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. Th...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2012-07, Vol.109 (29), p.11516-11521
Main Authors: Hexter, Suzannah V, Grey, Felix, Happe, Thomas, Climent, Victor, Armstrong, Fraser A
Format: Article
Language:English
Subjects:
Active sites
Catalysis
catalysts
catalytic activity
Electric current
Electrocatalysis
Electrocatalysts
Electrochemical Techniques - methods
electrochemistry
ELECTROCHEMISTRY: SPECIAL FEATURE
Electrodes
Electron transfer
Electrons
energy metabolism
Energy Metabolism - physiology
Enzymes
Hydrogen
Hydrogen - chemistry
Hydrogenases
Iron
Iron - chemistry
mathematical models
Models, Chemical
Molecular Structure
Nickel
Nickel - chemistry
Oxidation
Oxidoreductases - chemistry
Oxidoreductases - classification
Physical Sciences
platinum
Voltammetry
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1204770109