1403:
679:). In this system, the N-terminal P450 domain is fused to the reductase domain that shows sequence similarity to phthalate dioxygenase reductase and consists, in its turn, of FMN-binding domain and C-terminal plant-type ferredoxin domain. Similar systems have been identified in the heavy-metal-tolerant bacterium
965:
McLean, K.J.; Sabri, M.; Marshall, K.R.; Lawson, R.J.; Lewis, D.G.; Clift, D.; Balding, P.R.; Dunford, A.J.; Warman, A.J.; McVey, J.P.; Quinn, A.-M.; Sutcliffe, M.J.; Scrutton, N.S.; Munro, A.W. (2005). "Biodiversity of cytochrome P450 redox systems".
869:) are examples of P450 enzymes that do not require a reductase or molecular oxygen for their catalytic activity. Substrates for all these enzymes are fatty acid derivatives containing partially reduced dioxygen (either hydroperoxy or epidioxy groups).
42:
chains, called P450-containing monooxygenase systems, although self-sufficient, non-monooxygenase P450s have been also described. All known P450-containing monooxygenase systems share common structural and functional
84:
transfer electrons between the flavin reductase (protein or domain) and P450. While P450-containing systems are found throughout all kingdoms of life, some organisms lack one or more of these redox domains.
417:, CPR is a C-terminal domain of CYP102, a single polypeptide self-sufficient soluble P450 system (P450 is an N-terminal domain). The general scheme of electron flow in the CPR/P450 system is:
1042:
McLean, K.J.; Warman, A.J.; Seward, H.E.; Marshall, K.R.; Girvan, H.M.; Cheesman, M.R.; Waterman, M.R.; Munro, A.W. (2006). "Biophysical characterization of the sterol demethylase P450 from
112:
and several membrane-bound P450s (CYP11A, CYP11B, CYP27). In bacteria, putidaredoxin, terpredoxin, and rhodocoxin serve as electron carriers between corresponding
746:
1263:
104:
ferredoxins (Fd) that act as single electron carriers between FAD-containing ferredoxin reductase (FR) and P450. In mitochondrial monooxygenase systems,
1155:
77:. These ubiquitous redox domains, in various combinations, are widely distributed in biological systems. FMN domain, ferredoxin or cytochrome
1083:"A self-sufficient cytochrome P450 with a primary structural organisation that includes a flavin domain and a [2Fe-2S] redox center"
1003:"Redundancy or flexibility: molecular diversity of the electron transfer components for P450 monooxygenases in higher plants"
922:
1348:
1148:
1241:
1081:
Roberts, G.A.; Γelik, A.; Hunter, D.J.B.; Ost, T.W.B.; White, J.H.; Chapman, S.K.; Turner, N.J.; Flitsch, S.L. (2003).
949:
134:
113:
1306:
17:
1311:
1283:
1256:
1234:
1219:
1184:
1141:
1128:
1229:
886:
Degtyarenko, K.N.; Kulikova, T.A. (2001). "Evolution of bioinorganic motifs in P450-containing systems".
52:
1393:
398:
P450 enzymes and some bacterial P450s receive electrons from a FAD- and FMN-containing enzyme known as
323:
825:
399:
267:
The general scheme of electron flow in the P450 systems containing adrenodoxin-type ferredoxins is:
1423:
1333:
863:
856:
849:
495:
403:
328:
1365:
1343:
1082:
803:
484:
472:
can serve as an effector (activator or inhibitor) of P450s. It was hypothesized that cytochrome
1328:
1224:
47:
architecture. Apart from the cytochrome itself, these systems contain one or more fundamental
318:
232:
109:
60:
8:
1380:
1370:
1338:
117:
1375:
759:
941:
1107:
1063:
1024:
983:
945:
903:
834:
811:
44:
39:
409:). Microsomal CPR is membrane-bound protein that interacts with different P450s. In
1097:
1055:
1014:
975:
937:
895:
1041:
845:) as an oxidant. These enzymes do not require any reduction system for catalysis.
1168:
1133:
750:
28:
1407:
1316:
1199:
1176:
1080:
964:
1417:
1211:
1194:
768:
93:
68:
1111:
1102:
1067:
1028:
987:
907:
764:
56:
1189:
855:), fatty acid hydroperoxide lyase (CYP74B), prostacyclin synthase (CYP8;
763:. This enzyme does not have monooxygenase activity but is able to reduce
240:
105:
866:
859:
852:
1301:
1278:
979:
899:
779:
695:
622:
505:
498:
421:
406:
395:
343:
271:
124:
64:
1059:
833:) catalyse the hydroxylation reaction of long-chain fatty acids using
38:
P450 enzymes usually function as a terminal oxidase in multicomponent
691:. The general scheme of electron flow in this system appears to be:
1402:
830:
816:
754:
684:
676:
1019:
1002:
248:
1273:
1268:
1164:
885:
1358:
1353:
753:
in several fungal species. The best-characterized P450nor is
671:
An unusual one-component P450 system was originally found in
48:
1251:
1246:
923:"Electron transfer proteins of cytochrome P450 systems"
595:
system to support P450 catalysis has been demonstrated
108:
functions as a soluble electron carrier between NADPH:
1391:
465:
The ubiquitous electron-transport protein cytochrome
1264:
Branched-chain alpha-keto acid dehydrogenase complex
1000:
116:-dependent ferredoxin reductases and soluble P450s (
1366:
Phosphoenolpyruvate sugar phosphotransferase system
1046:, its cognate ferredoxin, and their interactions".
