Details zur Publikation |
| Kategorie | Textpublikation |
| Referenztyp | Zeitschriften |
| DOI | 10.1038/s41586-026-10744-9 |
Lizenz  |
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| Titel (primär) | Architecture of the 8 MDa Hdr–Vhu–Fwd super-assembly in class I methanogens |
| Autor | Paul, S.; Pascoa, T.C.; Klamke, M.A.; Bohn, S.; Abendroth, F.; Deobald, D.
; Vázquez, O. |
| Quelle | Nature |
| Erscheinungsjahr | 2026 |
| Department | MEB |
| Sprache | englisch |
| Topic | T7 Bioeconomy |
| Supplements | Supplement 1 Supplement 2 Supplement 3 |
| Abstract |
Methanogens
are central to global carbon cycling and among the largest biological sources
of methane, a potent greenhouse gas. 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 conditions. 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 II. 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. |
| Paul, S., Pascoa, T.C., Klamke, M.A., Bohn, S., Abendroth, F., Deobald, D., Vázquez, O. (2026): Architecture of the 8 MDa Hdr–Vhu–Fwd super-assembly in class I methanogens Nature 10.1038/s41586-026-10744-9 |
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