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Protonation and hydrogen bonding of C<sup>2+</sup> site residues in the E2P phosphoenzyme intermediate of Sarcoplasmic Reticulum C<sup>2+</sup>-ATPase studied by a combination of infrared spectroscopy and electrostatic calculations

Protonation and hydrogen bonding of C2+ site residues in the E2P phosphoenzyme intermediate of Sarcoplasmic Reticulum C2+-ATPase studied by a combination of infrared spectroscopy and electrostatic calculations

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ANDERSSON, Julia, Karin HAUSER, Eeva-Liisa KARJALAINEN, Andreas BARTH, 2008. Protonation and hydrogen bonding of C2+ site residues in the E2P phosphoenzyme intermediate of Sarcoplasmic Reticulum C2+-ATPase studied by a combination of infrared spectroscopy and electrostatic calculations. In: Biophysical Journal. 94(2), pp. 600-611. ISSN 0006-3495. eISSN 1542-0086. Available under: doi: 10.1529/biophysj.107.114033

@article{Andersson2008-01-15Proto-17546, title={Protonation and hydrogen bonding of C2+ site residues in the E2P phosphoenzyme intermediate of Sarcoplasmic Reticulum C2+-ATPase studied by a combination of infrared spectroscopy and electrostatic calculations}, year={2008}, doi={10.1529/biophysj.107.114033}, number={2}, volume={94}, issn={0006-3495}, journal={Biophysical Journal}, pages={600--611}, author={Andersson, Julia and Hauser, Karin and Karjalainen, Eeva-Liisa and Barth, Andreas} }

Karjalainen, Eeva-Liisa 2012-02-28T07:56:43Z Barth, Andreas 2012-02-28T07:56:43Z Hauser, Karin 2008-01-15 Andersson, Julia Protonation of the Ca21 ligands of the SR Ca21-ATPase (SERCA1a) was studied by a combination of rapid scan FTIR spectroscopy and electrostatic calculations. With FTIR spectroscopy, we investigated the pH dependence of C¼O bands of the Ca21-free phosphoenzyme (E2P) and obtained direct experimental evidence for the protonation of carboxyl groups upon Ca21 release. At least three of the infrared signals from protonated carboxyl groups of E2P are pH dependent with pKa values near 8.3: a band at 1758 cm 1 characteristic of nonhydrogen-bonded carbonyl groups, a shoulder at 1720 cm 1, and part of a band at 1710 cm 1, both characteristic of hydrogen-bonded carbonyl groups. The bands are thus assigned to H1 binding residues, some of which are involved in H1 countertransport. At pH 9, bands at 1743 and 1710 cm 1 remain which we do not attribute to Ca21/H1 exchange.Wealso obtained evidence for a pH-dependent conformational change in b-sheet or turn structures of the ATPase. With MCCE on the E2P analog E2(TG1MgF4 2), we assigned infrared bands to specific residues and analyzed whether or not the carbonyl groups of the acidic Ca21 ligands are hydrogen bonded. The carbonyl groups of Glu771, Asp800, and Glu908 were found to be hydrogen bonded and will thus contribute to the lower wave number bands. The carbonyl group of some side-chain conformations of Asp800 is left without a hydrogen-bonding partner; they will therefore contribute to the higher wave number band. eng Hauser, Karin deposit-license Karjalainen, Eeva-Liisa First publ. in: Biophysical Journal ; 94 (2008), 2. - pp. 600–611 Protonation and hydrogen bonding of C<sup>2+</sup> site residues in the E2P phosphoenzyme intermediate of Sarcoplasmic Reticulum C<sup>2+</sup>-ATPase studied by a combination of infrared spectroscopy and electrostatic calculations Andersson, Julia Barth, Andreas

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