Three-megadalton complex of methanogenic electron-bifurcating and CO 2 -fixing enzymes

Author:

Watanabe Tomohiro1ORCID,Pfeil-Gardiner Olivia2ORCID,Kahnt Jörg3,Koch Jürgen1,Shima Seigo1ORCID,Murphy Bonnie J.2ORCID

Affiliation:

1. Microbial Protein Structure Group, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany.

2. Redox and Metalloprotein Research Group, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany.

3. Core Facility for Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, 35043 Marburg, Germany.

Abstract

Methanogenesis megacomplex An important first step in methanogenesis is the conversion of carbon dioxide to a reduced one-carbon formyl unit that is a substrate for downstream steps. This reaction is catalyzed by a complex of enzymes, including components for oxidizing hydrogen or formate and splitting two electrons along different energetic paths. Watanabe et al . carefully purified and prepared anaerobic cryo–electron microscopy samples of the enzyme complex responsible, resulting in a three-megadalton hexameric structure at 3- to 3.5-ångström resolution. The arrangement of iron–sulfur cofactors provides an explanation for how electron bifurcation is coupled to large protein motions, which are expected from the multiple conformational states present. —MAF

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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