Replacements of lysine 32 in yeast cytochrome c. Effects on the binding and reactivity with physiological partners.
Open Access
- 1 December 1988
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 263 (34) , 18290-18297
- https://doi.org/10.1016/s0021-9258(19)81358-3
Abstract
No abstract availableThis publication has 31 references indexed in Scilit:
- Effects of amino acid replacements in yeast iso-1 cytochrome c on heme accessibility and intracomplex electron transfer in complexes with cytochrome c peroxidaseBiochemistry, 1988
- Kinetics of reduction by free flavin semiquinones of the components of the cytochrome c-cytochrome c peroxidase complex and intracomplex electron transferBiochemistry, 1987
- The structure, function and evolution of cytochromesProgress in Biophysics and Molecular Biology, 1985
- Guided by electrostatics, a textbook protein comes of ageTrends in Biochemical Sciences, 1983
- Transient Kinetics of the One‐Electron Transfer Reaction between Reduced Flavocytochrome b2 and Oxidized Cytochrome cEuropean Journal of Biochemistry, 1982
- Spectrophotometric analysis of the interaction between cytochrome b5 and cytochrome cBiochemistry, 1982
- Amino acid replacements of the evolutionarily invariant tryptophan at position 64 in mutant forms of iso-1-cytochrome c from Saccharomyces cerevisiaeJournal of Molecular Biology, 1978
- An hypothetical structure for an intermolecular electron transfer complex of cytochromes c and b5Journal of Molecular Biology, 1976
- Mutagenic specificity: Reversion of iso-1-cytochrome c mutants of yeastJournal of Molecular Biology, 1973
- Contribution of Hydrophobic Interactions to the Stability of the Globular Conformation of ProteinsJournal of the American Chemical Society, 1962