@article{Peinelt2002Kinet-6787,
  year={2002},
  doi={10.1016/S0006-3495(02)75384-8},
  title={Kinetics of the Ca2+, H+, and Mg2+ interaction with the ion-binding sites of the SR Ca-ATPase},
  number={1},
  volume={82},
  issn={0006-3495},
  journal={Biophysical Journal},
  pages={170--181},
  author={Peinelt, Christine and Apell, Hans-Jürgen}
}

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    <dcterms:title>Kinetics of the Ca2+, H+, and Mg2+ interaction with the ion-binding sites of the SR Ca-ATPase</dcterms:title>
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    <dcterms:bibliographicCitation>First publ. in: Biophysical Journal 82 (2002), pp. 170-181</dcterms:bibliographicCitation>
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    <dc:contributor>Apell, Hans-Jürgen</dc:contributor>
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    <dcterms:abstract xml:lang="deu">Electrochromic styryl dyes were used to investigate mutually antagonistic effects of Ca2+ and H+ on binding of the other ion in the E1 and P-E2 states of the SR Ca-ATPase. On the cytoplasmic side of the protein in the absence of Mg2+ a strictly competitive binding sequence, H2E1 ↔ HE1 ↔ E1 ↔ CaE1 ↔ Ca2E1, was found with two Ca2+ ions bound cooperatively. The apparent equilibrium dissociation constants were in the order of K1/2(2 Ca) = 34 nM, K1/2(H) = 1 nM and K1/2(H2) = 1.32 µM. Up to 2 Mg2+ ions were also able to enter the binding sites electrogenically and to compete with the transported substrate ions (K1/2(Mg) = 165 µM, K1/2(Mg2) = 7.4 mM). In the P-E2 state, with binding sites facing the lumen of the sarcoplasmatic reticulum, the measured concentration dependence of Ca2+ and H+ binding could be described satisfactorily only with a branched reaction scheme in which a mixed state, P-E2CaH, exists. From numerical simulations, equilibrium dissociation constants could be determined for Ca2+ (0.4 mM and 25 mM) and H+ (2 µM and 10 µM). These simulations reproduced all observed antagonistic concentration dependences. The comparison of the dielectric ion binding in the E1 and P-E2 conformations indicates that the transition between both conformations is accompanied by a shift of their (dielectric) position.</dcterms:abstract>
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