title: The hows and whys of aerobic H2 metabolism.
abstract: The bacterial [NiFe]-hydrogenases have been classified as either 'standard' or 'O2-tolerant' based on their ability to function in the presence of O2. Typically, these enzymes contain four redox-active metal centers: a Ni-Fe-CO-2CN- active site and three electron-transferring Fe-S clusters. Recent research suggests that, rather than differences at the catalytic active site, it is a novel Fe-S cluster electron transfer (ET) relay that controls how [NiFe]-hydrogenases recover from O2 attack. In light of recent structural data and mutagenic studies this article reviews the molecular mechanism of O2-tolerance in [NiFe]-hydrogenases and discusses the biosynthesis of the unique Fe-S relay.
authors.affiliation: Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, Oxford OX1 3QR, UK.
authors.forename: Alison
authors.initials: A
authors.lastname: Parkin
authors.forename: Frank
authors.initials: F
authors.lastname: Sargent
mesh_terms: D000332:Aerobiosis; D006859:Hydrogen / Q000737:chemistry / Q000378:metabolism*; D006864:Hydrogenase / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000378:metabolism; D010100:Oxygen / Q000737:chemistry / Q000378:metabolism
chemical_list: D007506:Iron-Sulfur Proteins; D006859:Hydrogen; C043296:nickel-iron hydrogenase; D006864:Hydrogenase; D010100:Oxygen