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Architecture of the 8 MDa Hdr-Vhu-Fwd super-assembly in class I methanogens.
Nature, DOI: 10.1038/s41586-026-10744-9 (2026)
Methanogens are central to global carbon cycling and among the largest biological sources of methane, a potent greenhouse gas1. At the heart of their energy metabolism lies the Hdr-Vhu-Fwd super-assembly, which couples H2 oxidation with CO2 reduction through flavin-based electron bifurcation. Here we present the cryogenic electron microscopy structure of the Hdr-Vhu-Fwd super-assembly from Methanococcus maripaludis, revealing an 8 MDa complex comprising 252 polypeptide chains and over 600 redox cofactors. Cryo-electron tomography further support that this super-assembly forms an intact structure within the cytoplasm of intact cells. This architecture comprises two hexameric HdrABC-Vhu rings linked by a tetrameric FwdF core, forming a continuous, circular electron chain. In this unique arrangement, 12 polyferredoxin subunits (VhuB) connect the Vhu-Hdr and Fwd complexes, thereby coupling electron bifurcation with CO2 reduction and directly linking the last and the first step of methanogenesis. Moreover, we identify a modular variant of the complex in which the [NiFe]-hydrogenase Vhu is substituted by tungsten-containing formate dehydrogenase (FdhAB), indicating flexible integration of electron-input modules facilitating metabolic adaptation under diverse environmental conditions2. Analysis of the taxonomic distribution reveals that this architecture is specific to class I methanogens and is distinct from the smaller Hdr-Fmd complex of class II3. Together, our study reveals that the the Hdr-Vhu-Fwd super-assembly has a modular and adaptable bioenergetic assembly, suggesting a lineage-specific architecture to adapt to diverse anaerobic niches.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Heterodisulfide Reductase; Methanobacterium-thermoautotrophicum; Electron Bifurcation; Protein; Tomography; Selenium; Formate; Pathway; Binding; Genome
ISSN (print) / ISBN
0028-0836
e-ISSN
1476-4687
Journal
Nature
Publisher
Nature Publishing Group
Publishing Place
London
Reviewing status
Peer reviewed
Institute(s)
Cryo-EM facility (CEMP)
Grants
Philipps-Universitat Marburg
German Research Foundation
EMBO postdoctoral fellowship
Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy (Microbes-for-Climate (M4C) Cluster of Excellence, Synmikro, Marburg, Germany)
European Union's Horizon 2020 research and innovation programme
Philipps-Universitat Marburg
German Research Foundation
EMBO postdoctoral fellowship
Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy (Microbes-for-Climate (M4C) Cluster of Excellence, Synmikro, Marburg, Germany)
European Union's Horizon 2020 research and innovation programme