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thioredoxin glutathione reductase Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways
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thioredoxin glutathione reductase Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways
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Thioredoxin and glutathione reductases ScienceDirect Frontiers Assigning function to active site residues of Schistosoma mansoni thioredoxin glutathione reductase from analysis of transient state reductive half reactions with variant forms of the enzyme Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox active selenolthiol selenenylsulfide formed from the conserved cysteine selenocysteine sequence PNAS GSH glutaredoxin and thioredoxin systems. Yeast contains two gene pairs Download Scientific Diagram
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thioredoxin glutathione reductase Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways
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