239:
1444:
365:, however these transporters aren't exactly selective as they provide difficulty in binding to the Iron (II) ion so other ions bind as well such as Zn(II), Mn(II), and Cd(II). Transportation like this mainly takes place in plants and in anaerobic environments where oxidation back to the Iron (III) species is impossible.
303:) to monodehydroascorbate is essential when the ferric Fe(III) ion is converted to ferrous Fe(II).The Fe(III) species is insoluble, hence becoming one of the most problematic metal species to introduce and dissolve into an organism's system. Especially in eukaryotes such as humans, fungi, and bacteria, the
341:
Reducing the ferrous (III) ion to ferrous (II) increases the bio availability which improves the rate and extent at which the aqueous soluble ferrous (II) iron will reach the system of the organism and will prevent the mineralization of the aqueous ferrous (III). The general for a following reduction
332:
have a very strong binding affinity to Fe and does not bind to other metal ions that may be present. The following is a general chemical equation to represent the process of chelation: A structure of a siderophore. The phenyls with two hydroxyl groups are the binding spots. These iron complexes binds
345:
Once the iron complex nears the cell surface, the Iron (II) ion becomes susceptible to accept water ligands, thus hydrating the ion. This process usually occurs in aerobic environments where the Iron (II) ion is also favored. Once the complex is reduced, it must be then re-oxidized in proximity to
333:
to a receptor on an iron transport that is unique to the siderophore used. The receptor dissociates once it nears the cell's membrane which creates an aqueous ferric Fe(III) ion that can either be used for uptake or reduced to Fe where transporters specific to that ion can transport it instead.
327:
Chelation can increase the solubility of the iron (III) by coupling 'siderophore ligands' to the Iron species in its solid state to make it transform into an aqueous species. Especially in bacteria, and fungi,
417:
McKie AT, Barrow D, Latunde-Dada GO, Rolfs A, Sager G, Mudaly E, Mudaly M, Richardson C, Barlow D, Bomford A, Peters TJ, Raja KB, Shirali S, Hediger MA, Farzaneh F, Simpson RJ (March 2001).
270:
1103:
966:
1108:
165:
856:
184:
661:
Srai SK, Bomford A, McArdle HJ (June 2002). "Iron transport across cell membranes: molecular understanding of duodenal and placental iron uptake".
971:
1120:
382:
Flatmark T, Terland O (December 1971). "Cytochrome b 561 of the bovine adrenal chromaffin granules. A high potential b-type cytochrome".
849:
1163:
1130:
177:
937:
842:
144:
120:
1319:
696:
Nicklaus MC, Wang S, Driscoll JS, Milne GW (April 1995). "Conformational changes of small molecules binding to proteins".
346:
the cell membrane because it contains binding sites typically only for Iron (III) ions that the protein will then undergo
1434:
824:
1125:
311:
of the ferrous (II) ion. There are three ways to increase the solubility of Iron (III) and overcome that challenge:
1304:
1420:
1407:
1394:
1381:
1368:
1355:
1342:
1076:
1027:
1004:
981:
947:
919:
879:
1314:
138:
1268:
1211:
1085:
1017:
961:
870:
828:
238:
205:
43:
985:
125:
1216:
466:
Su D, Asard H (August 2006). "Three mammalian cytochromes b561 are ascorbate-dependent ferrireductases".
255:
189:
1237:
1156:
612:"A cytochrome b561 with ferric reductase activity from the parasitic blood fluke, Schistosoma japonicum"
347:
113:
1309:
892:
1273:
1115:
1090:
141:
17:
65:
1464:
1206:
1095:
551:
491:
448:
353:
There are some transporters that allow the Iron (II) ions to be transported directly such as the
510:
803:
754:
713:
678:
643:
592:
543:
483:
440:
399:
233:
132:
1252:
1247:
1221:
1149:
956:
793:
785:
744:
705:
670:
633:
623:
610:
Glanfield A, McManus DP, Smyth DJ, Lovas EM, Loukas A, Gobert GN, Jones MK (November 2010).
