522:
40:
472:
206:
740:
Friesner, R. A.; Baik, M.-H.; Gherman, B. F.; Guallar, V.; Wirstam, M.; Murphy, R. B.; Lippard, S. J. (2003). "How iron-containing proteins control dioxygen chemistry: a detailed atomic level description via accurate quantum chemical and mixed quantum mechanics/molecular mechanics calculations".
543:
each, although some species have dimeric, trimeric and tetrameric hemerythrins. Each subunit has a four-α-helix fold binding a binuclear iron centre. Because of its size hemerythrin is usually found in cells or "corpuscles" in the blood rather than free floating.
764:
Chow ED, Liu OW, O'Brien S, Madhani HD (September 2007). "Exploration of whole-genome responses of the human AIDS-associated yeast pathogen
Cryptococcus neoformans var grubii: nitric oxide stress and body temperature".
911:
Karlsen, O.A., Ramsevik, L., Bruseth, L.J., Larsen, Ø., Brenner, A., Berven, F.S., Jensen, H.B. and
Lillehaug, J.R. (2005). "Characterization of a prokaryotic haemerythrin from the methanotrophic bacterium
340:-binding protein found in the muscles of marine invertebrates. Hemerythrin and myohemerythrin are essentially colorless when deoxygenated, but turn a violet-pink in the oxygenated state.
355:, and hemerythrin do not refer to the heme group (only found in globins). Instead, these names are derived from the Greek word for blood. Hemerythrin may also contribute to
959:
710:
173:
1059:
570:, unlike hemoglobin which has a very high affinity for CO. Hemerythrin's low affinity for CO poisoning reflects the role of hydrogen-bonding in the binding of O
559:. Cooperative binding is achieved by interactions between subunits: the oxygenation of one subunit increases the affinity of a second unit for oxygen.
121:
1052:
810:"Widespread Distribution in Pathogenic Bacteria of Di-Iron Proteins That Repair Oxidative and Nitrosative Damage to Iron-Sulfur Centers"
620:(Filobasidiella neoformans) that contains haemerythrin/HHE cation-binding domains is also involved in nitric oxide response. A
630:
switches to living in environments with low oxygen concentrations; perhaps this protein acts as an oxygen store or scavenger.
1045:
509:). Then electrons are transferred from the ferrous ions to generate the binuclear ferric (Fe,Fe) centre with bound peroxide (
501:
substrate. This proton-transfer result in the formation of a single oxygen atom (μ-oxo) bridge in oxy- and methemerythrin. O
411:
residues. Hemerythrin and myohemerythrin are often described according to oxidation and ligation states of the iron center:
193:
1193:
267:
240:
723:
D. M. Kurtz, Jr. "Dioxygen-binding
Proteins" in Comprehensive Coordination Chemistry II 2003, Volume 8, Pages 229–260.
399:
consists of a pair of iron centres. The iron atoms are bound to the protein through the carboxylate side chains of a
859:"Structure, function and evolution of the hemerythrin-like domain superfamily: Hemerythrin-like Domain Superfamily"
626:
protein containing this domain, iron-sulfur cluster repair protein ScdA, has been noted to be important when the
1183:
1178:
1133:
181:
1188:
633:
Hemerythrin/HHE (H-HxxxE-HxxxH-HxxxxD) proteins found in bacteria are implicated in signal transduction and
616:
1037:
539:
Hemerythrin typically exists as a homooctamer or heterooctamer composed of α- and β-type subunits of 13–14
360:
258:
231:
574:, a pathway mode that is incompatible with CO complexes which usually do not engage in hydrogen bonding.
