Characterization of an autoreduction pathway for the [Fe4S4](3+) cluster of mutant Chromatium vinosum high-potential iron proteins. Site-directed mutagenesis studies to probe the role of phenylalanine 66 in defining the stability of the [Fe4S4] center provide evidence for oxidative degradation via a [Fe3S4] cluster
Characterization of an autoreduction pathway for the [Fe4S4](3+) cluster of mutant Chromatium vinosum high-potential iron proteins. Site-directed mutagenesis studies to probe the role of phenylalanine 66 in defining the stability of the [Fe4S4] center provide evidence for oxidative degradation via a [Fe3S4] cluster
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DOI：
10.1021/bi961658l
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发表时间：
1996-11-19
期刊：
影响因子：
2.9
通讯作者：
Cowan, JA
中科院分区：
文献类型：
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作者：
Bian, SM;Hemann, CF;Cowan, JA
已经检查了 Chromatium vinosum 高电位铁硫蛋白中保守芳香残基苯丙氨酸 66 (Phe66Tyr、-Asn、-Cys、-Ser) 的许多点突变，目的是了解该残基的功能作用，极性残基的非保守替换对 [Fe4S4](3+/2+) 簇的中点电位的影响最小，通常
A number of point mutations of the conserved aromatic residue phenylalanine 66 (Phe66Tyr, -Asn, -Cys, -Ser) in Chromatium vinosum high-potential iron sulfur protein have been examined with the aim of understanding the functional role of this residue, Nonconservative replacements with polar residues have a minimal effect on the midpoint potential of the [Fe4S4](3+/2+) cluster, typically