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P450-containing systems

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1392: 668:). 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 954:
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".
858:) 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). 31:
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
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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.
406:, 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: 1031:
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
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and several membrane-bound P450s (CYP11A, CYP11B, CYP27). In bacteria, putidaredoxin, terpredoxin, and rhodocoxin serve as electron carriers between corresponding
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ferredoxins (Fd) that act as single electron carriers between FAD-containing ferredoxin reductase (FR) and P450. In mitochondrial monooxygenase systems,
66:. These ubiquitous redox domains, in various combinations, are widely distributed in biological systems. FMN domain, ferredoxin or cytochrome 1072:"A self-sufficient cytochrome P450 with a primary structural organisation that includes a flavin domain and a [2Fe-2S] redox center" 1337: 1137: 1230: 123: 938: 102: 1295: 1300: 1272: 1245: 1223: 1208: 1173: 1130: 992:"Redundancy or flexibility: molecular diversity of the electron transfer components for P450 monooxygenases in higher plants" 911: 1382: 1218: 1070:
Roberts, G.A.; Γ‡elik, A.; Hunter, D.J.B.; Ost, T.W.B.; White, J.H.; Chapman, S.K.; Turner, N.J.; Flitsch, S.L. (2003).
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Degtyarenko, K.N.; Kulikova, T.A. (2001). "Evolution of bioinorganic motifs in P450-containing systems".
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P450 enzymes and some bacterial P450s receive electrons from a FAD- and FMN-containing enzyme known as
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The general scheme of electron flow in the P450 systems containing adrenodoxin-type ferredoxins is:
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can serve as an effector (activator or inhibitor) of P450s. It was hypothesized that cytochrome
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architecture. Apart from the cytochrome itself, these systems contain one or more fundamental
33: 28: 1086: 1044: 1003: 964: 926: 884: 1157: 739: 17: 1396: 1305: 1188: 1165: 930: 1406: 1200: 1183: 757: 82: 57: 398:). Microsomal CPR is membrane-bound protein that interacts with different P450s. In 753: 45: 834:) as an oxidant. These enzymes do not require any reduction system for catalysis. 1122: 1178: 229: 94: 1391: 1290: 1267: 384: 317: 53: 1100: 1091: 1056: 1017: 976: 896: 844:), fatty acid hydroperoxide lyase (CYP74B), prostacyclin synthase (CYP8; 752:. This enzyme does not have monooxygenase activity but is able to reduce 855: 848: 841: 968: 888: 768: 684: 611: 494: 487: 410: 395: 332: 260: 237: 113: 1048: 822:) catalyse the hydroxylation reaction of long-chain fatty acids using 27:
P450 enzymes usually function as a terminal oxidase in multicomponent
1262: 1257: 1153: 680:. The general scheme of electron flow in this system appears to be: 1347: 1342: 819: 805: 743: 673: 665: 37: 1008: 991: 1240: 1235: 1126: 742:
in several fungal species. The best-characterized P450nor is
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An unusual one-component P450 system was originally found in
912:"Electron transfer proteins of cytochrome P450 systems" 584:
