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Journal Article

Three-megadalton complex of methanogenic electron-bifurcating and CO2-fixing enzymes

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Watanabe,  Tomohiro
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Pfeil-Gardiner,  Olivia
Redox and Metalloprotein Research Group, Max Planck Institute of Biophysics, Max Planck Society;

Koch,  Jürgen
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Shima,  Seigo
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Murphy,  Bonnie J.       
Redox and Metalloprotein Research Group, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Watanabe, T., Pfeil-Gardiner, O., Kahnt, J., Koch, J., Shima, S., & Murphy, B. J. (2021). Three-megadalton complex of methanogenic electron-bifurcating and CO2-fixing enzymes. Science, 373(6559), 1151-1156. doi:10.1126/science.abg5550.


Cite as: https://hdl.handle.net/21.11116/0000-0009-282B-B
Abstract
The first reaction of the methanogenic pathway from carbon dioxide (CO2) is the reduction and condensation of CO2 to formyl-methanofuran, catalyzed by formyl-methanofuran dehydrogenase (Fmd). Strongly reducing electrons for this reaction are generated by heterodisulfide reductase (Hdr) in complex with hydrogenase or formate dehydrogenase (Fdh) using a flavin-based electron-bifurcation mechanism. Here, we report enzymological and structural characterizations of Fdh-Hdr-Fmd complexes from Methanospirillum hungatei. The complexes catalyze this reaction using electrons from formate and the reduced form of the electron carrier F420. Conformational changes in HdrA mediate electron bifurcation, and polyferredoxin FmdF directly transfers electrons to the CO2 reduction site, as evidenced by methanofuran-dependent flavin-based electron bifurcation even without free ferredoxin, a diffusible electron carrier between Hdr and Fmd. Conservation of Hdr and Fmd structures suggests that this complex is common among hydrogenotrophic methanogens.