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glutathione reductase fad

glutathione reductase fad disulfide activity where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain Sigma-Aldrich Glutathione Reductase human oxidized glutathione oxidoreductase Harnessing the Mechanism of Glutathione

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doi: 10.1126/science.abf0529 283 TmerZ.MllerL

glutathione reductase fad disulfide activity where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain Sigma-Aldrich Glutathione Reductase human oxidized glutathione oxidoreductase Harnessing the Mechanism of Glutathione

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glutathione reductase fad disulfide activity where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain Sigma-Aldrich Glutathione Reductase human oxidized glutathione oxidoreductase Harnessing the Mechanism of Glutathione

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glutathione reductase fad disulfide activity where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain Sigma-Aldrich Glutathione Reductase human oxidized glutathione oxidoreductase Harnessing the Mechanism of Glutathione

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glutathione reductase fad disulfide activity where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain Sigma-Aldrich Glutathione Reductase human oxidized glutathione oxidoreductase Harnessing the Mechanism of Glutathione

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glutathione reductase fad disulfide activity where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain Sigma-Aldrich Glutathione Reductase human oxidized glutathione oxidoreductase Harnessing the Mechanism of Glutathione

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glutathione reductase fad disulfide activity where one binds to reduced nicotinamide adenine dinucleotide phosphate (NADPH) and flavin adenine dinucleotide (FAD) the second one is an interface dimerization domain Sigma-Aldrich Glutathione Reductase human oxidized glutathione oxidoreductase Harnessing the Mechanism of Glutathione
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