Minimal and hybrid hydrogenases are active from archaea
Greening, C.; Cabotaje, P.R.; Valentin A., L.E.; Leung, P.M.; Land, H.; Rodrigues-Oliveira, T.; Ponce-Toledo, R.I.; Senger, M.; Klamke, M.A.; Milton, M.; Lappan, R.; Mullen, S.; West-Roberts, J.; Mao, J.; Song, J.; Schoelmerich, M.; Stairs, C.W.; Schleper, C.; Grinter, R.; Spang, A.; Banfield, J.F.; Berggren, G. (2024). Minimal and hybrid hydrogenases are active from archaea. Cell 187(13): 3357-3372.e19. https://dx.doi.org/10.1016/j.cell.2024.05.032
In: Cell. Cell Press: Cambridge. ISSN 0092-8674; e-ISSN 1097-4172, more
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| Author keywords |
archaea; hydrogen; hydrogenase; anaerobic; eukaryogenesis |
| Abstract |
Microbial hydrogen (H2) cycling underpins the diversity and functionality of diverse anoxic ecosystems. Among the three evolutionarily distinct hydrogenase superfamilies responsible, [FeFe] hydrogenases were thought to be restricted to bacteria and eukaryotes. Here, we show that anaerobic archaea encode diverse, active, and ancient lineages of [FeFe] hydrogenases through combining analysis of existing and new genomes with extensive biochemical experiments. [FeFe] hydrogenases are encoded by genomes of nine archaeal phyla and expressed by H2-producing Asgard archaeon cultures. We report an ultraminimal hydrogenase in DPANN archaea that binds the catalytic H-cluster and produces H2. Moreover, we identify and characterize remarkable hybrid complexes formed through the fusion of [FeFe] and [NiFe] hydrogenases in ten other archaeal orders. Phylogenetic analysis and structural modeling suggest a deep evolutionary history of hybrid hydrogenases. These findings reveal new metabolic adaptations of archaea, streamlined H2 catalysts for biotechnological development, and a surprisingly intertwined evolutionary history between the two major H2-metabolizing enzymes. |
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