Structure of a methyl-coenzyme M reductase from Black Sea mats that oxidize methane anaerobically

Seigo Shima (), Martin Krueger, Tobias Weinert, Ulrike Demmer, Jörg Kahnt, Rudolf K. Thauer and Ulrich Ermler ()
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Seigo Shima: Max Planck Institute for Terrestrial Microbiology, Karl--Frisch-Strasse 10, D-35043 Marburg, Germany
Martin Krueger: Federal Institute for Geosciences and Resources, Stilleweg 2, 30655 Hannover, Germany
Tobias Weinert: Max Planck Institute for Biophysics, Max-von-Laue-Strasse 3, D-60438 Frankfurt, Germany
Ulrike Demmer: Max Planck Institute for Biophysics, Max-von-Laue-Strasse 3, D-60438 Frankfurt, Germany
Jörg Kahnt: Max Planck Institute for Terrestrial Microbiology, Karl--Frisch-Strasse 10, D-35043 Marburg, Germany
Rudolf K. Thauer: Max Planck Institute for Terrestrial Microbiology, Karl--Frisch-Strasse 10, D-35043 Marburg, Germany
Ulrich Ermler: Max Planck Institute for Biophysics, Max-von-Laue-Strasse 3, D-60438 Frankfurt, Germany

Nature, 2012, vol. 481, issue 7379, 98-101

Abstract: The crystal structure of the enzyme MCR from methanogenic archaea shows that it is very similar to that of methanotrophic archaea; the differences observed may tune the enzymes for their respective biological context within the sea mats.

Date: 2012
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DOI: 10.1038/nature10663

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