Kinetic characterization of wild-type and proton transfer-impaired variants of beta-carbonic anhydrase from Arabidopsis thaliana.

@article{Rowlett2002KineticCO,
  title={Kinetic characterization of wild-type and proton transfer-impaired variants of beta-carbonic anhydrase from Arabidopsis thaliana.},
  author={Roger Rowlett and Chingkuang Tu and Melissa M. McKay and Jeffrey R Preiss and Rebecca J Loomis and Katherine A. Hicks and Robb J. Marchione and Jacob A Strong and George S Donovan and J. Edward Chamberlin},
  journal={Archives of biochemistry and biophysics},
  year={2002},
  volume={404 2},
  pages={
          197-209
        }
}
We have cloned and overexpressed a truncated, recombinant form of beta-carbonic anhydrase from Arabidopsis thaliana. The wild-type enzyme and two site-directed variants, H216N and Y212F, have been kinetically characterized both at steady state by stopped-flow spectrophotometry and at chemical equilibrium by (18)O isotope exchange methods. The wild-type enzyme has a maximal k(cat) for CO2 hydration of 320 ms(-1) and is rate limited by proton transfer involving two residues with apparent pK(a… CONTINUE READING

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