Design of a minimal di-nickel hydrogenase peptide.
Journal
Science advances
ISSN: 2375-2548
Titre abrégé: Sci Adv
Pays: United States
ID NLM: 101653440
Informations de publication
Date de publication:
10 03 2023
10 03 2023
Historique:
entrez:
10
3
2023
pubmed:
11
3
2023
medline:
15
3
2023
Statut:
ppublish
Résumé
Ancestral metabolic processes involve the reversible oxidation of molecular hydrogen by hydrogenase. Extant hydrogenase enzymes are complex, comprising hundreds of amino acids and multiple cofactors. We designed a 13-amino acid nickel-binding peptide capable of robustly producing molecular hydrogen from protons under a wide variety of conditions. The peptide forms a di-nickel cluster structurally analogous to a Ni-Fe cluster in [NiFe] hydrogenase and the Ni-Ni cluster in acetyl-CoA synthase, two ancient, extant proteins central to metabolism. These experimental results demonstrate that modern enzymes, despite their enormous complexity, likely evolved from simple peptide precursors on early Earth.
Identifiants
pubmed: 36897954
doi: 10.1126/sciadv.abq1990
pmc: PMC10005181
doi:
Substances chimiques
Nickel
7OV03QG267
Hydrogenase
EC 1.12.7.2
Protons
0
Hydrogen
7YNJ3PO35Z
Peptides
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
eabq1990Subventions
Organisme : NIGMS NIH HHS
ID : T32 GM135141
Pays : United States
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