Effect of a dipole moment on the ionic strength dependence of electron-transfer reactions of cytochrome c
- 1 April 1987
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 109 (9) , 2679-2682
- https://doi.org/10.1021/ja00243a020
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- The asymmetric distribution of charges on the surface of horse cytochrome c. Functional implications.Journal of Biological Chemistry, 1982
- Use of specific lysine modifications to identify the site of reaction between cytochrome c and ferricyanide.Journal of Biological Chemistry, 1981
- Mapping of anion binding sites on cytochrome c by differential chemical modification of lysine residues.Proceedings of the National Academy of Sciences, 1980
- Effect of a molecular dipole on the ionic strength dependence of a biomolecular rate constant. Identification of the site of reactionBiophysical Journal, 1980
- Comparison of the electron-transfer reactivities of tris(oxalato)cobaltate(III) (Co(ox)33-) and tris(1,10-phenanthroline)cobalt(III) (Co(phen)33+) with metalloproteinsJournal of the American Chemical Society, 1980
- Ion binding to cytochrome c studied by nuclear magnetic quadrupole relaxationBiochemistry, 1979
- Definition of cytochrome c binding domains by chemical modification. I. Reaction with 4-chloro-3,5-dinitrobenzoate and chromatographic separation of singly substituted derivatives.Journal of Biological Chemistry, 1978
- Ion binding to lysine-modified derivatives of cytochrome cCanadian Journal of Biochemistry, 1977
- Metalloprotein electron transfer reactions: analysis of reactivity of horse heart cytochrome c with inorganic complexes.Proceedings of the National Academy of Sciences, 1976
- Electrophoretic Behavior of Mammalian-type Cytochromes cJournal of Biological Chemistry, 1966