Fourier-transform infra-red studies of the alkaline isomerization of mitochondrial cytochrome c and the ionization of carboxylic acids
- 1 March 1989
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 258 (2) , 599-605
- https://doi.org/10.1042/bj2580599
Abstract
The alkaline transitions of tuna and horse ferricytochromes c and the trifluoroacetyl-lysine derivative of horse ferricytochrome c have been studied by Fourier-transform (FT) i.r. spectroscopy. The spectral perturbations resulting from the transition have been interpreted by reference to FT i.r. data on simple carboxylic-acid-containing compounds and a bacterial cytochrome c551 in which a haem propionate ionizes without causing a significant conformational change. The analysis strongly suggests that ionization of a haem propionate of mitochondrial cytochrome c triggers the alkaline conformation change.This publication has 25 references indexed in Scilit:
- Electrostatic interactions in globular proteins: Calculation of the pH dependence of the redox potential of cytochrome c551Journal of Molecular Biology, 1985
- Structural basis for the variation of pH-dependent redox potentials of Pseudomonas cytochromes c-551Biochemistry, 1984
- Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox formsJournal of Molecular Biology, 1982
- Conformation change of cytochrome cJournal of Molecular Biology, 1981
- Redox potentials of the photosynthetic bacterial cytochromes c2 and the structural bases for variabilityBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1978
- Nuclear magnetic resonance studies of hemoproteinsBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- The pH dependence of the resonance Raman spectra and structural alterations at heme moieties of various cytochromesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- Mechanism of hydrolysis by serine proteases: direct determination of the pKa's of aspartyl-102 and aspartyl-194 in bovine trypsin using difference infrared spectroscopyBiochemistry, 1976
- Some aspects of pH and temperature dependence of the NMR spectra of cytochrome cBiochemical and Biophysical Research Communications, 1971
- Some properties of the 695 m? band of pseudomonas cytochrome CBiopolymers, 1970