Crystal Structure of Methyl-Coenzyme M Reductase: The Key Enzyme of Biological Methane Formation
10.1126/science.278.5342.1457
Crossref journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
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.

Bibliography

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.

Authors 5
  1. Ulrich Ermler (first)
  2. Wolfgang Grabarse (additional)
  3. Seigo Shima (additional)
  4. Marcel Goubeaud (additional)
  5. Rudolf K. Thauer (additional)
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  51. We thank D. Vinzenz for crystallization H. Michel for generous support and for reading the manuscript K. Diederichs for reading the manuscript C. Kratky for providing us with coordinates of coenzyme F 430 analogs B. Jaun for discussions and the staff of the Max-Planck beamline at the Deutsches Elektronensynchrotron Hamburg for help during data collection. The cartoon in Fig. 6 was suggested by R. Cammack (King's College London). The coordinates of the MCR ox1-silent structure will be deposited in the Protein Data Bank with the accession number 1mro.
Dates
Type When
Created 23 years ago (July 27, 2002, 5:45 a.m.)
Deposited 1 year, 7 months ago (Jan. 12, 2024, 11:47 p.m.)
Indexed 1 week, 3 days ago (Aug. 12, 2025, 5:54 p.m.)
Issued 27 years, 9 months ago (Nov. 21, 1997)
Published 27 years, 9 months ago (Nov. 21, 1997)
Published Print 27 years, 9 months ago (Nov. 21, 1997)
Funders 0

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@article{Ermler_1997, title={Crystal Structure of Methyl-Coenzyme M Reductase: The Key Enzyme of Biological Methane Formation}, volume={278}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.278.5342.1457}, DOI={10.1126/science.278.5342.1457}, number={5342}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Ermler, Ulrich and Grabarse, Wolfgang and Shima, Seigo and Goubeaud, Marcel and Thauer, Rudolf K.}, year={1997}, month=nov, pages={1457–1462} }