system to support P450 catalysis has been demonstrated
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functions as a soluble electron carrier between NADPH:
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The ubiquitous electron-transport protein cytochrome
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Branched-chain alpha-keto acid dehydrogenase complex
105:-dependent ferredoxin reductases and soluble P450s ( 1355:
Phosphoenolpyruvate sugar phosphotransferase system
1283: 1199: 1164: 1035:, its cognate ferredoxin, and their interactions". 607:the first and second electrons are donated by CBR. 85:and some bacterial P450 systems employ soluble Fe 1174:Photosynthetic reaction center complex proteins 1138: 764:O) directly using NAD(P)H as electron donor: 8: 1145: 1131: 1123: 921:. Advances in Molecular and Cell Biology. 472:electron to P450, either from CPR or from 316:contains flavoprotein reductase A (FprA), 1090: 1007: 1387: 867: 7: 1118:Directory of P450-containing Systems 1338:Mitochondrial trifunctional protein 808:) and fatty acid Ξ±-hydroxylase P450 468:is involved in the transfer of the 851:) and thromboxane synthase (CYP5; 699: 588:using purified CBR and cytochrome 577:The ability of the CBR/cytochrome 347: 275: 20:protein or domain can be called a 14: 777: 712: 637: 626: 431: 360: 288: 1390: 736:Nitric oxide reductase (P450nor) 16:Any enzyme system that includes 1296:Carbamoyl phosphate synthase II 990:Ohta, D.; Mizutani, M. (2004). 837:Allene oxide synthase (CYP74A; 1301:Aspartate carbamoyltransferase 1209:Pyruvate dehydrogenase complex 693: 620: 425: 419: 341: 269: 1: 1333:Glycine decarboxylase complex 1328:Fatty acid synthetase complex 931:10.1016/S1569-2558(08)60339-2 793:Fatty acid Ξ²-hydroxylase P450 738:is a P450 enzyme involved in 676:) and in several species of 771: 687: 614: 535: 497: 413: 335: 263: 214: 182: 150: 116: 1429: 1365:Sucrase-isomaltase complex 1231:Oxoglutarate dehydrogenase 1033:Mycobacterium tuberculosis 313:Mycobacterium tuberculosis 389:cytochrome P450 reductase 1323:Electron transport chain 815:Pseudomonas paucimobilis 597:Saccharomyces cerevisiae 1313:P450-containing systems 670:Ralstonia metallidurans 328:and CYP51 hemoprotein. 124:putidaredoxin reductase 1318:Cytochrome b6f complex 1092:10.1074/jbc.M309630200 910:Hanukoglu, I. (1996). 599:and CYP51 enzyme from 157:terpredoxin reductase 22:P450-containing system 1158:multienzyme complexes 222:adrenodoxin reductase 189:rhodocoxin reductase 99:adrenodoxin reductase 1370:Tryptophan synthase 1360:Polyketide synthase 1085:(49): 48914–48920. 957:Biochem. Soc. Trans 919:Adv. Mol. Cell Biol 877:Biochem. Soc. Trans 656:FMN/Fd/P450 systems 450:CBR/b5/P450 systems 400:Bacillus megaterium 109:, CYP108, CYP116). 1002:(1–3): 1587–1597. 969:10.1042/BST0330796 889:10.1042/BST0290139 749:Fusarium oxysporum 603:. In this system, 308:sterol demethylase 78:FR/Fd/P450 systems 1378: 1377: 1049:10.1021/bi0601609 1043:(27): 8427–8443. 824:hydrogen peroxide 801:Bacillus subtilis 788: 787: 731:P450-only systems 726: 725: 651: 650: 573: 572: 445: 444: 404:Bacillus subtilis 374: 373: 318:bacterial-type Fe 302: 301: 252: 251: 29:electron-transfer 1420: 1395: 1394: 1386: 1147: 1140: 1133: 1124: 1105: 1104: 1094: 1076: 1067: 1061: 1060: 1028: 1022: 1021: 1011: 987: 981: 980: 951: 945: 944: 916: 907: 901: 900: 872: 769: 685: 664:sp. NCIMB 9784 ( 612: 601:Candida albicans 495: 474:NADH:cytochrome 411: 379:CPR/P450 systems 333: 261: 114: 1428: 1427: 1423: 1422: 1421: 1419: 1418: 1417: 1413:Cytochrome P450 1403: 1402: 1401: 1389: 1381: 1379: 1374: 1279: 1195: 