glutathione reductase substrates where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain 1GRA: SUBSTRATE BINDING AND CATALYSIS
1GRA: SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES The role of glutathione in disulphide bond formation and endoplasmic reticulum generated oxidative stress PMC Deciphering the mechanism of glutaredoxin catalyzed roGFP2 redox sensing reveals a ternary complex with glutathione for protein disulfide reduction Nature Communications Physiological functions of thioredoxin and thioredoxin reductase Arnr 2000 European Journal of Biochemistry Wiley Online Library Glutathione Related Enzymes and Proteins: A Review
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