582:
533:
525:
475:
430:
391:
101:
1299:
1283:
1196:
362:
358:
354:
308:
222:
213:
77:
48:
1448:
1337:
1278:
866:
834:
798:
773:
638:
611:
160:
674:
1458:
1242:
1201:
932:
709:
479:
395:
555:
538:
495:
452:
1191:
1044:
419:"An iron-regulated ferric reductase associated with the absorption of dietary iron"
587:
570:
529:
628:
1415:
1350:
1186:
994:
329:
1443:
733:"Combinatorial control of yeast FET4 gene expression by iron, zinc, and oxygen"
1031:
1008:
883:
789:
511:"An Arabidopsis cytochrome b561 with trans-membrane ferrireductase capability"
284:
1389:
1363:
435:
418:
312:
304:
300:
245:
229:
807:
758:
749:
732:
682:
647:
596:
571:"Dcytb (Cybrd1) functions as both a ferric and a cupric reductase in vitro"
547:
487:
444:
717:
403:
208:
89:
1035:
288:
108:
1402:
1172:
218:
172:
84:
72:
60:
1376:
1064:
1059:
1054:
923:
316:
1049:
907:
902:
897:
96:
1145:
838:
237:
1141:
226:
Fe(III):ascorbate oxidorectuctase (electron-translocating)
259:
1432:
569:
Wyman S, Simpson RJ, McKie AT, Sharp PA (June 2008).
258:
287:
that acts on hexacyanoferrate(III) and other ferric
1328:
1292:
1261:
1230:
1179:
1075:
1026:
1003:
980:
946:
918:
878:
384:
Biochimica et
Biophysica Acta (BBA) - Bioenergetics
183:
171:
159:
154:
131:
119:
107:
95:
83:
71:
59:
54:
42:
37:
32:
967:4-Hydroxy-3-methylbut-2-enyl diphosphate reductase
663:Best Practice & Research. Clinical Haematology
264:
350:to transition to the other side of the membrane.
342:in relation to an iron complex is as follows:
307:of ascorbate is very important as well as the
1157:
850:
8:
295:Ferric Fe(III) and Ferrous Fe(II) Solubility
1079:: Acting on X-H and Y-H to form an X-Y bond
1164:
1150:
1142:
857:
843:
835:
151:
827:at the U.S. National Library of Medicine
797:
748:
637:
627:
586:
537:
434:
257:
825:Ascorbate+ferrireductase+(transmembrane)
202:Ascorbate ferrireductase (transmembrane)
33:Ascorbate ferrireductase (transmembrane)
1439:
972:7-Hydroxymethyl chlorophyll a reductase
374:
509:BĂ©rczi A, Su D, Asard H (April 2007).
29:
731:Waters BM, Eide DJ (September 2002).
283:Ascorbate ferrireductase is a diheme
7:
1121:Tetrahydrocannabinolic acid synthase
698:Bioorganic & Medicinal Chemistry
737:The Journal of Biological Chemistry
299:Using the conversion of ascorbate (
265:{\displaystyle \rightleftharpoons }
18:L-ascorbate—cytochrome-b5 reductase
25:
1442:
1131:Dichlorochromopyrrolate synthase
616:PLOS Neglected Tropical Diseases
480:10.1111/j.1742-4658.2006.05381.x
938:(Methionine synthase) reductase
1:
1109:(-)-bisdechlorogeodin-forming
1104:(+)-bisdechlorogeodin-forming
675:10.1016/s1521-6926(02)90003-4
588:10.1016/j.febslet.2008.05.010
530:10.1016/j.febslet.2007.03.006
950:: Acting on CH or CH2 groups
772:Garrick MD (February 2011).
710:10.1016/0968-0896(95)00031-b
629:10.1371/journal.pntd.0000884
396:10.1016/0005-2728(71)90052-1
272:monodehydroascorbate radical
1126:Cannabidiolic acid synthase
1481:
1320:Michaelis–Menten kinetics
790:10.1007/s12263-010-0184-8
774:"Human iron transporters"
150:
1212:Diffusion-limited enzyme
1086:Isopenicillin N synthase
1018:Nitrogenase (flavodoxin)
962:Ribonucleotide reductase
829:Medical Subject Headings
539:10067/629620151162165141
436:10.1126/science.1057206
244:
750:10.1074/jbc.m206214200
348:conformational changes
266:
242:
1305:Eadie–Hofstee diagram
1238:Allosteric regulation
778:Genes & Nutrition
319:, and acidification.
