Kinetic and spectroscopic studies of the molybdenum-copper CO dehydrogenase from Oligotropha carboxidovorans.

@article{Zhang2010KineticAS,
  title={Kinetic and spectroscopic studies of the molybdenum-copper CO dehydrogenase from Oligotropha carboxidovorans.},
  author={Bo Zhang and Craig F. Hemann and R. F. Hille},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 17},
  pages={12571-8}
}
Carbon monoxide dehydrogenase from the aerobic bacterium Oligotropha carboxidovorans catalyzes the oxidation of CO to CO(2), yielding two electrons and two H(+). The steady-state kinetics of the enzyme exhibit a pH optimum of 7.2 with a k(cat) of 93.3 s(-1) and K(m) of 10.7 microM at 25 degrees C. k(red) for the reductive half-reaction agrees well with k(cat) and exhibits a similar pH optimum, indicating that the rate-limiting step of overall turnover is likely in the reductive half-reaction… CONTINUE READING