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Journal Article

Structural Basis of Hydrogenotrophic Methanogenesis


Ermler,  Ulrich       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Shima, S., Huang, G., Wagner, T., & Ermler, U. (2020). Structural Basis of Hydrogenotrophic Methanogenesis. Annual Review of Microbiology, 74, 713-733. doi:10.1146/annurev-micro-011720-122807.

Cite as: https://hdl.handle.net/21.11116/0000-0006-E7F3-3
Most methanogenic archaea use the rudimentary hydrogenotrophic pathway-from CO2 and H2 to methane-as the terminal step of microbial biomass degradation in anoxic habitats. The barely exergonic process that just conserves sufficient energy for a modest lifestyle involves chemically challenging reactions catalyzed by complex enzyme machineries with unique metal-containing cofactors. The basic strategy of the methanogenic energy metabolism is to covalently bind C1 species to the C1 carriers methanofuran, tetrahydromethanopterin, and coenzyme M at different oxidation states. The four reduction reactions from CO2 to methane involve one molybdopterin-based two-electron reduction, two coenzyme F420-based hydride transfers, and one coenzyme F430-based radical process. For energy conservation, one ion-gradient-forming methyl transfer reaction is sufficient, albeit supported by a sophisticated energy-coupling process termed flavin-based electron bifurcation for driving the endergonic CO2 reduction and fixation. Here, we review the knowledge about the structure-based catalytic mechanism of each enzyme of hydrogenotrophic methanogenesis.