A nickel-alkyl bond in an inactivated state of the enzyme catalyzing methane formation

被引：34

作者：

Hinderberger, Dariush

Piskorski, Rafal R.

Goenrich, Meike

Thauer, Rudolf K.

Schweiger, Arthur

Harmer, Jeffrey ^{[1
]}

Jaun, Bernhard

机构：

[1] ETH, Dept Chem & Appl Biosci, Phys Chem Lab, CH-8093 Zurich, Switzerland

[2] ETH, Dept Chem & Appl Biosci, Organ Chem Lab, CH-8093 Zurich, Switzerland

[3] Max Planck Inst Terr Microbiol, Dept Biochem, D-35043 Marburg, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2006年 / 45卷 / 22期

关键词：

bioinorganic chemistry; enzymes; EPR spectroscopy; methanogenesis; nickel;

D O I：

10.1002/anie.200600366

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Chemical Equation Presented) The spin reveals all: Electron paramagnetic resonance spectroscopy reveals the formation of a nickel-alkyl bond in the active site of methyl-coenzyme M reductase (MCR), the key enzyme of methanogenesis, when active MCRred1 reacts with the irreversible inhibitor 3-bromopropane sulfonate to form the MCRBPS species. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.

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页码：3602 / 3607

页数：6

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