Turning a riboflavin-binding protein into a self-sufficient monooxygenase by cofactor redesign |
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Authors: | de Gonzalo Gonzalo Smit Christian Jin Jianfeng Minnaard Adriaan J Fraaije Marco W |
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Institution: | Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands. |
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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 H(2)O(2)-driven enantioselective sulfoxidations. By altering the flavin structure, opposite enantioselectivities could be achieved, in accordance with the binding mode predicted by in silico flavin-protein docking of the unnatural flavin cofactors. The study shows that cofactor redesign is a viable approach to create artificial flavoenzymes with unprecedented activities. |
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