267:
241:
1315:Lineweaver–Burk plot
1007:: Acting on reduced
986:iron–sulfur proteins
893:Superoxide dismutase
256:
1116:Aureusidin synthase
1091:Columbamine oxidase
1274:Enzyme superfamily
1207:Enzyme promiscuity
1100:Sulochrin oxidase
1096:Reticuline oxidase
262:
243:
1430:
1429:
1139:
1138:
234:chemical reaction
199:
198:
195:
194:
114:metabolic pathway
16:(Redirected from
1472:
1447:
1446:
1438:
1310:Hanes–Woolf plot
1253:Enzyme activator
1248:Enzyme inhibitor
1222:Enzyme catalysis
1166:
1159:
1152:
1143:
957:Xanthine oxidase
859:
852:
845:
836:
812:
811:
801:
769:
763:
762:
752:
743:(37): 33749–57.
728:
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721:
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658:
652:
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641:
631:
607:
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468:The FEBS Journal
463:
457:
456:
438:
429:(5509): 1755–9.
414:
408:
407:
379:
271:
269:
268:
263:
152:
30:
27:Class of enzymes
21:
1480:
1479:
1475:
1474:
1473:
1471:
1470:
1469:
1455:
1454:
1453:
1441:
1433:
1431:
1426:
1338:Oxidoreductases
1324:
1300:Enzyme kinetics
1288:
1284:List of enzymes
1257:
1226:
1197:Catalytic triad
1175:
1170:
1140:
1135:
1071:
1022:
999:
976:
942:
914:
874:
867:oxidoreductases
863:
821:
816:
815:
771:
770:
766:
730:
729:
725:
695:
694:
690:
660:
659:
655:
609:
608:
604:
568:
567:
563:
513:
508:
507:
503:
474:(16): 3722–34.
465:
464:
460:
416:
415:
411:
381:
380:
376:
371:
339:
325:
309:bioavailability
297:
281:
280:
277:
274:
254:
253:
252:
249:
223:systematic name
214:cytochrome b561
28:
23:
22:
15:
12:
11:
5:
1478:
1476:
1468:
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1457:
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1411:
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1302:
1296:
1294:
1290:
1289:
1287:
1286:
1281:
1276:
1271:
1265:
1263:
1262:Classification
1259:
1258:
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1240:
1234:
1232:
1228:
1227:
1225:
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1194:
1189:
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1168:
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1154:
1146:
1137:
1136:
1134:
1133:
1128:
1123:
1118:
1113:
1112:
1111:
1106:
1098:
1093:
1088:
1082:
1080:
1073:
1072:
1070:
1069:
1068:
1067:
1062:
1057:
1052:
1041:
1039:
1024:
1023:
1021:
1020:
1014:
1012:
1001:
1000:
998:
997:
991:
989:
978:
977:
975:
974:
969:
964:
959:
953:
951:
944:
943:
941:
940:
935:
929:
927:
916:
915:
913:
912:
911:
910:
905:
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875:
864:
862:
861:
854:
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839:
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832:
820:
819:External links
817:
814:
813:
764:
723:
688:
653:
602:
581:(13): 1901–6.
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338:
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232:the following
228:. This enzyme
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1279:Enzyme family
1277:
1275:
1272:
1270:
1267:
1266:
1264:
1260:
1254:
1251:
1249:
1246:
1244:
1243:Cooperativity
1241:
1239:
1236:
1235:
1233:
1229:
1223:
1220:
1218:
1215:
1213:
1210:
1208:
1205:
1203:
1202:Oxyanion hole
1200:
1198:
1195:
1193:
1190:
1188:
1185:
1184:
1182:
1178:
1174:
1167:
1162:
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933:Ceruloplasmin
931:
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917:
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904:
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751:
746:
742:
738:
734:
727:
724:
719:
715:
711:
707:
704:(4): 411–28.
