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• W2091387166 abstract "The alkaline conformation (state IV) of yeast iso-1-ferricytochrome c and variants in which selected lysyl residues were replaced with alanyl residues has been studied by 1H NMR spectroscopy, electronic spectroscopy, EPR spectroscopy, direct electrochemistry, pH-jump kinetics, and temperature-dependent circular dichroism spectroscopy. On the basis of the NMR studies, Lys73 and Lys79 are shown to replace Met80 as the axial ligand in the two conformers of state IV that were detected in previous studies (Hong, X. L.; Dixon, D. W. FEBS Lett. 1989, 246, 105−108; Ferrer, J. C.; Guillemette, J. G.; Bogumil, R.; Inglis, S. C.; Smith, M.; Mauk, A. G. J. Am. Chem. Soc. 1993, 115, 7507−7508). The pKa for the conformational equilibrium between state III (native conformation) and state IV of the wild-type protein (8.70(2)) is found to be intermediate between that of the Lys73 bound conformer (8.44(1)) and that of the Lys79 bound conformer (8.82(2)) (0.1 M NaCl, 25 °C) as are the kinetic parameters for the conversion o..." @default.
• W2091387166 created "2016-06-24" @default.
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• W2091387166 date "1998-10-27" @default.
• W2091387166 modified "2023-10-17" @default.
• W2091387166 title "Proton-Linked Protein Conformational Switching: Definition of the Alkaline Conformational Transition of Yeast Iso-1-ferricytochrome <i>c</i>" @default.
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• W2091387166 doi "https://doi.org/10.1021/ja971756+" @default.
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