Complexation of iron hexacyanides by cytochrome c. Evidence for electron exchange at the exposed heme edge.
Open Access
- 1 March 1975
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 250 (6) , 2095-2098
- https://doi.org/10.1016/s0021-9258(19)41687-6
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Nuclear magnetic resonance study of the rate of electron transfer between cytochrome c and iron hexacyanidesJournal of Molecular Biology, 1973
- Distinction between oxidizing and reducing sites of cytochrome C by chemical modification with pyridoxal phosphateFEBS Letters, 1973
- Nuclear magnetic resonance study of exchangeable protons in ferrocytochrome cJournal of Molecular Biology, 1973
- The Amino-acid Sequence of Cytochrome c from Euglena gracilisNature, 1973
- The Properties and Amino-acid Sequence of Cytochrome c from Euglena gracilisNature, 1973
- Conformation of cytochromes. VI. Structure and enzymic properties of N-bromosuccinimide-modified horse heart cytochrome cBiochemistry, 1972
- Participation of the protein ligands in the folding of cytochrome cBiochemistry, 1972
- Effects of phosphate and other anions on the reaction between ferrous ion and cytochrome cBiochemistry, 1972
- Conformation of ferricytochrome c. IV. Relationship between optical absorption and protein conformationBiopolymers, 1967
- Ionization of cytochrome cBiochemical and Biophysical Research Communications, 1966