The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Crystal Structure of Methyl-Coenzyme M Reductase: The Key Enzyme of Biological Methane Formation
Abstract
Methyl–coenzyme M reductase (MCR), the enzyme responsible for the microbial formation of methane, is a 300-kilodalton protein organized as a hexamer in an α 2 β 2 γ 2 arrangement. The crystal structure of the enzyme from Methanobacterium thermoautotrophicum , determined at 1.45 angstrom resolution for the inactive enzyme state MCR ox1-silent , reveals that two molecules of the nickel porphinoid coenzyme F 430 are embedded between the subunits α, α′, β, and γ and α′, α, β′, and γ′, forming two identical active sites. Each site is accessible for the substrate methyl–coenzyme M through a narrow channel locked after binding of the second substrate coenzyme B. Together with a second structurally characterized enzyme state (MCR silent ) containing the heterodisulfide of coenzymes M and B, a reaction mechanism is proposed that uses a radical intermediate and a nickel organic compound.
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Cites
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Metadata
- Authors
- Ermler, U., Grabarse, W., Shima, S., Goubeaud, M., & Thauer, R. K.
- Venue
- Science
- Published
- 1997-11-21
- Volume
- 278
- Issue
- 5342
- Pages
- 1457-1462
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2016034432
- Cited by
- 608
- References
- 24
- FWCI
- 19.67
- Type
- journal article
- Language
- en
- Open access
- closed
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- Ermler, U., Grabarse, W., Shima, S., Goubeaud, M., & Thauer, R. K. (1997). Crystal Structure of Methyl-Coenzyme M Reductase: The Key Enzyme of Biological Methane Formation. Science. https://doi.org/10.1126/science.278.5342.1457
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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