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Science 21 November 1997:
Vol. 278. no. 5342, pp. 1457 - 1462
DOI: 10.1126/science.278.5342.1457
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Reports

Crystal Structure of Methyl-Coenzyme M Reductase: The Key Enzyme of Biological Methane Formation

Ulrich Ermler, * Wolfgang Grabarse, Seigo Shima, Marcel Goubeaud, Rudolf K. Thauer

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 alpha 2beta 2gamma 2 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.

U. Ermler, Max-Planck-Institut für Biophysik, Heinrich-Hoffmann-Strabeta e 7, 60528 Frankfurt, Germany.
W. Grabarse, Max-Planck-Institut für Biophysik, Heinrich-Hoffmann-Strabeta e 7, 60528 Frankfurt, Germany, and Max-Planck-Institut für Terrestrische Mikrobiologie and Laboratorium für Mikrobiologie der Philipps-Universität, Karl-von-Frisch-Strabeta e, 35043 Marburg, Germany.
S. Shima, M. Goubeaud, R. K. Thauer, Max-Planck-Institut für Terrestrische Mikrobiologie and Laboratorium für Mikrobiologie der Philipps-Universität, Karl-von-Frisch-Strabeta e, 35043 Marburg, Germany.
*   To whom correspondence should be addressed.

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