title: Turning a riboflavin-binding protein into a self-sufficient monooxygenase by cofactor redesign.
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.
authors: Laboratory of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
authors: Gonzalo
authors: G
authors: de Gonzalo
authors: Christian
authors: C
authors: Smit
authors: Jianfeng
authors: J
authors: Jin
authors: Adriaan J
authors: AJ
authors: Minnaard
authors: Marco W
authors: MW
authors: Fraaije
mesh_terms: D000818:Animals; D040761:Biomimetic Materials / Q000737:chemistry* / Q000378:metabolism*; D002645:Chickens; D015195:Drug Design; D005415:Flavins / Q000737:chemistry* / Q000378:metabolism*; D026901:Membrane Transport Proteins / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D055672:Static Electricity; D013237:Stereoisomerism; D013379:Substrate Specificity; D013454:Sulfoxides / Q000737:chemistry / Q000378:metabolism
chemical_list: D005415:Flavins; D026901:Membrane Transport Proteins; D013454:Sulfoxides; C019079:riboflavin-binding protein; D006899:Mixed Function Oxygenases