Characterization of the flavoprotein domain of gp91phox which has NADPH diaphorase activity.

@article{Han2001CharacterizationOT,
  title={Characterization of the flavoprotein domain of gp91phox which has NADPH diaphorase activity.},
  author={Catherine H Han and Yukio Nisimoto and Siew Hwee Lee and Eric T. Kim and J. David Lambeth},
  journal={Journal of biochemistry},
  year={2001},
  volume={129 4},
  pages={513-20}
}
A series of truncated forms of gp91phox were expressed in Escherichia coli in which the N-terminal hydrophobic transmembrane region was replaced with a portion of the highly soluble bacterial protein thioredoxin. TRX-gp91phox (306-569), which contains the putative FAD and NADPH binding sites, showed weak NADPH-dependent NBT (nitroblue tetrazolium) reductase activity, whereas TRX-gp91phox (304-423) and TRX-gp91phox (424-569) were inactive. Activity saturated at about a 1:1 molar ratio of FAD to… CONTINUE READING