Fluorescence probing of the function-specific cysteines of rat microsomal NADPH-cytochrome P-450 reductase.

@article{Lee1986FluorescencePO,
  title={Fluorescence probing of the function-specific cysteines of rat microsomal NADPH-cytochrome P-450 reductase.},
  author={J. Lee and L. Kaminsky},
  journal={Biochemical and biophysical research communications},
  year={1986},
  volume={134 1},
  pages={
          393-9
        }
}
  • J. Lee, L. Kaminsky
  • Published 1986
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
Titration of NADPH-cytochrome P-450 reductase with a fluorigenic maleimide suggests that approximately four cysteines are initially accessible and in close proximity to four tryptophans. Perturbation of the cysteines and/or tryptophans results in concomitant decreases in enzymic activity. These cysteines were correlated with functional components by binding studies and subsequent tryptic peptide mapping on the acid mobile phase-reverse phase HPLC. Adenine nucleotides and cytochrome c block… Expand
5 Citations

References

SHOWING 1-10 OF 12 REFERENCES
Some properties of mammalian cardiac cytochrome c1.
Three-dimensional structure of glutathione reductase at 2 A resolution.
...
1
2
...