Carbon monoxide adducts of KatG and KatG(S315T) as probes of the heme site and isoniazid binding.

@article{LukatRodgers2001CarbonMA,
  title={Carbon monoxide adducts of KatG and KatG(S315T) as probes of the heme site and isoniazid binding.},
  author={Gudrun S Lukat-Rodgers and Nancy L. Wengenack and Frank Rusnak and Kenton R. Rodgers},
  journal={Biochemistry},
  year={2001},
  volume={40 24},
  pages={7149-57}
}
KatG, the catalase peroxidase from Mycobacterium tuberculosis, is important in the activation of the antitubercular drug, isoniazid. About 50% of isoniazid-resistant clinical isolates contain a mutation in KatG wherein the serine at position 315 is substituted with threonine, KatG(S315T). The heme pockets of KatG and KatG(S315T) and their interactions with isoniazid are probed using resonance Raman (rR) spectroscopy to characterize their ferrous CO complexes. Three vibrational modes, C-O and Fe… CONTINUE READING