Characterization of the role of lysine 110 of NADH-cytochrome b5 reductase in the binding and oxidation of NADH by site-directed mutagenesis.

@article{Strittmatter1992CharacterizationOT,
  title={Characterization of the role of lysine 110 of NADH-cytochrome b5 reductase in the binding and oxidation of NADH by site-directed mutagenesis.},
  author={Philipp Strittmatter and Joseph Kittler and John Coghill},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 28},
  pages={20164-7}
}
An expression vector for bovine NADH-cytochrome b5 reductase was used for site-directed mutagenesis of lysine 110, the residue previously implicated in NADH interactions with this flavoprotein. Replacement of this basic residue with an uncharged glutamine resulted in an increase of 3 orders of magnitude in the Km for NADH and a decrease in kcat of an order… CONTINUE READING