glutathione disulfide reductase where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain Information on EC 1.8.1.7 -

Information on EC 1.8.1.7 glutathione disulfide reductase BRENDA Enzyme Database reduced oxidized glutathione Glutathione Disulfide an overview Deciphering the mechanism of glutaredoxin catalyzed roGFP2 redox sensing reveals a ternary complex with glutathione for protein disulfide reduction Nature Communications Sigma Aldrich Glutathione Reductase human, CAS 9001 48 3, buffered aqueous solution, 10 units mg protein, recombinant, expressed in E. coli 500 ug Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox active selenolthiol selenenylsulfide formed from the conserved cysteine selenocysteine sequence PNAS Total Glutathione Quantification Kit T419 manual DOJINDO

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