The Mononuclear Molybdenum Enzymes

被引：517

作者：

Hille, Russ ^{[1
]}

Hall, James ^{[1
]}

Basu, Partha ^{[2
]}

机构：

[1] Univ Calif Riverside, Dept Biochem, Riverside, CA 92521 USA

[2] Duquesne Univ, Dept Chem & Biochem, Pittsburgh, PA 15282 USA

来源：

CHEMICAL REVIEWS | 2014年 / 114卷 / 07期

基金：

美国国家科学基金会;

关键词：

ELECTRON-PARAMAGNETIC-RESONANCE; PERIPLASMIC NITRATE REDUCTASE; DIMETHYL-SULFOXIDE REDUCTASE; OXYGEN-ATOM-TRANSFER; HUMAN SULFITE OXIDASE; LIVER XANTHINE DEHYDROGENASE; RAY-ABSORPTION-SPECTROSCOPY; CARBON-MONOXIDE DEHYDROGENASE; SITE-DIRECTED MUTAGENESIS; PROTEIN FILM VOLTAMMETRY;

D O I：

10.1021/cr400443z

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A study is conducted to discuss the mononuclear molybdenum enzymes. Enzymes containing molybdenum in their active sites have been recognized with more than 50 molybdenum-containing enzymes being purified and biochemically characterized. It is well-established that all molybdenum-containing enzymes other than nitrogenase fall into three large and mutually exclusive families, as exemplified by the enzymes xanthine oxidase, sulfite oxidase, and DMSO reductase. The structures of the three canonical molybdenum centers in their oxidized Mo(VI) states are examined along with that for the pyranopterin cofactor. The active sites of members of the xanthine oxidase family ALSO have an LMoVIOS-(OH) structure with a square-pyramidal coordination geometry.

引用

页码：3963 / 4038

页数：76

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