Diversity of electron-bifurcating CO2-fixing supercomplexes in methanogens.

Pablo San Segundo-Acosta¹, Shunsuke Nomura², Joao Pedro Fernandes-Queiroz², Evgenii Protasov², Jörg Kahnt², Masanori Kaneko^2,3, Georg Hochberg⁴, Seigo Shima⁴, Bonnie J Murphy¹

¹Redox and Metalloprotein Research Group, Max Planck Institute of Biophysics, Frankfurt am Main, Germany.

²Microbial Protein Structure Group, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.

³Geological Survey of Japan, National Institute of Advanced Industrial Science and Technology (AIST), Tokyo, Japan.

⁴Evolutionary Biochemistry Group, Max Planck Institute for Terrestrial Microbiology, Marburg, Germany.

PubMed DOI

Abstract

In the hydrogenotrophic methanogenic pathway, formylmethanofuran dehydrogenase (Fmd) reduces and fixes CO2, driven by low-potential electrons provided by electron-bifurcating heterodisulfide reductase (Hdr) complexed with electron-donating proteins such as Mvh hydrogenase. Here, we report the structure of a C2-symmetric (Mvh-Hdr)2-Fmd4 supercomplex from a Class I methanogen, Methanothermobacter ma…

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