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Minimal and hybrid hydrogenases are active from archaea. | LitMetric

AI Article Synopsis

  • Microbial hydrogen cycling is critical for the variety and function of anoxic ecosystems, traditionally linked to [FeFe] hydrogenases found in bacteria and eukaryotes.
  • Recent research shows that anaerobic archaea also possess diverse and active [FeFe] hydrogenases, indicating a broader evolutionary history than previously understood.
  • The study reveals new metabolic adaptations in archaea, introduces a simple hydrogenase in DPANN archaea, and uncovers hybrid hydrogenases formed by mixing [FeFe] and [NiFe] types, suggesting a complex evolutionary relationship between these enzyme groups.

Article Abstract

Microbial hydrogen (H) 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 H-producing Asgard archaeon cultures. We report an ultraminimal hydrogenase in DPANN archaea that binds the catalytic H-cluster and produces H. 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 H catalysts for biotechnological development, and a surprisingly intertwined evolutionary history between the two major H-metabolizing enzymes.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11216029PMC
http://dx.doi.org/10.1016/j.cell.2024.05.032DOI Listing

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