Cooperativity and stoichiometry of substrate binding to the catalytic sites of Escherichia coli F1-ATPase. Effects of magnesium, inhibitors, and mutation.

@article{Weber1994CooperativityAS,
  title={Cooperativity and stoichiometry of substrate binding to the catalytic sites of Escherichia coli F1-ATPase. Effects of magnesium, inhibitors, and mutation.},
  author={Joachim Weber and Susan Wilke-Mounts and Alan E. Senior},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 32},
  pages={20462-7}
}
The fluorescence of residue Trp beta 331 in beta Y331W mutant Escherichia coli F1-ATPase was used as reporter probe to investigate the effects of magnesium ions, inhibitors, and mutation on substrate (ATP) binding stoichiometry and cooperativity. It was found that Mg2+ is required for catalytic site binding cooperativity. In the absence of magnesium, ATP bound to three independent catalytic sites, each with Kd = 76 microM. In contrast, MgATP bound to three catalytic sites with Kd1 < 50 nM, Kd2… CONTINUE READING

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