Structural basis of enzymatic benzene ring reduction

被引:0
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作者
Tobias Weinert
Simona G Huwiler
Johannes W Kung
Sina Weidenweber
Petra Hellwig
Hans-Joachim Stärk
Till Biskup
Stefan Weber
Julien J H Cotelesage
Graham N George
Ulrich Ermler
Matthias Boll
机构
[1] Max Planck Institute of Biophysics,Department of Analytical Chemistry
[2] Microbiology,Department of Geological Sciences
[3] Faculty of Biology,undefined
[4] University of Freiburg,undefined
[5] Laboratoire de Bioélectrochimie et Spectroscopie,undefined
[6] UMR 7140,undefined
[7] Chimie de la Matière Complexe,undefined
[8] Université de Strasbourg–CNRS,undefined
[9] Helmholtz Centre for Environmental Research UFZ,undefined
[10] Institute of Physical Chemistry,undefined
[11] University of Freiburg,undefined
[12] University of Saskatchewan,undefined
[13] Canadian Light Source,undefined
来源
Nature Chemical Biology | 2015年 / 11卷
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摘要
Structural, spectroscopic and kinetic analyses suggest that class II benzoyl-CoA reductases from anaerobic bacteria use an unusual tungsten cofactor and a conserved histidine to perform a reduction akin to the widely used Birch reduction in organic chemistry.[graphic not available: see fulltext]
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页码:586 / 591
页数:5
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