Abstract
In vitro biocatalysis with cytochrome P450 BM-3 was investigated aiming for the substitution of the expensive natural cofactor NADPH by electrochemistry. The monooxygenase was immobilized on electrodes by entrapment in polypyrrole as a conductive polymer for electrochemically wiring the enzyme. Electropolymerization of pyrrole proved to be a useful means of immobilising an active cytochrome P450 BM-3 mutein on platinum and glassy carbon electrodes without denaturation. Repeatedly sweeping the electric potential between -600 and +600 mV versus Ag/AgCl led to enzymatically-catalysed product formation while in the absence of the enzyme no product formed under otherwise identical conditions.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism*
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Biocatalysis*
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Carbon
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Cytochrome P-450 Enzyme System / isolation & purification
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Cytochrome P-450 Enzyme System / metabolism*
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Electrochemical Techniques / methods*
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Electrodes
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Enzymes, Immobilized / metabolism*
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NADPH-Ferrihemoprotein Reductase / isolation & purification
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NADPH-Ferrihemoprotein Reductase / metabolism*
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Platinum
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Polymers / metabolism*
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Protein Binding
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Pyrroles / metabolism*
Substances
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Bacterial Proteins
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Enzymes, Immobilized
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Polymers
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Pyrroles
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polypyrrole
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Platinum
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Carbon
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Cytochrome P-450 Enzyme System
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NADPH-Ferrihemoprotein Reductase
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flavocytochrome P450 BM3 monoxygenases