Human erythrocyte glutathione reductase: chemical mechanism and structure of the transition state for hydride transfer.

@article{Sweet1991HumanEG,
  title={Human erythrocyte glutathione reductase: chemical mechanism and structure of the transition state for hydride transfer.},
  author={W L Sweet and John S Blanchard},
  journal={Biochemistry},
  year={1991},
  volume={30 35},
  pages={
          8702-9
        }
}
Kinetic parameters and primary deuterium kinetic isotope effects for NADH and five pyridine nucleotide substrates have been determined at pH 8.1 for human erythrocyte glutathione reductase. DV/KNADH and DV are equal to 1.4 and are pH independent below pH 8.1, but DV decreases to 1.0 at high pH as a group exhibiting a pK of 8.6 is deprotonated. This result suggests that as His-467' is deprotonated, the rate of the isotopically insensitive oxidative half-reaction is specifically decreased and… CONTINUE READING