Kinetics of K+ Occlusion by the Phosphoenzyme of the Na+,K+ -ATPase

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2011
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Myers, Sian L.
Cornelius, Flemming
Clarke, Ronald J.
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Biophysical Journal ; 100 (2011), 1. - pp. 70-79. - ISSN 0006-3495. - eISSN 1542-0086
Abstract
Investigations of K+-occlusion by the phosphoenzyme of Na+,K+-ATPase from shark rectal gland and pig kidney by stopped-flow fluorimetry reveal major differences in the kinetics of the two enzymes. In the case of the pig enzyme, a single K+-occlusion step could be resolved with a rate constant of 342 (±26) s−1. However, in the case of the shark enzyme, two consecutive K+-occlusions were detected with rate constants of 391 (±19) s−1 and 48 (±2) s−1 at 24°C and pH 7.4. A conformational change of the phosphoenzyme associated with K+-occlusion is, thus, the major rate-determining step of the shark enzyme under saturating concentrations of all substrates, whereas for the pig enzyme the major rate-determining step under the same conditions is the E2 → E1 transition and its associated K+ deocclusion and release to the cytoplasm. The differences in rate constants of the K+ occlusion reactions of the two enzymes are paralleled by compensating changes to the rate constant for the E2 → E1 transition, which explains why the differences in the enzymes' kinetic behaviors have not previously been identified.
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570 Biosciences, Biology
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ISO 690MYERS, Sian L., Flemming CORNELIUS, Hans-Jürgen APELL, Ronald J. CLARKE, 2011. Kinetics of K+ Occlusion by the Phosphoenzyme of the Na+,K+ -ATPase. In: Biophysical Journal. 100(1), pp. 70-79. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1016/j.bpj.2010.11.038
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@article{Myers2011Kinet-7976,
  year={2011},
  doi={10.1016/j.bpj.2010.11.038},
  title={Kinetics of K+ Occlusion by the Phosphoenzyme of the Na+,K+ -ATPase},
  number={1},
  volume={100},
  issn={0006-3495},
  journal={Biophysical Journal},
  pages={70--79},
  author={Myers, Sian L. and Cornelius, Flemming and Apell, Hans-Jürgen and Clarke, Ronald J.}
}
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