Proton uptake upon anaerobic reduction of the Paracoccus denitrificans cytochrome c oxidase: a kinetic investigation of the K354M and D124N mutants.

@article{Forte2004ProtonUU,
  title={Proton uptake upon anaerobic reduction of the Paracoccus denitrificans cytochrome c oxidase: a kinetic investigation of the K354M and D124N mutants.},
  author={Elena Forte and Francesca Maria Scandurra and Oliver-Matthias H. Richter and Emilio D'Itri and Paolo Sarti and Maurizio Brunori and B. Ludwig and Alessandro Giuffr{\`e}},
  journal={Biochemistry},
  year={2004},
  volume={43 10},
  pages={2957-63}
}
The kinetics and stoichiometry of the redox-linked protonation of the soluble Paracoccus denitrificans cytochrome c oxidase were investigated at pH = 7.2-7.5 by multiwavelength stopped-flow spectroscopy, using the pH indicator phenol red. We compared the wild-type enzyme with the K354M and the D124N subunit I mutants, in which the K- and D-proton-conducting pathways are impaired, respectively. Upon anaerobic reduction by Ru-II hexamine, the wild-type enzyme binds 3.3 +/- 0.6 H(+)/aa(3), i.e… CONTINUE READING

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