glutathione reductase molecular structure Differences in active site geometry of human (PDB RCSB PDB - 3GRS: REFINED

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

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 +

Microbiol Spectr 10(2):e0067222

People with immune compromise , chronic illness, or malnutrition

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)

doi:10.4161/psb.6.8.16253 Dourado DF, Fernandes PA, Mannervik B, Ramos MJ (2010) Glutathione transferase A1-1: catalytic importance of arginine 15