1076:
953:
704:
622:
586:
occurs as a duplicated domain in hemerythrins, myohemerythrins and related proteins. This domain binds
177:
1143:
356:
134:
602:
596:
548:
300:
279:
252:
521:
1128:
941:
790:
663:"Immunological properties of oxygen transport proteins: hemoglobin, hemocyanin and hemerythrin"
998:
933:
890:
839:
782:
692:
527:
211:
168:
46:
1095:
976:
925:
880:
870:
829:
821:
774:
746:
724:
682:
674:
380:
303:
39:
160:
1068:
563:
494:
857:
Alvarez-Carreño, Claudia; Alva, Vikram; Becerra, Arturo; Lazcano, Antonio (April 2018).
1072:
885:
858:
834:
809:
687:
662:
583:
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1172:
929:
728:
642:
540:
459:
388:
126:
109:
1027:
945:
794:
78:
1138:
607:
156:
1164:
808:
Overton TW, Justino MC, Li Y, Baptista JM, Melo AM, Cole JA, et al. (2008).
90:
1107:
1102:
552:
471:
778:
678:
637:. More distantly related ones include H-HxxxE-H-HxxxE proteins (including the
634:
352:
348:
315:
307:
638:
408:
404:
400:
311:
205:
17:
937:
894:
843:
786:
696:
130:
1160:
1090:
627:
490:
482:
324:
285:
85:
980:
825:
505:
binds to the pentacoordinate Fe centre at the vacant coordination site (
611:
591:
590:
in hemerythrin, but can bind other metals in related proteins, such as
455:
333:
319:
288:
102:
97:
1017:
1008:
994:
531:
215:
50:
875:
551:
to oxygen, making it roughly 1/4 as efficient as hemoglobin. In some
525:
Hemerythrin homooctamer with a single monomer highlighted in yellow.
292:
188:
520:
470:
204:
114:
1031:
454:
by hemerythrin is accompanied by two-electron oxidation of the di
1156:
587:
489:). One iron is hexacoordinate and another is pentacoordinate. A
481:
Deoxyhemerythrin contains two high-spin ferrous ions bridged by
344:
150:
73:
1041:
343:
Hemerythrin does not, as the name might suggest, contain a
272:
245:
475:
Active site of hemerythrin before and after oxygenation.
600:
hemerythrin. It is also found in the NorA protein from
1155:
This article incorporates text from the public domain
375:
The mechanism of dioxygen binding is unusual. Most O
1116:
1083:
967:Stenkamp, R.E. (1994). "Dioxygen and hemerythrin".
187:
167:
149:
144:
120:
108:
96:
84:
72:
64:
59:
32:
610:, which suggests a different set-up for its metal
555:though, hemerythrin shows cooperative binding of O
1020:– PDB structure of azido-met myohemerythrin from
566:(CO) is actually lower than its affinity for O
1053:
606:, this protein is a regulator of response to
497:but also functions as a proton donor to the O
347:. The names of the blood oxygen transporters
8:
958:: CS1 maint: multiple names: authors list (
709:: CS1 maint: multiple names: authors list (
1060:
1046:
1038:
547:Unlike hemoglobin, most hemerythrins lack
141:
884:
874:
833:
686:
413:
1011:– PDB structure of oxyhemerythrin from
653:
44:Singly oxygenated hemerythrin protein.
951:
702:
517:Quaternary structure and cooperativity
466:is roughly described in this diagram:
209:Trimeric Hemerythrin Protein Complex (
29:
578:Hemerythrin/HHE cation-binding domain
7:
582:The hemerythrin/HHE cation-binding
379:carriers operate via formation of
25:
661:Coates, C.J., Decker, H. (2017).
395:, or -OOH). The site that binds O
930:10.1111/j.1742-4658.2005.04663.x
38:
462:(OOH) complex. The binding of O
1001:structure of deoxyhemerythrin
729:10.1016/B0-08-043748-6/08171-8
1:
751:10.1016/S0010-8545(02)00284-9
441:Fe—OH—Fe— (any other ligand)
383:, but hemerythrin holds the O
145:Available protein structures:
273:
246:
1210:
1154:
262:
235:
779:10.1007/s00294-007-0147-9
679:10.1007/s00018-016-2326-7
562:Hemerythrin affinity for
140:
37:
914:Methylococcus capsulatus
407:as well as through five
617:Cryptococcus neoformans
33:Hemerythrin-like family
536:
476:
220:
1077:Non-heme iron protein
1034:entry for hemerythrin
623:Staphylococcus aureus
524:
474:
284:'red') is an
208:
1194:Respiratory pigments
1144:Tyrosine hydroxylase
1022:Themiste zostericola
745:. 238–239: 267–290.