618:the first and second electrons are donated by CBR.
1163:
96:and some bacterial P450 systems employ soluble Fe
1415:
1185:Photosynthetic reaction center complex proteins
1149:
920:
775:O) directly using NAD(P)H as electron donor:
1156:
1142:
932:. Advances in Molecular and Cell Biology.
483:electron to P450, either from CPR or from
327:contains flavoprotein reductase A (FprA),
1101:
1018:
14:
1416:
666:
460:
1137:
88:
1129:Directory of P450-containing Systems
741:
1349:Mitochondrial trifunctional protein
819:) and fatty acid Ξ±-hydroxylase P450
479:is involved in the transfer of the
389:
24:
862:) and thromboxane synthase (CYP5;
710:
599:using purified CBR and cytochrome
588:The ability of the CBR/cytochrome
358:
286:
31:protein or domain can be called a
25:
1435:
1122:
788:
723:
648:
637:
442:
371:
299:
1401:
747:Nitric oxide reductase (P450nor)
27:Any enzyme system that includes
1307:Carbamoyl phosphate synthase II
1001:Ohta, D.; Mizutani, M. (2004).
848:Allene oxide synthase (CYP74A;
1312:Aspartate carbamoyltransferase
1220:Pyruvate dehydrogenase complex
1074:
1035:
994:
958:
914:
879:
704:
631:
436:
430:
352:
280:
13:
1:
1344:Glycine decarboxylase complex
1339:Fatty acid synthetase complex
942:10.1016/S1569-2558(08)60339-2
872:
804:Fatty acid Ξ²-hydroxylase P450
749:is a P450 enzyme involved in
687:) and in several species of
7:
782:
698:
625:
546:
508:
424:
346:
274:
225:
193:
161:
127:
10:
1440:
1376:Sucrase-isomaltase complex
1242:Oxoglutarate dehydrogenase
1044:Mycobacterium tuberculosis
324:Mycobacterium tuberculosis
1294:
1210:
1175:
400:cytochrome P450 reductase
1334:Electron transport chain
826:Pseudomonas paucimobilis
608:Saccharomyces cerevisiae
1324:P450-containing systems
681:Ralstonia metallidurans
339:and CYP51 hemoprotein.
135:putidaredoxin reductase
1329:Cytochrome b6f complex
1103:10.1074/jbc.M309630200
921:Hanukoglu, I. (1996).
610:and CYP51 enzyme from
168:terpredoxin reductase
33:P450-containing system
1169:multienzyme complexes
233:adrenodoxin reductase
200:rhodocoxin reductase
110:adrenodoxin reductase
1381:Tryptophan synthase
1371:Polyketide synthase
1096:(49): 48914β48920.
968:Biochem. Soc. Trans
930:Adv. Mol. Cell Biol
888:Biochem. Soc. Trans
667:FMN/Fd/P450 systems
461:CBR/b5/P450 systems
411:Bacillus megaterium
120:, CYP108, CYP116).
1013:(1β3): 1587β1597.
980:10.1042/BST0330796
900:10.1042/BST0290139
760:Fusarium oxysporum
614:. In this system,
319:sterol demethylase
89:FR/Fd/P450 systems
1389:
1388:
1060:10.1021/bi0601609
1054:(27): 8427β8443.
835:hydrogen peroxide
812:Bacillus subtilis
799:
798:
742:P450-only systems
737:
736:
662:
661:
584:
583:
456:
455:
415:Bacillus subtilis
385:
384:
329:bacterial-type Fe
313:
312:
263:
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40:electron-transfer
16:(Redirected from
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912:
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883:
780:
696:
675:sp. NCIMB 9784 (
623:
612:Candida albicans
506:
485:NADH:cytochrome
422:
390:CPR/P450 systems
344:
272:
125:
21:
1439:
1438:
1434:
1433:
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1430:
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1424:Cytochrome P450
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751:denitrification
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29:cytochrome P450
23:
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18:Microsomal P450
15:
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1317:Dihydroorotase
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1177:Photosynthesis
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1138:
1132:
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1124:
1123:External links
1121:
1118:
1117:
1073:
1034:
993:
974:(4): 796β801.
