
853:
791:
955:
808:
762:
233:
713:
377:
291:
269:
245:
132:
381:
353:
195:
139:
840:
Schenkman JB, Jansson I (February 2003). "The many roles of cytochrome b5".
479:
373:
39:
861:
799:
832:
770:
674:
636:
586:
240:
144:
824:
543:
507:
445:
438:
431:
424:
417:
257:
252:
25:
918:
899:
880:
478:
formed by spatially close N-terminal and C-terminal segments. The two
120:
48:
357:
323:
127:
365:
361:
749:
Lederer F (1994). "The cytochrome b5-fold: an adaptable module".
939:
807:
Rivera M, Barillas-Mury C, Christensen KA, Little JW, Wells MA,
285:
228:
108:
35:
380:
variants are membrane-bound, while bacterial and those from
780:
Prostaglandins, Leukotrienes, and
Essential Fatty Acids
942:– Methemoglobinemia due to deficiency of cytochrome
322:
302:
284:
279:
263:
251:
239:
227:
219:
214:
209:
191:
181:
176:
155:
150:
138:
126:
114:
102:
90:
78:
70:
62:
57:
18:
903: – Solution structure of rat cytochrome
884: – Solution structure of rat cytochrome
692:+ 2 H → γ-linolenoyl-CoA + 2 ferricytochrome
8:
395:-like proteins includes (besides cytochrome
388:are water-soluble. The family of cytochrome
618:-glycoloylneuraminate + 2 ferricytochrome
276:
173:
38:in black, iron in orange and iron-binding
24:
573:→ monodehydroascorbate + ferrocytochrome
463:3-D structures of a number of cytochrome
922: – X-ray structure of cytochrome
455:/acyl lipid desaturase fusion proteins.
427:), plant and fungal nitrate reductases (
656:+ 2 H → oleoyl-CoA + 2 ferricytochrome
603:-acetylneuraminate + 2 ferrocytochrome
206:
15:
7:
936:Online Mendelian Inheritance in Man
448:), and plant and fungal cytochrome
681:linoleoyl-CoA + 2 ferrocytochrome
14:
645:stearoyl-CoA + 2 ferrocytochrome
30:Cytochrome B5 (rat) bound to its
594:-acetylneuraminate monooxygenase
842:Pharmacology & Therapeutics
1:
854:10.1016/S0163-7258(02)00327-3
792:10.1016/S0952-3278(02)00263-6
566:-ascorbate + ferricytochrome
523:NADH + H + 2 ferricytochrome
500:in some biochemical reactions
280:Available protein structures:
962:Genes on human chromosome 18
931:Ectothiorhodospira vacuolata
763:10.1016/0300-9084(94)90144-9
370:purple phototrophic bacteria
677:linoleoyl-CoA 9-desaturase
42:residues shown as sticks. (
983:
530:→ NAD + 2 ferrocytochrome
470:and yeast flavocytochrome
640:stearoyl-CoA 9-desaturase
275:
172:
23:
413:-lactate dehydrogenase;
728:P450-containing systems
551:ascorbate—cytochrome-
420:), sulfite oxidase (
825:10.1021/bi00163a037
351:electron transport
565:
548:
412:
338:
337:
334:
333:
329:structure summary
205:
204:
201:
200:
974:
921:
902:
883:
865:
836:
819:(48): 12233–40.
803:
774:
563:
546:
410:
277:
207:
174:
51:
28:
16:
982:
981:
977:
976:
975:
973:
972:
971:
952:
951:
948:
928:
913:
909:
894:
890:
875:
872:
839:
806:
777:
748:
745:
736:
722:
710:
702:
698:
691:
687:
666:
662:
655:
651:
628:
624:
613:
609:
579:
572:
557:
536:
529:
517:
502:
499:
488:
476:
469:
461:
454:
408:
401:
394:
349:are ubiquitous
347:
53:
43:
12:
11:
5:
980:
978:
970:
969:
964:
954:
953:
950:
949:
946:
933:
926:
911:
907:
892:
888:
871:
870:External links
868:
867:
866:
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775:
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460:
457:
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406:
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386:animal tissues
345:
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273:
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29:
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10:
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6:
4:
3:
2:
979:
968:
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937:
934:
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920:
916:
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901:
897:
893:
887:
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878:
874:
873:
869:
863:
859:
855:
851:
848:(2): 139–52.
847:
843:
838:
834:
830:
826:
822:
818:
814:
810:
805:
801:
797:
793:
789:
786:(2): 135–43.
785:
781:
776:
772:
768:
764:
760:
757:(7): 674–92.
