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.[3]
C: conserved cysteine residue involved in the binding of the 4Fe-4S core.[4]
[Fe4S4] clustersedit
The [Fe4S4] clusters are abundant cofactors of metalloproteins.[5] They participate in electron-transfer sequences. The core structure for the [Fe4S4] 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 [Fe4S4] clusters are known: the ferredoxin (Fd) family and the high-potential iron–suflur protein (HiPIP) family. Both HiPIP and Fd share the same resting state: [Fe4S4]2+, which have the same geometric and spectroscopic features. Differences arise when it comes to their active state: HiPIP forms by oxidation to [Fe4S4]3+, and Fd is formed by reduction to [Fe4S4]+.
The different oxidation states are explained by the proteins that combined with the [Fe4S4] 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 [Fe4S4] 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).[6] Also, the unique protein structure and dipolar interactions from peptide and intermolecular water contribute to shielding the [Fe4S4]3+ cluster from the attack of random outside electron donors, which protects itself from hydrolysis.
Synthetic analoguesedit
HiPIP analogues can be synthesized by ligand exchange reactions of [Fe4S4{N(SiMe3)2}4]− with 4 equiv of thiols (HSR) as follows:
The precursor cluster [Fe4S4{N(SiMe3)2}4]− can be synthesized by one-pot reaction of FeCl3, NaN(SiMe3)2, and NaSH. The synthesis of HiPIP analogues can help people understand the factors that cause variety redox of HiPIP.[7]
Biochemical reactionsedit
HiPIPs take part in many oxidizing reactions in creatures, and are especially known with photosynthetic anaerobic bacteria, such as Chromatium, and Ectothiorhodospira. 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 cytochrome bc1 complex. Other oxidation reactions HiPIP involved include catalyzing Fe(II) oxidation, being electron donor to reductase and electron accepter for some thiosulfate-oxidizing enzyme.[8]
Referencesedit
^Benning MM, Meyer TE, Rayment I, Holden HM (1994). "Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated from Ectothiorhodospira vacuolata". Biochemistry. 33 (9): 2476–2483. doi:10.1021/bi00175a016. PMID 8117708.
^Stephens, P. J.; Jollie, D. R.; Warshel, A. (1996). "Protein Control of Redox Potentials of Iron−Sulfur Proteins". Chemical Reviews. 96 (7): 2491–2514. doi:10.1021/cr950045w. PMID 11848834.
^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". The Journal of Biological Chemistry. 266 (28): 18660–18667. doi:10.2210/pdb2hip/pdb. PMID 1917989.
^R. H. Holm (2004). "Electron Transfer: Iron-Sulfur Clusters". Comprehensive Coordination Chemistry II. 8: 61-90.
^Perrin, Bradley Scott Jr.; Ichiye, Toshiko (2013). "Identifying sequence determinants of reduction potentials of metalloproteins". Biological Inorganic Chemistry. 18 (6): 599–608. doi:10.1007/s00775-013-1004-6. PMC3723707. PMID 23690205.
^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". Science. 318 (5855): 1464–1468. Bibcode:2007Sci...318.1464D. doi:10.1126/science.1147753. PMID 18048692. S2CID 33046150.
^Ohki, Yasuhiro; Tanifuji, Kazuki; Yamada, Norihiro; Imada, Motosuke; Tajima, Tomoyuki; Tatsumi, Kazujuki (2011). "Synthetic analogues of [Fe4S4(Cys)3(His)] in hydrogenases and [Fe4S4(Cys)4] in HiPIP derived from all-ferric [Fe4S4{N(SiMe3)2}4]". Proceedings of the National Academy of Sciences of the United States of America. 108 (31): 12635–12640. doi:10.1073/pnas.1106472108. PMC3150945. PMID 21768339.
^Valentine, Joan; Bertini, Ivano; Gray, Harry; Stiefel, Edward (2006-10-30). Biological Inorganic Chemistry: Structure and Reactivity (first ed.). University Science Books. ISBN978-1891389436.
External linksedit
PDOC00515 - High potential iron-sulfur proteins in PROSITE
Further readingedit
Nogi T, Fathir I, Kobayashi M, Nozawa T, Miki K (2000). "Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: Thermostability and electron transfer". Proceedings of the National Academy of Sciences. 97 (25): 13561–13566. Bibcode:2000PNAS...9713561N. doi:10.1073/pnas.240224997. PMC17615. PMID 11095707.
