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  Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation

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, 278(5342), 1457-1462. doi:10.1126/science.278.5342.1457.

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 Creators:
Ermler, Ulrich1, Author           
Grabarse, Wolfgang1, 2, Author           
Shima, Seigo2, 3, Author
Goubeaud, Marcel 2, 3, Author
Thauer, Rudolf K. 2, 3, Author
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Max-Planck-Institut für Terrestrische Mikrobiologie and Laboratorium für Mikrobiologie der Philipps-Universität, Karl-von-Frisch-Straβe, 35043 Marburg, Germany., ou_persistent22              
3Laboratorium für Mikrobiologie der Philipps-Universität, Karl-von-Frisch-Straβe, 35043 Marburg, Germany, ou_persistent22              

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 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 α2β2γ2 arrangement. The crystal structure of the enzyme from Methanobacterium thermoautotrophicum, determined at 1.45 angstrom resolution for the inactive enzyme state MCRox1-silent, reveals that two molecules of the nickel porphinoid coenzyme F430 are embedded between the subunits alpha, alpha', beta, and gamma and alpha', alpha, beta', and gamma', 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 (MCRsilent) 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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Language(s): eng - English
 Dates: 1997-11-21
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1126/science.278.5342.1457
PMID: 9367957
 Degree: -

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Title: Science
  Other : Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 278 (5342) Sequence Number: - Start / End Page: 1457 - 1462 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1