756:
752:
747:
746:
742:
738:
731:
729:
726:
724:
717:
715:
712:
711:
707:
695:
684:
680:
679:
678:
676:
673:
659:
648:
644:
643:
642:
641:
638:
635:
621:
617:
606:
602:
598:
597:
596:
595:
593:
588:
585:
576:
569:
562:
561:
560:
559:
554:
545:
542:
533:
526:
522:
521:
520:
519:
514:
509:
506:
496:
492:
490:
485:
481:
473:
466:
458:
456:
451:
447:
444:
440:
437:
433:
430:
426:
423:
419:
416:
405:
398:
391:
387:
383:
379:
378:mitochondrial
375:
371:
367:
363:
359:
355:
352:
348:
344:
330:
327:
325:
321:
318:
314:
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307:
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297:
293:
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287:
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278:
274:
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259:
256:
254:
250:
247:
244:
242:
238:
235:
232:
230:
226:
222:
218:
213:
210:Cytochrome b5
208:
197:
194:
190:
187:
184:
180:
175:
171:
168:
167:
163:
160:
158:
154:
149:
146:
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137:
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131:
129:
125:
122:
119:
117:
113:
110:
107:
105:
101:
98:
95:
93:
89:
86:
83:
81:
77:
73:
69:
65:
61:
56:
50:
46:
41:
37:
33:
27:
22:
19:Cytochrome b5
17:
943:
930:
923:
904:
885:
845:
841:
816:
813:Biochemistry
812:
783:
779:
754:
750:
733:Cytochrome b
719:Cytochrome b
714:Cytochrome b
693:
682:
670:
657:
646:
632:
619:
615:
614:+ 2 H → CMP-
604:
600:
591:
582:
574:
567:
552:
539:
531:
524:
512:
503:
494:
483:
471:
464:
462:
449:
403:
396:
389:
382:erythrocytes
354:hemoproteins
342:
341:Cytochromes
340:
339:
164:
71:Alt. symbols
967:Cytochromes
511:cytochrome-
493:Cytochrome
215:Identifiers
186:Swiss-model
58:Identifiers
956:Categories
743:References
723:deficiency
384:and other
374:microsomal
292:structures
265:Membranome
182:Structures
177:Search for
151:Other data
809:Walker FA
751:Biochimie
675:1.14.19.3
637:1.14.19.1
587:1.14.18.2
558:reductase
518:reductase
480:histidine
459:Structure
356:found in
258:PDOC00170
246:IPR001199
133:NM_001914
80:NCBI gene
40:histidine
938:(OMIM):
910:(form B)
891:(form A)
862:12559387
800:12538077
737:, type A
708:See also
544:1.10.2.1
309:RCSB PDB
241:InterPro
196:InterPro
52:)
32:cofactor
833:1333795
771:7893819
508:1.6.2.2
446:1.7.1.3
439:1.7.1.2
432:1.7.1.1
425:1.8.3.1
418:1.1.2.3
358:animals
253:PROSITE
234:PF00173
192:Domains
162:Chr. 18
140:UniProt
940:250790
860:
831:
798:
769:
372:. The
362:plants
324:PDBsum
298:
288:
223:Cyt_B5
220:Symbol
145:P00167
128:RefSeq
109:250790
63:Symbol
929:from
366:fungi
157:Locus
66:CYB5A
919:1CXY
900:1B5B
881:1B5A
858:PMID
829:PMID
796:PMID
767:PMID
599:CMP-
590:CMP-
376:and
368:and
317:PDBj
313:PDBe
296:ECOD
286:Pfam
229:Pfam
121:1JEX
104:OMIM
97:2570
92:HGNC
85:1528
74:CYB5
49:1ICC
36:Haem
927:558
915:PDB
896:PDB
877:PDB
850:doi
821:doi
788:doi
759:doi
699:+ H
688:+ O
663:+ H
652:+ O
625:+ H
610:+ O
304:PDB
270:211
166:q23
116:PDB
45:PDB
958::
917::
898::
879::
856:.
846:97
844:.
827:.
817:31
815:.
794:.
784:68
782:.
765:.
755:76
753:.
672:EC
634:EC
584:EC
541:EC
505:EC
443:EC
441:,
436:EC
434:,
429:EC
422:EC
415:EC
364:,
360:,
315:;
311:;
294:/
47::
34:.
947:5
944:b
924:b
908:5
905:b
889:5
886:b
864:.
852::
835:.
823::
802:.
790::
773:.
761::
735:5
721:5
703:O
701:2
697:5
694:b
690:2
686:5
683:b
667:O
665:2
661:5
658:b
654:2
650:5
647:b
629:O
627:2
623:5
620:b
616:N
612:2
608:5
605:b
601:N
592:N
578:5
575:b
571:5
568:b
564:L
556:5
553:b
549:-
547:L
535:5
532:b
528:5
525:b
516:5
513:b
498:5
495:b
487:5
484:b
475:2
472:b
468:5
465:b
453:5
450:b
411:L
409:(
407:2
404:b
400:5
397:b
393:5
390:b
346:5
343:b
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