Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases.
The extraordinary ability of Fe- and Ni-containing enzymes to catalyze rapid and efficient H(+)/H(2) interconversion--a property otherwise exclusive to platinum metals--has been investigated in a series of experiments combining variable-temperature protein film voltammetry with mathematical modeling. The results highlight important differences between the catalytic performance of [FeFe]-hydrogenases and [NiFe]-hydrogenases and justify a simple model for reversible catalytic electron flow in enzymes and electrocatalysts that should be widely applicable in fields as diverse as electrochemistry, catalysis, and bioenergetics. The active site of [FeFe]-hydrogenases, an intricate Fe-carbonyl complex known as the "H cluster," emerges as a supreme catalyst.
Inorganic Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 3QR, United Kingdom.
Suzannah V
SV
Hexter
Felix
F
Grey
Thomas
T
Happe
Victor
V
Climent
Fraser A
FA
Armstrong
D002384:Catalysis; D055664:Electrochemical Techniques / Q000379:methods*; D004734:Energy Metabolism / Q000502:physiology*; D006859:Hydrogen / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D008956:Models, Chemical; D015394:Molecular Structure; D009532:Nickel / Q000737:chemistry*; D010088:Oxidoreductases / Q000737:chemistry* / Q000145:classification
D009532:Nickel; D006859:Hydrogen; D007501:Iron; D010088:Oxidoreductases