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Dependence of the rates of dissolution of the Fe4S4 clusters of Chromatium vinosum high-potential iron protein and ferredoxin on cluster oxidation state.
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Oxidation-reduction properties of Chromatium vinosum high potential iron-sulfur protein.
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The role of histidine-42 in the oxidation-reduction mechanism of Chromatium vinosum high potential iron-sulfur protein.
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Cluster characterization in iron-sulfur proteins by magnetic circular dichroism.
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Kinetics of oxidation and reduction of high-potential iron-sulfur proteins with nonphysiological reactants.
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Formation of super-reduced Chromatium high-potential iron--sulphur protein in aqueous solution by pulse radiolysis.
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Experimental evidence for the role of buried polar groups in determining the reduction potential of metalloproteins: the S79P variant of Chromatium vinosum HiPIP.
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Kinetic study of the dissolution of Fe4S4(2-)-cluster core ions of ferredoxins and high potential iron protein.
Biochemistry. 1977 Jun 28;16(13):3024-9. doi: 10.1021/bi00632a033.
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Protein control of iron-sulfur cluster redox potentials.
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Characterization of [4Fe-4S]-containing and cluster-free forms of Streptomyces WhiD.
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Role of aromatic residues in stabilization of the [Fe4S4] cluster in high-potential iron proteins (HiPIPs): physical characterization and stability studies of Tyr-19 mutants of Chromatium vinosum HiPIP.
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本文引用的文献
1
Iron-sulfur clusters II: Kinetics of ligand exchange studied on a water-soluble Fe(4)S(4)(SR)(4) cluster.
Proc Natl Acad Sci U S A. 1975 Jul;72(7):2478-82. doi: 10.1073/pnas.72.7.2478.
2
The Acid-Base Properties, Hydrolytic Mechanism, and Susceptibility to O(2) Oxidation of Fe(4)S(4)(SR)(4) Clusters.
Proc Natl Acad Sci U S A. 1975 Jan;72(1):231-4. doi: 10.1073/pnas.72.1.231.
3
Chemical characterization of high potential iron proteins from Chromatium and Rhodopseudomonas gelatinosa.
Biochim Biophys Acta. 1967 Jun 27;140(2):291-311. doi: 10.1016/0005-2795(67)90470-9.
4
Determination of oxidation-reduction potentials by spectropolarimetric titration: application to several iron-sulfur proteins.
Arch Biochem Biophys. 1974 May;162(1):301-9. doi: 10.1016/0003-9861(74)90129-5.
5
A comparison of Fe 4 S 4 clusters in high-potential iron protein and in ferredoxin.
Proc Natl Acad Sci U S A. 1972 Dec;69(12):3526-9. doi: 10.1073/pnas.69.12.3526.
6
Comparison of oxidation-reduction site geometries in oxidized and reduced Chromatium high potential iron protein and oxidized Peptococcus aerogenes ferredoxin.
J Biol Chem. 1974 Oct 10;249(19):6339-46.
7
Letter: Theoretical model for the 4-Fe active sites in oxidized ferredoxin and reduced "high-potential" proteins. Electronic structure of the analogue [Fe4S4(SCH3)4]2-.
J Am Chem Soc. 1975 Oct 29;97(22):6596-8. doi: 10.1021/ja00855a062.
8
NH---S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein.
Proc Natl Acad Sci U S A. 1975 Dec;72(12):4854-8. doi: 10.1073/pnas.72.12.4854.
9
Kinetic study of the dissolution of Fe4S4(2-)-cluster core ions of ferredoxins and high potential iron protein.
Biochemistry. 1977 Jun 28;16(13):3024-9. doi: 10.1021/bi00632a033.
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