Mediated electron transfer with P450cin

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ID: 47799
2010
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Abstract
P450cin stereoselectively hydroxylated its natural substrate 1,8-cineole to 2β-hydroxy-1,8-cineole in an electrochemical cell which allowed for substitution of the natural cofactor NADPH by artificial redox mediators. Cobalt sepulchrate, phenosafranine, safranine T, FAD and FMN enabled artificial electron transfer from the platinum electrode to P450cin via the redox partner protein cindoxin. The highest product formation, 6.50±0.60 nmol (product) nmol (P450)−1 min−1 cm−2, was achieved using cobalt sepulchrate. Surprisingly, phenosafranine and safranine T enabled electron transfer even in the absence of NADPH, cindoxin, and cindoxin reductase, thereby illustrating that none of the natural redox partners is needed for product formation. Keywords: Cytochrome P450, Mediator, Cineole, Phenosafranine, Safranine T, Bioelectrocatalysis
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Authors Çekiç, Sevil Zengin;Holtmann, Dirk;Güven, Güray;Mangold, Klaus-Michael;Schwaneberg, Ulrich;Schrader, Jens;
Journal electrochemistry communications
Year 2010
DOI
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http://www.sciencedirect.com/science/article/pii/S1388248110003760
Keywords
chemistry microscopy Microbiology Biology (General) Medicine (General) Medicine Engineering (General). Civil engineering (General) Information technology Industrial electrochemistry Technology Electrical engineering. Electronics. Nuclear engineering Descriptive and experimental mechanics animal culture pathology

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