703:
699:
692:
689:
684:
680:
676:
672:
669:(2): 243–59.
668:
664:
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645:
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635:
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625:
621:
617:
613:
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603:
598:
594:
589:
584:
580:
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572:
565:
562:
557:
553:
549:
545:
540:
535:
531:
527:
524:(7): 1505–8.
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390:(2): 487–91.
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100:
98:
94:
91:
90:NiceZyme view
88:
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79:
76:
74:
70:
67:
64:
62:
58:
53:
50:
47:
45:
41:
36:
31:
19:
1416:Translocases
1413:
1400:
1387:
1374:
1361:
1351:Transferases
1348:
1335:
1192:Binding site
1045:Glutaredoxin
1030:: Acting on
984:: Acting on
922:: Oxidizing
882:: Acting on
784:(1): 45–54.
781:
777:
767:
740:
736:
726:
701:
697:
691:
666:
662:
656:
622:(11): e884.
619:
615:
605:
578:
575:FEBS Letters
574:
564:
521:
518:FEBS Letters
517:
504:
471:
467:
461:
426:
422:
412:
387:
383:
377:
352:
344:
340:
330:siderophores
326:
298:
282:
225:
212:
201:
200:
78:BRENDA entry
1187:Active site
995:Nitrogenase
886:as acceptor
66:IntEnz view
38:Identifiers
1390:Isomerases
1364:Hydrolases
1231:Regulation
1032:phosphorus
1009:flavodoxin
884:superoxide
873:1.15–1.21)
369:References
361:, and the
285:cytochrome
135:structures
102:KEGG entry
1465:EC 1.16.5
1269:EC number
1038:in donors
988:as donors
337:Reduction
323:Chelation
317:reduction
313:chelation
301:Vitamin C
260:⇌
250:+ Fe(III)
246:ascorbate
230:catalyses
55:Databases
1459:Category
1293:Kinetics
1217:Cofactor
1180:Activity
1011:as donor
808:21437029
759:12095998
683:12401306
648:21103361
597:18498772
556:40210419
548:17376442
496:23331329
488:16911521
453:44351106
445:11230685
289:chelates
275:+ Fe(II)
217:) is an
209:1.16.5.1
190:proteins
178:articles
166:articles
139:RCSB PDB
49:1.16.5.1
1449:Biology
1403:Ligases
1173:Enzymes
1036:arsenic
799:3040799
718:8581425
639:2982821
423:Science
404:4332308
305:upcycle
126:profile
109:MetaCyc
1435:Portal
1377:Lyases
865:Other
831:(MeSH)
806:
796:
757:
716:
681:
646:
636:
595:
554:
546:
494:
486:
451:
443:
402:
219:enzyme
173:PubMed
155:Search
145:PDBsum
85:ExPASy
73:BRENDA
61:IntEnz
44:EC no.
1329:Types
1065:GLRX5
1060:GLRX3
1055:GLRX2
924:metal
552:S2CID
514:(PDF)
492:S2CID
449:S2CID
221:with
121:PRIAM
1421:list
1414:EC7
1408:list
1401:EC6
1395:list
1388:EC5
1382:list
1375:EC4
1369:list
1362:EC3
1356:list
1349:EC2
1343:list
1336:EC1
1077:1.21
1050:GLRX
1028:1.20
1005:1.19
982:1.18
948:1.17
926:ions
920:1.16
908:SOD3
903:SOD2
898:SOD1
880:1.15
804:PMID
755:PMID
714:PMID
679:PMID
644:PMID
593:PMID
544:PMID
484:PMID
441:PMID
400:PMID
363:Irt1
359:Dmt1
355:Fet4
185:NCBI
142:PDBe
97:KEGG
1034:or
794:PMC
786:doi
745:doi
741:277
706:doi
671:doi
634:PMC
624:doi
583:doi
579:582
534:hdl
526:doi
522:581
476:doi
472:273
431:doi
427:291
392:doi
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