glutathione reductase molecular structure Differences in active site geometry of human (PDB Glutathione | C10H17N3O6S | CID

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Unravelling cadmium toxicity and tolerance in plants: insight into regulatory mechanisms

The first spectrum captured reflects spectral perturbation consistent with the binding of NADPH adjacent to the flavin without evidence of NADPH oxidation or flavin reduction

As it was previously reported, NADP + must dissociate from the active site prior to deprotonation of the C159 residue that forms the thiolate-FAD charge transfer complex, implicating roles for Y296 in the efficiency of reduction and in the dissociation of NADP +

When corrected for the fraction reduced, the extinction coefficient of this second charge transfer band is estimated to be 1100 M 1 cm 1 at 680 nm (dashed spectrum in Figure 3A inset)