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Issue 39, 2011
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Turning a riboflavin-binding protein into a self-sufficient monooxygenase by cofactor redesign

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Abstract

By cofactor redesign, self-sufficient monooxygenases could be prepared. Tight binding of N-alkylated flavins to riboflavin-binding protein results in the creation of artificial flavoenzymes capable of H2O2-driven enantioselective sulfoxidations. By altering the flavin structure, opposite enantioselectivities could be achieved, in accordance with the binding mode predicted by in silicoflavin-protein docking of the unnatural flavin cofactors. The study shows that cofactor redesign is a viable approach to create artificial flavoenzymes with unprecedented activities.

Graphical abstract: Turning a riboflavin-binding protein into a self-sufficient monooxygenase by cofactor redesign

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Article information


Submitted
06 Jul 2011
Accepted
25 Aug 2011
First published
08 Sep 2011

Chem. Commun., 2011,47, 11050-11052
Article type
Communication

Turning a riboflavin-binding protein into a self-sufficient monooxygenase by cofactor redesign

G. de Gonzalo, C. Smit, J. Jin, A. J. Minnaard and M. W. Fraaije, Chem. Commun., 2011, 47, 11050
DOI: 10.1039/C1CC14039F

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