458:centre to produce a
1134:Iron–sulfur protein
981:10.1021/cr00027a008
826:10.1128/JB.01733-07
667:Cell. Mol. Life Sci
645:(H-HExxE-H-HxxxE).
603:Cupriavidus necator
597:Nereis diversicolor
549:cooperative binding
361:tissue regeneration
301:marine invertebrate
299:) transport in the
1129:Inositol oxygenase
537:
493:group serves as a
477:
381:dioxygen complexes
363:in certain worms.
318:, and in a single
221:
1152:
1151:
1024:(sipunculid worm)
1013:Themiste dyscrita
1005:(sipunculid worm)
1003:Themiste dyscrita
924:(10): 2428–2440.
614:. A protein from
448:
447:
371:binding mechanism
283:
271:
257:'blood',
256:
244:
203:
202:
199:
198:
194:structure summary
16:(Redirected from
1201:
1096:Bacterioferritin
1069:Carrier proteins
1062:
1055:
1048:
1039:
984:
963:
957:
949:
899:
898:
888:
878:
876:10.1002/pro.3374
854:
848:
847:
837:
805:
799:
798:
761:
755:
754:
743:Coord. Chem. Rev
737:
731:
721:
715:
714:
708:
700:
690:
658:
534:
420:deoxy (reduced)
414:
291:responsible for
278:
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266:
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251:
249:
239:
237:
218:
142:
53:
42:
30:
21:
1209:
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1198:
1184:Metalloproteins
1179:Protein domains
1169:
1168:
1167:
1153:
1148:
1112:
1079:
1073:metalloproteins
1066:
991:
966:
950:
910:
907:
905:Further reading
902:
863:Protein Science
856:
855:
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807:
806:
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773:(3–4): 137–48.
763:
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739:
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734:
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660:
659:
655:
651:
580:
573:
569:
564:carbon monoxide
558:
526:
519:
504:
500:
495:bridging ligand
465:
453:
450:The uptake of O
444:met (oxidized)
436:oxy (oxidized)
398:
394:
386:
378:
373:
370:
357:innate immunity
339:
298:
210:
55:
45:
28:
27:InterPro Family
23:
22:
15:
12:
11:
5:
1207:
1205:
1197:
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1191:
1189:Iron compounds
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1136:
1131:
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1120:
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1114:
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1111:
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990:
989:External links
987:
986:
985:
975:(3): 715–726.
964:
906:
903:
901:
900:
869:(4): 848–860.
849:
820:(6): 2004–13.
800:
756:
732:
716:
673:(2): 293–317.
