Structural Analysis of a Ni-Methyl Species in Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis
- Michigan
We present the 1.2 {angstrom} 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 {angstrom} proximal of the Ni atom of the MCR coenzyme F{sub 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.
- Research Organization:
- Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
- Sponsoring Organization:
- DOE - BASIC ENERGY SCIENCESOTHER U.S. STATES
- OSTI ID:
- 1029398
- Journal Information:
- J. Am. Chem. Soc., Journal Name: J. Am. Chem. Soc. Journal Issue: (15) ; 04, 2011 Vol. 133; ISSN JACSAT; ISSN 0002-7863
- Country of Publication:
- United States
- Language:
- ENGLISH
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