1H NMR Studies of the Electron Exchange Between Cytochrome c and Iron Hexacyanides
Open Access
- 1 May 1982
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 124 (2) , 295-303
- https://doi.org/10.1111/j.1432-1033.1982.tb06591.x
Abstract
Binding of [Fe(CN)6]3−, [Cr(CN)6]3−, [Co(CN)6]3− and [Cr(C2O4)3]3− to horse, tuna and Candida krusi cytochromes c has been studied by high‐resolution 1H NMR spectroscopy. All the reagents bind at the same sites. There are at least two binding sites, and probably three, on horse cytochrome c at pH 7. One of the sites is only a weak binding site and is far from the haem group, whereas the other site(s) is(are) at the haem crevice. Ka for binding of [Fe(CN)6]3− to trimethyllysine‐72 of C. krusei ferricytochrome c is 140±15 M1 at 27 C and pH 7.This publication has 41 references indexed in Scilit:
- 1H NMR Studies of Eukaryotic Cytochrome cEuropean Journal of Biochemistry, 1982
- Kinetic data for redox reactions of cytochrome c with Fe(CN)5X complexes and the question of association prior to electron transferJournal of Inorganic Biochemistry, 1981
- Nuclear‐Magnetic‐Resonance Studies of Eukaryotic Cytochrome cEuropean Journal of Biochemistry, 1980
- Nuclear magnetic resonance studies of the phenylalanine residues of eukaryotic cytochrome cJournal of Inorganic Biochemistry, 1980
- The reaction of rhodospirillum rubrum cytochrome c2 with iron hexacyanidesBioinorganic Chemistry, 1975
- Nuclear magnetic resonance study of the rate of electron transfer between cytochrome c and iron hexacyanidesJournal of Molecular Biology, 1973
- Resolution enhancement of protein PMR spectra using the difference between a broadened and a normal spectrumJournal of Magnetic Resonance (1969), 1973
- Proton magnetic resonance studies of horse cytochrome cBiochemistry, 1973
- Thermodynamics of the redox reaction of cytochromes c of five different speciesFEBS Letters, 1970
- THE RATE OF OXIDATION OF CYTOCHROME c BY FERRICYANIDE IONS1Journal of the American Chemical Society, 1961