共 66 条
Understanding how the thiolate sulfur contributes to the function of the non-heme iron enzyme superoxide reductase
被引:85
作者:

Kovacs, Julie A.
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机构:
Univ Washington, Dept Chem, Seattle, WA 98195 USA Univ Washington, Dept Chem, Seattle, WA 98195 USA

Brines, Lisa M.
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h-index: 0
机构:
Univ Washington, Dept Chem, Seattle, WA 98195 USA Univ Washington, Dept Chem, Seattle, WA 98195 USA
机构:
[1] Univ Washington, Dept Chem, Seattle, WA 98195 USA
关键词:
D O I:
10.1021/ar600059h
中图分类号:
O6 [化学];
学科分类号:
0703 ;
摘要:
Toxic superoxide radicals, generated via adventitious reduction of dioxygen, have been implicated in a number of disease states. The cysteinate-ligated non-heme iron enzyme superoxide reductase (SOR) degrades superoxide via reduction. Biomimetic analogues which provide insight into why nature utilizes a trans-thiolate to promote SOR function are described. Spectroscopic and/or structural characterization of the first examples of thiolate-ligated Fe (III)peroxo complexes provides important benchmark parameters for the identification of biological intermediates. Oxidative addition of superoxide is favored by low redox potentials. The trans influence of the thiolate appears to significantly weaken the FeO peroxo bond, favoring proton-induced release of H2O2 from a high-spin Fe(III)OOH complex.
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页码:501 / 509
页数:9
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