最小限のジニッケル水素化酵素ペプチドの設計と水素産生能の実証
Hydrogenase enzymes catalyze the reversible oxidation of molecular hydrogen and are central to ancestral metabolic pathways. Modern hydrogenases are structurally elaborate, requiring hundreds of amino acids and multiple cofactors. In this study, researchers engineered a 13-amino acid nickel-binding peptide that reliably generates molecular hydrogen from protons across a broad range of conditions. Structural characterization revealed that the peptide assembles a di-nickel cluster analogous to the Ni-Fe cluster found in [NiFe] hydrogenase and the Ni-Ni cluster in acetyl-CoA synthase—both ancient metabolic proteins. These findings support the hypothesis that the complex enzymes of modern organisms descended from simple peptide precursors present on early Earth, providing experimental evidence for a minimal catalytic scaffold sufficient for hydrogen production.
A 13-amino acid nickel-binding peptide self-assembles into a di-nickel cluster structurally analogous to the Ni-Fe active site of [NiFe] hydrogenase, enabling catalytic reduction of protons to molecular hydrogen under varied conditions.
This is basic research at the cellular or molecular level. For human application, inhalation is the most promising delivery route, but inhalation carries explosion risk and concentration matters (empirical LFL of 10%; high-concentration devices are not recommended).
See also:
https://h2-papers.org/en/papers/36897954