Electron transfer, oxygen binding, and nitric oxide feedback inhibition in endothelial nitric-oxide synthase.

@article{AbuSoud2000ElectronTO,
  title={Electron transfer, oxygen binding, and nitric oxide feedback inhibition in endothelial nitric-oxide synthase.},
  author={Husam M Abu-Soud and Koji Ichimori and Anthony Presta and Dennis J. Stuehr},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 23},
  pages={17349-57}
}
We studied steps that make up the initial and steady-state phases of nitric oxide (NO) synthesis to understand how activity of bovine endothelial NO synthase (eNOS) is regulated. Stopped-flow analysis of NADPH-dependent flavin reduction showed the rate increased from 0. 13 to 86 s(-1) upon calmodulin binding, but this supported slow heme reduction in the presence of either Arg or N(omega)-hydroxy-l-arginine (0.005 and 0.014 s(-1), respectively, at 10 degrees C). O(2) binding to ferrous eNOS… CONTINUE READING

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