Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: insights into the puzzling difference between unready and ready oxidized inactive states.
Dynamic electrochemical studies, incorporating catalytic voltammetry and detailed potential-step manipulations, provide compelling evidence that the oxidized inactive state of [NiFe]-hydrogenases termed Unready (or Ni-A) contains a product of partial reduction of O(2) that is trapped in the active site.
Lamle
Sophie E
SE
Department of Chemistry, Inorganic Chemistry Laboratory, Oxford University, South Parks Road, Oxford, OX1 3QR, England.
Albracht
Simon P J
SP
Armstrong
Fraser A
FA
D000332:Aerobiosis; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D002841:Chromatiaceae / Q000201:enzymology*; D004563:Electrochemistry; D004789:Enzyme Activation; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology
D001426:Bacterial Proteins; C043296:nickel-iron hydrogenase; D006864:Hydrogenase; D010100:Oxygen