A Nickel-Alkyl Bond in an Inactivated State of the Enzyme Catalyzing Methane Formation

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 M...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2006-05, Vol.45 (22), p.3602-3607
Main Authors: Hinderberger, Dariush, Piskorski, Rafal P., Goenrich, Meike, Thauer, Rudolf K., Schweiger, Arthur, Harmer, Jeffrey, Jaun, Bernhard
Format: Article
Language:English
Subjects:
Alkanesulfonic Acids - chemistry
bioinorganic chemistry
Catalysis
Electron Spin Resonance Spectroscopy
enzymes
EPR spectroscopy
Methane - chemistry
methanogenesis
nickel
Nickel - chemistry
Oxidoreductases - chemistry
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Summary: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.200600366