1160: 1151: 1114: 1109: 1108: 1074: 1069: 1068: 1064: 1030: 1029: 1025: 989: 988: 984: 953: 952: 948: 941: 914: 909: 908: 904: 874: 873: 869: 864: 833: 829: 811: 796: 763: 740:denitrification 733: 722: 707: 703: 658: 647: 632: 594: 583: 569: 554: 531: 516: 480: 467: 460: 452: 441: 381: 370: 355: 351: 325: 321: 298: 283: 279: 248: 210: 178: 146: 92: 88: 80: 72: 64: 18:cytochrome P450 12: 11: 5: 1426: 1424: 1416: 1415: 1405: 1404: 1400: 1399: 1376: 1375: 1373: 1372: 1367: 1362: 1357: 1352: 1351: 1350: 1345: 1335: 1330: 1325: 1320: 1315: 1310: 1309: 1308: 1306:Dihydroorotase 1303: 1298: 1287: 1285: 1281: 1280: 1278: 1277: 1276: 1275: 1270: 1265: 1260: 1250: 1249: 1248: 1243: 1238: 1228: 1227: 1226: 1221: 1216: 1205: 1203: 1197: 1196: 1194: 1193: 1192: 1191: 1186: 1176: 1170: 1168: 1166:Photosynthesis 1162: 1161: 1152: 1150: 1149: 1142: 1135: 1127: 1121: 1120: 1113: 1112:External links 1110: 1107: 1106: 1062: 1023: 982: 963:(4): 796–801. 946: 939: 902: 883:(2): 139–147. 866: 865: 863: 860: 831: 827: 809: 794: 790: 789: 786: 785: 782: 779: 776: 773: 761: 732: 729: 728: 727: 724: 723: 720: 717: 714: 711: 708: 705: 701: 698: 695: 692: 689: 657: 654: 653: 652: 649: 648: 645: 642: 639: 636: 633: 630: 625: 622: 619: 616: 592: 581: 575: 574: 571: 570: 567: 564: 561: 558: 555: 552: 546: 543: 540: 537: 533: 532: 529: 526: 523: 520: 517: 514: 508: 505: 502: 499: 478: 465: 458: 451: 448: 447: 446: 443: 442: 439: 436: 433: 430: 427: 424: 421: 418: 415: 380: 377: 376: 375: 372: 371: 368: 365: 362: 359: 356: 353: 349: 346: 343: 340: 337: 323: 319: 304: 303: 300: 299: 296: 293: 290: 287: 284: 281: 277: 274: 271: 268: 265: 254: 253: 250: 249: 246: 243: 240: 235: 232: 227: 224: 219: 216: 212: 211: 208: 205: 202: 199: 196: 193: 190: 187: 184: 180: 179: 176: 173: 170: 167: 164: 161: 158: 155: 152: 148: 147: 144: 141: 138: 135: 132: 131:putidaredoxin 129: 126: 121: 118: 90: 86: 79: 76: 70: 62: 13: 10: 9: 6: 4: 3: 2: 1425: 1414: 1411: 1410: 1408: 1398: 1393: 1388: 1384: 1371: 1368: 1366: 1363: 1361: 1358: 1356: 1353: 1349: 1346: 1344: 1341: 1340: 1339: 1336: 1334: 1331: 1329: 1326: 1324: 1321: 1319: 1316: 1314: 1311: 1307: 1304: 1302: 1299: 1297: 1294: 1293: 1292: 1289: 1288: 1286: 1282: 1274: 1271: 1269: 1266: 1264: 1261: 1259: 1256: 1255: 1254: 1251: 1247: 1244: 1242: 1239: 1237: 1234: 1233: 1232: 1229: 1225: 1222: 1220: 1217: 1215: 1212: 1211: 1210: 1207: 1206: 1204: 1202: 1201:Dehydrogenase 1198: 1190: 1187: 1185: 1182: 1181: 1180: 1177: 1175: 1172: 1171: 1169: 1167: 1163: 1159: 1155: 1148: 1143: 1141: 1136: 1134: 1129: 1128: 1125: 1119: 1116: 1115: 1111: 1102: 1098: 1093: 1088: 1084: 1080: 1079:J. Biol. Chem 1073: 1066: 1063: 1058: 1054: 1050: 1046: 1042: 1038: 1034: 1027: 1024: 1019: 1015: 1010: 1005: 1001: 997: 996:Front. Biosci 993: 986: 983: 978: 974: 970: 966: 962: 958: 950: 947: 942: 940:9780762301133 936: 932: 928: 924: 920: 913: 906: 903: 898: 894: 890: 886: 882: 878: 871: 868: 861: 859: 857: 854: 850: 847: 843: 840: 835: 825: 821: 817: 816: 807: 803: 802: 797: 783: 780: 774: 770: 767: 766: 765: 759: 758:nitrous oxide 756:(NO) to form 755: 751: 750: 745: 741: 737: 730: 718: 715: 709: 696: 690: 686: 683: 682: 681: 679: 675: 671: 667: 663: 655: 643: 640: 634: 629: 623: 617: 613: 610: 609: 608: 606: 602: 598: 591: 587: 580: 565: 562: 559: 556: 551: 547: 544: 541: 538: 534: 527: 524: 521: 518: 513: 509: 506: 503: 500: 496: 493: 492: 491: 489: 486: 482: 477: 471: 464: 457: 449: 437: 434: 428: 422: 416: 412: 409: 408: 407: 405: 401: 397: 394: 390: 386: 378: 366: 363: 357: 344: 338: 334: 331: 330: 329: 327: 315: 314: 309: 294: 291: 285: 272: 266: 262: 