Redox potentiometry studies of particulate methane monooxygenase: Support for a trinuclear copper cluster active site

被引：116

作者：

Chan, Sunney I. ^{[1
]}

Wang, Vincent C-C

Lai, Jeff C. -H.

Yu, Steve S. -F

Chen, Peter P. -Y

Chen, Kelvin H. -C

Chen, Chang-Li

Chan, Michael K.

机构：

[1] Acad Sinica, Inst Chem, Taipei 11529, Taiwan

[2] Natl Taiwan Univ, Dept Chem, Taipei 106, Taiwan

[3] Ohio State Univ, Dept Chem, Columbus, OH 43210 USA

[4] Ohio State Univ, Dept Biochem, Columbus, OH 43210 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2007年 / 46卷 / 12期

关键词：

bioinorganic chemistry; cluster compounds; copper; EPR spectroscopy; oxidation;

D O I：

10.1002/anie.200604647

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A pocketful of coppers: Redox potentiometry and EPR experiments have confirmed that the active site of the particulate methane monooxygenase (pMMO), a membrane-bound enzyme that hydroxylates methane to methanol under ambient conditions, consists of one trinuclear copper cluster (see picture) and one type 2 copper site, in addition to the dinuclear copper cluster revealed previously by X-ray crystallography. (Figure Presented). © 2007 Wiley-VCH Verlag GmbH & Co. KGaA.

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页码：1992 / 1994

页数：3

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