Spin-state rationale for the peroxo-stabilizing role of the thiolate ligand in superoxide reductase

被引:46
作者
Bukowski, MR
Halfen, HL
van den Berg, TA
Halfen, JA
Que, L
机构
[1] Univ Minnesota, Ctr Met & Biocatalysis, Minneapolis, MN 55455 USA
[2] Univ Minnesota, Dept Chem, Minneapolis, MN 55455 USA
[3] Univ Wisconsin, Dept Chem, Eau Claire, WI 54702 USA
关键词
bioinorganic chemistry; coordination compounds; iron; peroxides; S ligands;
D O I
10.1002/anie.200461527
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Anti-push: The axial thiolate ligand stabilizes high-spin Fe III-OOR species (see picture) such as those found in superoxide reductase. This situation is in contrast to the "push effect" observed in structurally similar low-spin FeIII-OOR systems, including cytochrome P450, which promote O-O bond cleavage. These results show how very similar enzyme-active sites can carry out two very different functions.
引用
收藏
页码:584 / 587
页数:4
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