Solid state NMR studies of hydrogen bonding in a citrate synthase inhibitor complex.

@article{Gu1999SolidSN,
  title={Solid state NMR studies of hydrogen bonding in a citrate synthase inhibitor complex.},
  author={Zhiyong Gu and Dale G. Drueckhammer and Linda Kurz and Keliang Liu and Darrin P Martin and Ann McDermott},
  journal={Biochemistry},
  year={1999},
  volume={38 25},
  pages={8022-31}
}
The ionization state and hydrogen bonding environment of the transition state analogue (TSA) inhibitor, carboxymethyldethia coenzyme A (CMX), bound to citrate synthase have been investigated using solid state NMR. This enzyme-inhibitor complex has been studied in connection with the postulated contribution of short hydrogen bonds to binding energies and enzyme catalysis: the X-ray crystal structure of this complex revealed an unusually short hydrogen bond between the carboxylate group of the… CONTINUE READING