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Structural Analysis of a Ni-Methyl Species in Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis

Year: 2011
Type: article
Abstract: We present the 1.2 Å resolution X-ray crystal structure of a Ni-methyl species that is a proposed catalytic intermediate in methyl-coenzyme M reductase (MCR), the enzyme that catalyzes the biological formation of methane. The methyl group is situated 2.1 Å proximal of the Ni atom of the MCR coenzyme F(430). A rearrangement of the substrate channel has been posited to bring together substrate species, but Ni(III)-methyl formation alone does not lead to any observable structural changes in the channel.
DOI: 10.1021/ja110492p
Authors: Peder E. Cedervall, Mishtu Dey, Xianghui Li, Ritimukta Sarangi, Britt Hedman, Stephen W. Ragsdale, Carrie M. Wilmot
Institutions: University of Minnesota, University of Michigan, Massachusetts Institute of Technology, New England Biolabs (United States), SLAC National Accelerator Laboratory, Stanford Synchrotron Radiation Lightsource
Language: English
Field: Energy
Open Access status: green
Award: G113944070
OpenAlex ID: W2042500927
FWCI: 1.182
Cites: 20
Cited by: 43
Related to: 10