Minimal and hybrid hydrogenases are active from archaea

Cell. 2024 Jun 20;187(13):3357-3372.e19. doi: 10.1016/j.cell.2024.05.032. Epub 2024 Jun 11.

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.

Keywords: anaerobic; archaea; eukaryogenesis; hydrogen; hydrogenase.

MeSH terms

  • Archaea* / enzymology
  • Archaea* / genetics
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism
  • Genome, Archaeal
  • Hydrogen* / metabolism
  • Hydrogenase* / chemistry
  • Hydrogenase* / genetics
  • Hydrogenase* / metabolism
  • Iron-Sulfur Proteins / chemistry
  • Iron-Sulfur Proteins / genetics
  • Iron-Sulfur Proteins / metabolism
  • Models, Molecular
  • Phylogeny*
  • Protein Structure, Tertiary

Substances

  • Archaeal Proteins
  • Hydrogen
  • Hydrogenase
  • iron hydrogenase
  • Iron-Sulfur Proteins