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EC Number General Information Commentary Reference
Show all pathways known for 1.5.1.41Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.41physiological function in Escherichia coli NAD(P)H:flavin oxidoreductase is part of a multienzyme system that reduces the Fe(III) center of ribonucleotide reductase to Fe(II) and thereby sets the stage for the generation by dioxygen of a free tyrosyl radical required for enzyme activity 392192
Show all pathways known for 1.5.1.41Display the word mapDisplay the reaction diagram Show all sequences 1.5.1.41physiological function the flavin reductase Fre in Escherichia coli reduces the cofactor FMN of MsrQ, that is part of MsrPQ, a distinct type of methionine sulfoxide reductase (Msr) system found in bacteria. It is specifically involved in the repair of periplasmic methionine residues that are oxidized by hypochlorous acid. MsrP is a periplasmic molybdoenzyme that carries out the Msr activity, whereas MsrQ, an integral membrane-bound hemoprotein, acts as the physiological partner of MsrP to provide electrons for catalysis. MsrQ holds a flavin mononucleotide (FMN) cofactor that occupies the site where a second heme binds in other members of the FDR superfamily on the cytosolic side of the membrane. EPR spectroscopy indicates that the FMN cofactor can accommodate a radical semiquinone species. The cytosolic flavin reductase Fre has previously been shown to reduce the MsrQ heme. Fre uses the FMN MsrQ cofactor as a substrate to catalyze the electron transfer from cytosolic NADH to the heme. Formation of a specific complex between MsrQ and Fre favors this unprecedented mechanism, which most likely involves transfer of the reduced FMN cofactor from the Fre active site to MsrQ 763806
Results 1 - 2 of 2