Electrostatic modulation of the kinetics of electron transfer from cytochrome c to cobalt phenanthroline by binding to lipid bilayers: Effects of ionic strength and extent of incorporation of various negatively charged lipids
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference9 articles.
1. Electrostatic effects on the kinetics of electron transfer reactions of cytochrome c caused by binding to negatively charged lipid bilayer vesicles
2. Cytochrome c at charged interfaces. 2. Complexes with negatively charged macromolecular systems studied by resonance Raman spectroscopy
3. Quantitative conformational analysis of cytochromec bound to phospholipid vesicles studied by resonance Raman spectroscopy
4. Membrane binding induces destabilization of cytochrome c structure
5. Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. I. Evidence from deuterium NMR measurements
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1. The interaction of ferrocytochromecwith long-chain fatty acids and their CoA and carnitine esters;Biochemistry and Cell Biology;2000-12-01
2. Cytochrome c at Model Membrane Surfaces: Exploration via Second Harmonic Generation-Circular Dichroism and Surface-Enhanced Resonance Raman Spectroscopy;Langmuir;2000-06-13
3. The interaction of ferrocytochrome c with long-chain fatty acids and their CoA and carnitine esters;Biochemistry and Cell Biology;2000
4. Comparison of Electron Transfer Kinetics between Redox Proteins Free in Solution and Electrostatically Complexed to a Lipid Bilayer Membrane;Archives of Biochemistry and Biophysics;1994-05
5. Interaction of phospholipids with proteins and peptides. New advances III;International Journal of Biochemistry;1993-02
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