652:
650:
647:
643:F-box proteins
579:
576:
571:
567:
556:
518:
515:
502:
498:
479:
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463:
451:
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422:
421:
418:
396:
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337:
330:Myohemerythrin
296:
226:(also spelled
201:
200:
197:
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191:
185:
184:
171:
165:
164:
154:
147:
146:
138:
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668:
664:
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644:
641:) and animal
640:
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624:
619:
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496:
492:
488:
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473:
469:
468:
467:
461:
460:hydroperoxide
457:
443:
440:
439:
435:
432:
431:
427:
424:
423:
419:
416:
415:
412:
410:
406:
402:
390:
389:hydroperoxide
382:
366:
364:
362:
359:and anterior
358:
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341:
335:
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309:
305:
302:
294:
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275:
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259:Ancient Greek
254:
248:
242:
233:
232:Ancient Greek
229:
225:
217:
213:
207:
195:
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83:
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71:
67:
63:
58:
52:
48:
41:
36:
31:
19:
1139:Lipoxygenase
1123:
1021:
1012:
1002:
972:
968:
954:cite journal
921:
917:
913:
866:
862:
852:
817:
813:
803:
770:
766:
759:
742:
735:
719:
705:cite journal
670:
666:
656:
632:
621:
615:
608:nitric oxide
601:
595:
581:
561:
546:
538:
510:
506:
486:
480:
449:
433:Fe—O—Fe—OOH
374:
342:
329:
323:
322:worm genus,
228:haemerythrin
227:
223:
222:
18:Haemerythrin
1124:Hemerythrin
1108:Transferrin
1103:Lactoferrin
814:J Bacteriol
767:Curr. Genet
553:brachiopods
316:brachiopods
308:sipunculids
224:Hemerythrin
68:Hemerythrin
60:Identifiers
1173:Categories
649:References
635:chemotaxis
405:aspartates
353:hemocyanin
349:hemoglobin
312:priapulids
286:oligomeric
157:structures
1165:IPR012312
1028:IPR002063
969:Chem. Rev
916:(Bath)".
639:E3 ligase
428:semi-met
425:Fe—OH—Fe
417:Fe—OH—Fe
409:histidine
401:glutamate
334:monomeric
268:romanized
241:romanized
103:PDOC00476
91:IPR035938
1161:InterPro
1091:Ferritin
1032:InterPro
946:11002682
938:15885093
895:29330894
844:18203837
795:10212964
787:17661046
697:27518203
628:organism
491:hydroxyl
483:hydroxyl
325:Magelona
274:erythrós
219:)
174:RCSB PDB
86:InterPro
1117:nonheme
886:5866928
835:2258886
688:5219038
612:ligands
594:in the
592:cadmium
535:
485:group (
456:ferrous
320:annelid
289:protein
282:
270::
263:ἐρυθρός
255:
243::
98:PROSITE
79:PF01814
54:
944:
936:
918:FEBS J
893:
883:
842:
832:
793:
785:
695:
685:
584:domain
293:oxygen
189:PDBsum
163:
153:
135:SUPFAM
65:Symbol
942:S2CID
791:S2CID
387:as a
332:is a
304:phyla
247:haîma
131:SCOPe
122:SCOP2
1159:and
1157:Pfam
1084:heme
1018:2MHR
1009:1HMO
995:1HMD
960:link
934:PMID
891:PMID
840:PMID
783:PMID
711:link
693:PMID
588:iron
532:1HMO
403:and
345:heme
280:lit.
253:lit.
236:αἷμα
216:1HMO
182:PDBj
178:PDBe
161:ECOD
151:Pfam
127:2HMZ
115:1HMO
110:CATH
74:Pfam
51:1HMO
999:PDB
977:doi
926:doi
922:272
881:PMC
871:doi
830:PMC
822:doi
818:190
775:doi
747:doi
725:doi
683:PMC
675:doi
541:kDa
528:PDB
513:).
391:(HO
306:of
212:PDB
169:PDB
47:PDB
1175::
1163::
1075::
1071:,
1030:–
997:-
973:94
971:.
956:}}
952:{{
940:.
932:.
920:.
889:.
879:.
867:27
865:.
861:.
838:.
828:.
816:.
812:.
789:.
781:.
771:52
769:.
707:}}
703:{{
691:.
681:.
671:74
669:.
665:.
530::
351:,
328:.
314:,
310:,
295:(O
277:,
265:,
261::
250:,
238:,
234::
230:;
214::
180:;
176:;
159:/
133:/
129:/
49::
1061:e
1054:t
1047:v
983:.
979::
962:)
948:.
928::
897:.
873::
846:.
824::
797:.
777::
753:.
749::
727::
713:)
699:.
677::
572:2
568:2
557:2
511:C
507:B
503:2
499:2
487:A
464:2
452:2
397:2
393:2
385:2
377:2
369:2
367:O
338:2
336:O
297:2
20:)
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