259: 258: 257: 244: 241: 239: 236: 233: 231: 228: 225: 223: 220: 217: 213: 206: 203: 200: 197: 194: 191: 188: 185: 181: 174: 171: 168: 165: 162: 159: 156: 153: 149: 142: 139: 136: 133: 130: 127: 125: 122: 119: 115: 112: 111: 110: 108: 104: 100: 96: 84: 83:Mitochondrial 77: 75: 69: 65: 61: 55: 51: 47: 43: 39: 35: 30: 25: 23: 19: 1312: 1082: 1078: 1065: 1040: 1037:Biochemistry 1036: 1032: 1026: 1009:10.2741/1356 999: 995: 985: 960: 956: 949: 922: 918: 905: 880: 876: 870: 836: 813: 799: 791: 754:nitric oxide 747: 734: 677: 669: 661: 659: 627: 604: 600: 596: 589: 585: 578: 576: 549: 511: 475: 469: 462: 455: 453: 403: 399: 382: 311: 310:system from 305: 255: 163:terpredoxin 81: 67: 59: 46:flavoprotein 44:-containing 26: 21: 15: 1179:Photosystem 678:Burkolderia 662:Rhodococcus 383:Eukaryotic 230:adrenodoxin 195:rhodocoxin 95:adrenodoxin 58:cytochrome 48:or domain, 862:References 385:microsomal 326:ferredoxin 54:ferredoxin 925:: 29–56. 481:reductase 40:domains: 1407:Category 1101:14514666 1057:16819841 1018:14977570 977:16042601 897:11356142 856:5.3.99.5 849:5.3.99.4 842:4.2.1.92 820:CYP152B1 806:CYP152A1 674:CYP116A1 666:CYP116B2 615:NAD(P)H 586:in vitro 52:domain, 1397:Biology 1154:Enzymes 772:NAD(P)H 744:CYP55A1 488:1.6.2.2 396:1.6.2.4 336:NAD(P)H 264:NAD(P)H 238:CYP11A1 201:CYP116 169:CYP108 137:CYP101 1383:Portal 1263:BCKDHB 1258:BCKDHA 1099:  1055:  1016:  975:  937:  895:  483:(CBR; 470:second 391:(CPR; 107:CYP101 34:domain 1348:HADHB 1343:HADHA 1284:Other 1075:(PDF) 915:(PDF) 812:from 798:from 778:P450 746:from 713:P450 638:P450 595:from 560:P450 522:P450 498:NADPH 432:P450 414:NADPH 361:P450 289:P450 215:NADPH 38:redox 1241:DLST 1236:OGDH 1097:PMID 1053:PMID 1014:PMID 973:PMID 935:ISBN 893:PMID 694:FMN 688:NADH 621:FAD 605:both 548:cyt 536:NADH 510:cyt 426:FMN 420:FAD 402:and 342:FAD 306:The 270:FAD 183:NADH 151:NADH 117:NADH 103:NADH 56:and 1291:CAD 1273:DLD 1268:DBT 1246:DLD 1087:doi 1083:278 1045:doi 1004:doi 965:doi 927:doi 885:doi 810:SPΞ± 795:BSΞ² 784:NO 542:CBR 504:CPR 490:): 50:FMN 42:FAD 1409:: 1224:E3 1219:E2 1214:E1 1189:II 1156:: 1095:. 1081:. 1077:. 1051:. 1041:45 1039:. 1012:. 998:. 994:. 971:. 961:33 959:. 933:. 923:14 917:. 891:. 881:29 879:. 853:EC 846:EC 839:EC 826:(H 775:β†’ 760:(N 710:β†’ 700:Fe 697:β†’ 691:β†’ 641:β†’ 635:β†’ 624:β†’ 618:β†’ 545:β†’ 539:β†’ 507:β†’ 501:β†’ 485:EC 429:β†’ 423:β†’ 417:β†’ 393:EC 358:β†’ 348:Fe 345:β†’ 339:β†’ 286:β†’ 276:Fe 273:β†’ 267:β†’ 234:β†’ 226:β†’ 218:β†’ 198:β†’ 192:β†’ 186:β†’ 166:β†’ 160:β†’ 154:β†’ 134:β†’ 128:β†’ 120:β†’ 24:. 1385:: 1184:I 1146:e 1139:t 1132:v 1103:. 1089:: 1059:. 1047:: 1020:. 1006:: 1000:9 979:. 967:: 943:. 929:: 899:. 887:: 832:2 830:O 828:2 818:( 804:( 781:β†’ 762:2 721:2 719:O 716:β†’ 706:2 704:S 702:2 672:( 646:2 644:O 631:5 628:b 593:5 590:b 582:5 579:b 568:2 566:O 563:β†’ 557:β†’ 553:5 550:b 530:2 528:O 525:β†’ 519:β†’ 515:5 512:b 479:5 476:b 466:5 463:b 459:5 456:b 440:2 438:O 435:β†’ 369:2 367:O 364:β†’ 354:4 352:S 350:3 324:4 322:S 320:3 297:2 295:O 292:β†’ 282:2 280:S 278:2 247:2 245:O 242:β†’ 209:2 207:O 204:β†’ 177:2 175:O 172:β†’ 145:2 143:O 140:β†’ 91:2 89:S 87:2 71:5 68:b 63:5 60:b

Index

cytochrome P450
electron-transfer
domain
redox
FAD
flavoprotein
FMN
ferredoxin
cytochrome b5
Mitochondrial
adrenodoxin
adrenodoxin reductase
NADH
CYP101
putidaredoxin reductase
adrenodoxin reductase
adrenodoxin
CYP11A1
sterol demethylase
Mycobacterium tuberculosis
bacterial-type Fe3S4 ferredoxin
microsomal
cytochrome P450 reductase
EC
1.6.2.4
NADH:cytochrome b5 reductase
EC
1.6.2.2
CYP116B2
CYP116A1

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