publication . Article . Other literature type . 2015

[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation

John Peters;
  • Published: 01 Jun 2015
Abstract
AbstractThe [FeFe]- and [NiFe]-hydrogenases catalyze the formal interconversion between hydrogen and protons and electrons, possess characteristic non-protein ligands at their catalytic sites and thus share common mechanistic features. Despite the similarities between these two types of hydrogenases, they clearly have distinct evolutionary origins and likely emerged from different selective pressures. [FeFe]-hydrogenases are widely distributed in fermentative anaerobic microorganisms and likely evolved under selective pressure to couple hydrogen production to the recycling of electron carriers that accumulate during anaerobic metabolism. In contrast, many [NiFe]...
Subjects
free text keywords: Hydrogen oxidation, Proton reduction, Bifurcation, Iron-sulfur, Carbon monoxide, Cyanide, Cell Biology, Molecular Biology, Hydrogen production, Chemistry, Biochemistry, Hydrogenase, chemistry.chemical_compound, Ligand, Biogenesis, Hydrogen, chemistry.chemical_element, Catalysis, Bioinorganic chemistry
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publication . Article . Other literature type . 2015

[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation

John Peters;