This article incorporates text from the public domain Pfam and InterPro: IPR000170
April 12, 2024
high, potential, iron, sulfur, protein, high, potential, iron, sulfur, proteins, hipip, class, iron, sulfur, proteins, they, ferredoxins, that, participate, electron, transfer, photosynthetic, bacteria, well, paracoccus, denitrificans, high, potential, iron, s. High potential iron sulfur proteins HIPIP are a class of iron sulfur proteins 2 They are ferredoxins that participate in electron transfer in photosynthetic bacteria as well as in Paracoccus denitrificans High potential iron sulfur proteinStructure of the oxidized high potential iron sulfur protein 1 IdentifiersSymbolHIPIPPfamPF01355InterProIPR000170PROSITEPDOC00515SCOP21hpi SCOPe SUPFAMOPM superfamily116OPM protein1hpiAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary Contents 1 Structure 2 Fe4S4 clusters 3 Synthetic analogues 4 Biochemical reactions 5 References 6 External links 7 Further readingStructure editThe 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 3 4Fe 4S cluster xxxxxxxxxxxxxxxxxxxCxCxxxxxxxCxxxxxCxxxx C conserved cysteine residue involved in the binding of the 4Fe 4S core 4 Fe4S4 clusters editThe Fe4S4 clusters are abundant cofactors of metalloproteins 5 They participate in electron transfer sequences The core structure for the Fe4S4 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 Fe4S4 clusters are known the ferredoxin Fd family and the high potential iron suflur protein HiPIP family Both HiPIP and Fd share the same resting state Fe4S4 2 which have the same geometric and spectroscopic features Differences arise when it comes to their active state HiPIP forms by oxidation to Fe4S4 3 and Fd is formed by reduction to Fe4S4 Fe4S4 3 for HiPIP oxidation Fe4S4 2 resting state reduction Fe4S4 for Fd displaystyle ce underset for HiPIP Fe4S4 3 lt gt ce oxidation underset resting state Fe4S4 2 lt gt ce reduction underset for Fd Fe4S4 nbsp The different oxidation states are explained by the proteins that combined with the Fe4S4 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 Fe4S4 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 6 Also the unique protein structure and dipolar interactions from peptide and intermolecular water contribute to shielding the Fe4S4 3 cluster from the attack of random outside electron donors which protects itself from hydrolysis Synthetic analogues editHiPIP analogues can be synthesized by ligand exchange reactions of Fe4S4 N SiMe3 2 4 with 4 equiv of thiols HSR as follows Fe4S4 N SiMe3 2 4 4RSH Fe4S4 SR 4 4 HN SiMe3 2The precursor cluster Fe4S4 N SiMe3 2 4 can be synthesized by one pot reaction of FeCl3 NaN SiMe3 2 and NaSH The synthesis of HiPIP analogues can help people understand the factors that cause variety redox of HiPIP 7 Biochemical reactions editHiPIPs take part in many oxidizing reactions in creatures and are especially known with photosynthetic anaerobic bacteria such as Chromatium and Ectothiorhodospira 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 cytochrome bc1 complex Other oxidation reactions HiPIP involved include catalyzing Fe II oxidation being electron donor to reductase and electron accepter for some thiosulfate oxidizing enzyme 8 References edit Benning MM Meyer TE Rayment I Holden HM 1994 Molecular Structure of the Oxidized High Potential Iron Sulfur Protein Isolated from Ectothiorhodospira vacuolata Biochemistry 33 9 2476 2483 doi 10 1021 bi00175a016 PMID 8117708 Stephens P J Jollie D R Warshel A 1996 Protein Control of Redox Potentials of Iron Sulfur Proteins Chemical Reviews 96 7 2491 2514 doi 10 1021 cr950045w PMID 11848834 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 The Journal of Biological Chemistry 266 28 18660 18667 doi 10 2210 pdb2hip pdb PMID 1917989 R H Holm 2004 Electron Transfer Iron Sulfur Clusters Comprehensive Coordination Chemistry II 8 61 90 Perrin Bradley Scott Jr Ichiye Toshiko 2013 Identifying sequence determinants of reduction potentials of metalloproteins Biological Inorganic Chemistry 18 6 599 608 doi 10 1007 s00775 013 1004 6 PMC 3723707 PMID 23690205 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 Science 318 5855 1464 1468 Bibcode 2007Sci 318 1464D doi 10 1126 science 1147753 PMID 18048692 S2CID 33046150 Ohki Yasuhiro Tanifuji Kazuki Yamada Norihiro Imada Motosuke Tajima Tomoyuki Tatsumi Kazujuki 2011 Synthetic analogues of Fe4S4 Cys 3 His in hydrogenases and Fe4S4 Cys 4 in HiPIP derived from all ferric Fe4S4 N SiMe3 2 4 Proceedings of the National Academy of Sciences of the United States of America 108 31 12635 12640 doi 10 1073 pnas 1106472108 PMC 3150945 PMID 21768339 Valentine Joan Bertini Ivano Gray Harry Stiefel Edward 2006 10 30 Biological Inorganic Chemistry Structure and Reactivity first ed University Science Books ISBN 978 1891389436 External links editPDOC00515 High potential iron sulfur proteins in PROSITEFurther reading editNogi T Fathir I Kobayashi M Nozawa T Miki K 2000 Crystal structures of photosynthetic reaction center and high potential iron sulfur protein from Thermochromatium tepidum Thermostability and electron transfer Proceedings of the National Academy of Sciences 97 25 13561 13566 Bibcode 2000PNAS 9713561N doi 10 1073 pnas 240224997 PMC 17615 PMID 11095707 This article incorporates text from the public domain Pfam and InterPro IPR000170 Retrieved from https en wikipedia org w index php title High potential iron sulfur protein amp oldid 1182033771, wikipedia, wiki, book, books, library,
