Methanogenic heterodisulfide reductase (HdrABC-MvhAGD) uses two noncubane [4Fe-4S] clusters for reduction

Author:

Wagner Tristan1ORCID,Koch Jürgen1,Ermler Ulrich2ORCID,Shima Seigo1ORCID

Affiliation:

1. Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Straße 10, 35043 Marburg, Germany.

2. Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, 60438 Frankfurt am Main, Germany.

Abstract

Methanogenic archaea metabolism Most of the methane on Earth is produced by the metabolism of methanogenic archaea. The final step involves a reaction between methyl-coenzyme M and coenzyme B to give CoM-S-S-CoB and methane. Wagner et al. report a high-resolution structure of the methanogenic heterodisulfide reductase (HdtABC)-[NiFe]-hydrogenase, the enzyme that reduces the disulfide and couples this to the reduction of ferredoxin in an energy-conserving process known as flavin-based electron bifurcation (FBEB) (see the Perspective by Dobbek). The reduced ferredoxin, in turn, drives the first step of methanogenesis. The structure shows how two noncubane [4Fe-4S] clusters perform disulfide cleavage and gives insight into the mechanism of FBEB. Science , this issue p. 699 ; see also p. 642

Funder

Deutsche Forschungsgemeinschaft

Japan Science and Technology Agency

Max-Planck-Gesellschaft

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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