hsp90 is required for heme binding and activation of apo-neuronal nitric-oxide synthase: geldanamycin-mediated oxidant generation is unrelated to any action of hsp90.

@article{Billecke2002hsp90IR,
  title={hsp90 is required for heme binding and activation of apo-neuronal nitric-oxide synthase: geldanamycin-mediated oxidant generation is unrelated to any action of hsp90.},
  author={Scott S Billecke and Andrew T Bender and Kimon C. Kanelakis and Patrick J. M. Murphy and Ezra R. Lowe and Yasuhiko Kamada and William A B Pratt and Yoichi Osawa},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 23},
  pages={20504-9}
}
It is established that neuronal NO synthase (nNOS) is associated with the chaperone hsp90, although the functional role for this interaction has not been defined. We have discovered that inhibition of hsp90 by radicicol or geldanamycin nearly prevents the heme-mediated activation and assembly of heme-deficient apo-nNOS in insect cells. This effect is concentration-dependent with over 75% inhibition achieved at 20 microm radicicol. The ferrous carbonyl complex of nNOS is not formed when hsp90 is… CONTINUE READING