495:
cluster in a hydrophobic core, only being able to form about five conserved H-bond to the cluster ligands from the backbone. In contrast, the protein associated with the Fd's allows these clusters to contact solvent resulting in 8 protein H-bonding interactions. The protein binds Fd via conserved CysXXCysXXCys structure (X stands for any amino acid). Also, the unique protein structure and dipolar interactions from peptide and intermolecular water contribute to shielding the cluster from the attack of random outside electron donors, which protects itself from hydrolysis.
26:
489:
249:
the ferredoxin (Fd) family and the high-potential iron–suflur protein (HiPIP) family. Both HiPIP and Fd share the same resting state: , which have the same geometric and spectroscopic features. Differences arise when it comes to their active state: HiPIP forms by oxidation to , and Fd is formed by reduction to .
248:
The clusters are abundant cofactors of metalloproteins. They participate in electron-transfer sequences. The core structure for the cluster is a cube with alternating Fe and S vertices. These clusters exist in two oxidation states with a small structural change. Two families of clusters are known:
494:
The different oxidation states are explained by the proteins that combined with the cluster. Analysis from crystallographic data suggests that HiPIP is capable of preserving its higher oxidation state by forming fewer hydrogen bonds with water. The characteristic fold of the proteins wraps the
748:
Dey, Abhishek; Jenney, Francis; Adams, Michael; Babini, Elena; Takahashi, Yasuhiro; Fukuyama, Keiichi; Hodgson, Keith; Hedman, Britt; Solomon, Edward (2007). "Solvent Tuning of
Electrochemical Potentials in the Active Sites of HiPIP Versus Ferredoxin".
222:
The HiPIPs are small proteins, typically containing 63 to 85 amino acid residues. The sequences show significant variation. As shown in the following schematic representation the iron-sulfur cluster is bound by four conserved cysteine residues.
255:
645:
Breiter DR, Meyer TE, Rayment I, Holden HM (1991). "The molecular structure of the high potential iron-sulfur protein isolated from
Ectothiorhodospira halophila determined at 2.5-A resolution".
550:. HiPIPs are periplasmic proteins in photosynthetic bacteria. They play a role of electron shuttles in the cyclic electron flow between the photosynthetic reaction center and the
558:. Other oxidation reactions HiPIP involved include catalyzing Fe(II) oxidation, being electron donor to reductase and electron accepter for some thiosulfate-oxidizing enzyme.
575:
Benning MM, Meyer TE, Rayment I, Holden HM (1994). "Molecular
Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated from Ectothiorhodospira vacuolata".
161:
900:"Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: Thermostability and electron transfer"
117:
105:
802:"Synthetic analogues of [Fe4S4(Cys)3(His)] in hydrogenases and [Fe4S4(Cys)4] in HiPIP derived from all-ferric [Fe4S4{N(SiMe3)2}4]"
551:
979:
85:
484:{\displaystyle {\ce {{\underset {(for\ HiPIP)}{^{3}+}}<=>{\underset {(resting\ state)}{^{2}+}}<=>{\underset {(for\ Fd)}{+}}}}}
860:
538:
HiPIPs take part in many oxidizing reactions in creatures, and are especially known with photosynthetic anaerobic bacteria, such as
181:
530:, and NaSH. The synthesis of HiPIP analogues can help people understand the factors that cause variety redox of HiPIP.
610:
Stephens, P. J.; Jollie, D. R.; Warshel, A. (1996). "Protein
Control of Redox Potentials of Iron−Sulfur Proteins".
974:
800:
Ohki, Yasuhiro; Tanifuji, Kazuki; Yamada, Norihiro; Imada, Motosuke; Tajima, Tomoyuki; Tatsumi, Kazujuki (2011).
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169:
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HiPIP analogues can be synthesized by ligand exchange reactions of with 4 equiv of thiols (HSR) as follows:
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Proceedings of the
National Academy of Sciences of the United States of America
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701:"Identifying sequence determinants of reduction potentials of metalloproteins"
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Valentine, Joan; Bertini, Ivano; Gray, Harry; Stiefel, Edward (2006-10-30).
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C: conserved cysteine residue involved in the binding of the 4Fe-4S core.
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The precursor cluster can be synthesized by one-pot reaction of FeCl
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330:
226:| | | | xxxxxxxxxxxxxxxxxxxCxCxxxxxxxCxxxxxCxxxx
952:
138:
49:
680:
R. H. Holm (2004). "Electron
Transfer: Iron-Sulfur Clusters".
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Structure of the oxidized high-potential iron-sulfur protein.
448:
435:
369:
356:
290:
277:
898:
Nogi T, Fathir I, Kobayashi M, Nozawa T, Miki K (2000).
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Biological
Inorganic Chemistry: Structure and Reactivity
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This article incorporates text from the public domain
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699:Perrin, Bradley Scott Jr.; Ichiye, Toshiko (2013).
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855:(first ed.). University Science Books.
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884:- High potential iron-sulfur proteins in
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647:The Journal of Biological Chemistry
194:High potential iron-sulfur proteins
19:High potential iron-sulfur protein
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133:Available protein structures:
980:Peripheral membrane proteins
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717:10.1007/s00775-013-1004-6
507:+ 4RSH → + 4 HN(SiMe
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211:Paracoccus denitrificans
819:10.1073/pnas.1106472108
771:10.1126/science.1147753
196:(HIPIP) are a class of
925:10.1073/pnas.240224997
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534:Biochemical reactions
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204:that participate in
198:iron-sulfur proteins
916:2000PNAS...9713561N
910:(25): 13561–13566.
812:(31): 12635–12640.
763:2007Sci...318.1464D
757:(5855): 1464–1468.
659:10.2210/pdb2hip/pdb
653:(28): 18660–18667.
589:10.1021/bi00175a016
499:Synthetic analogues
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202:ferredoxins
200:. They are
118:OPM protein
36:Identifiers
969:Categories
562:References
541:Chromatium
522:, NaN(SiMe
145:structures
961:IPR000170
881:PDOC00515
412:reduction
333:oxidation
218:Structure
79:PDOC00515
67:IPR000170
957:InterPro
944:11095707
838:21768339
787:33046150
779:18048692
735:23690205
688:: 61-90.
632:11848834
407:⇌
328:⇌
233:clusters
162:RCSB PDB
62:InterPro
912:Bibcode
886:PROSITE
829:3150945
759:Bibcode
751:Science
726:3723707
667:1917989
597:8117708
556:complex
390:resting
74:PROSITE
55:PF01355
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177:PDBsum
151:
141:
99:SUPFAM
41:Symbol
935:17615
783:S2CID
396:state
317:HiPIP
95:SCOPe
86:SCOP2
44:HIPIP
955:and
953:Pfam
940:PMID
857:ISBN
834:PMID
775:PMID
731:PMID
663:PMID
628:PMID
593:PMID
239:edit
170:PDBj
166:PDBe
149:ECOD
139:Pfam
123:1hpi
91:1hpi
50:Pfam
930:PMC
920:doi
824:PMC
814:doi
810:108
767:doi
755:318
721:PMC
713:doi
655:doi
651:266
620:doi
585:doi
466:for
311:for
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157:PDB
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472:Fd
427:Fe
348:Fe
269:Fe
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463:(
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444:4
440:S
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387:(
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378:2
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365:4
361:S
352:4
344:[
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308:(
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299:3
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286:4
282:S
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