957:
950:
913:
894:(2): 139β147.
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1212:Dehydrogenase
1209:
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1090:J. Biol. Chem
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1038:
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1021:
1016:
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1008:
1007:Front. Biosci
1004:
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989:
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951:9780762301133
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828:
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770:
769:nitrous oxide
767:(NO) to form
766:
762:
761:
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752:
748:
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94:Mitochondrial
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36:
34:
30:
19:
1323:
1093:
1089:
1076:
1051:
1048:Biochemistry
1047:
1043:
1037:
1020:10.2741/1356
1010:
1006:
996:
971:
967:
960:
933:
929:
916:
891:
887:
881:
847:
824:
810:
802:
765:nitric oxide
758:
745:
688:
680:
672:
670:
638:
615:
611:
607:
600:
596:
589:
587:
560:
522:
486:
480:
473:
466:
464:
414:
410:
393:
322:
321:system from
316:
266:
174:terpredoxin
92:
78:
70:
57:flavoprotein
55:-containing
37:
32:
26:
1190:Photosystem
689:Burkolderia
673:Rhodococcus
394:Eukaryotic
241:adrenodoxin
206:rhodocoxin
106:adrenodoxin
69:cytochrome
59:or domain,
873:References
396:microsomal
337:ferredoxin
65:ferredoxin
936:: 29β56.
492:reductase
51:domains:
1418:Category
1112:14514666
1068:16819841
1029:14977570
988:16042601
908:11356142
867:5.3.99.5
860:5.3.99.4
853:4.2.1.92
831:CYP152B1
817:CYP152A1
685:CYP116A1
677:CYP116B2
626:NAD(P)H
597:in vitro
63:domain,
1408:Biology
1165:Enzymes
783:NAD(P)H
755:CYP55A1
499:1.6.2.2
407:1.6.2.4
347:NAD(P)H
275:NAD(P)H
249:CYP11A1
212:CYP116
180:CYP108
148:CYP101
1394:Portal
1274:BCKDHB
1269:BCKDHA
1110:
1066:
1027:
986:
948:
906:
494:(CBR;
481:second
402:(CPR;
118:CYP101
45:domain
1359:HADHB
1354:HADHA
1295:Other
1086:(PDF)
926:(PDF)
823:from
809:from
789:P450
757:from
724:P450
649:P450
606:from
571:P450
533:P450
509:NADPH
443:P450
425:NADPH
372:P450
300:P450
226:NADPH
49:redox
1252:DLST
1247:OGDH
1108:PMID
1064:PMID
1025:PMID
984:PMID
946:ISBN
904:PMID
705:FMN
699:NADH
632:FAD
616:both
559:cyt
547:NADH
521:cyt
437:FMN
431:FAD
413:and
353:FAD
317:The
281:FAD
194:NADH
162:NADH
128:NADH
114:NADH
67:and
1302:CAD
1284:DLD
1279:DBT
1257:DLD
1098:doi
1094:278
1056:doi
1015:doi
976:doi
938:doi
896:doi
821:SPΞ±
806:BSΞ²
795:NO
553:CBR
515:CPR
501:):
61:FMN
53:FAD
1420::
1235:E3
1230:E2
1225:E1
1200:II
1167::
1106:.
1092:.
1088:.
1062:.
1052:45
1050:.
1023:.
1009:.
1005:.
982:.
972:33
970:.
944:.
934:14
928:.
902:.
892:29
890:.
864:EC
857:EC
850:EC
837:(H
786:β
771:(N
721:β
711:Fe
708:β
702:β
652:β
646:β
635:β
629:β
556:β
550:β
518:β
512:β
496:EC
440:β
434:β
428:β
404:EC
369:β
359:Fe
356:β
350:β
297:β
287:Fe
284:β
278:β
245:β
237:β
229:β
209:β
203:β
197:β
177:β
171:β
165:β
145:β
139:β
131:β
35:.
1396::
1195:I
1157:e
1150:t
1143:v
1114:.
1100::
1070:.
1058::
1031:.
1017::
1011:9
990:.
978::
954:.
940::
910:.
898::
843:2
841:O
839:2
829:(
815:(
792:β
773:2
732:2
730:O
727:β
717:2
715:S
713:2
683:(
657:2
655:O
642:5
639:b
604:5
601:b
593:5
590:b
579:2
577:O
574:β
568:β
564:5
561:b
541:2
539:O
536:β
530:β
526:5
523:b
490:5
487:b
477:5
474:b
470:5
467:b
451:2
449:O
446:β
380:2
378:O
375:β
365:4
363:S
361:3
335:4
333:S
331:3
308:2
306:O
303:β
293:2
291:S
289:2
258:2
256:O
253:β
220:2
218:O
215:β
188:2
186:O
183:β
156:2
154:O
151:β
102:2
100:S
98:2
82:5
79:b
74:5
71:b
20:)
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