IR spectroelectrochemical study of the binding of carbon monoxide to the active site of Desulfovibrio fructosovorans Ni-Fe hydrogenase

@article{Lacey2001IRSS,
  title={IR spectroelectrochemical study of the binding of carbon monoxide to the active site of Desulfovibrio fructosovorans Ni-Fe hydrogenase},
  author={Antonio L. de Lacey and Christian H Stadler and Victor Manuel Fernandez and Claude E. Hatchikian and Hua-Jun Fan and Shuhua Li and Michael B. Hall},
  journal={JBIC Journal of Biological Inorganic Chemistry},
  year={2001},
  volume={7},
  pages={318-326}
}
The binding of carbon monoxide, a competitive inhibitor of many hydrogenases, to the active site of Desulfovibrio fructosovorans hydrogenase has been studied by infrared spectroscopy in a spectroelectrochemical cell. Direct evidence has been obtained of which redox states of the enzyme can bind extrinsic CO. Redox states A, B and SU do not bind extrinsic CO; only after reductive activation of the hydrogenase can CO bind to the active site. Two states with bound extrinsic CO can be distinguished… CONTINUE READING