Article
Electron-proton coupling in cytochrome c studied using protein variants.
European journal of biochemistry - 15 Feb 1992
Gao Y, McLendon G, Pielak G J, Williams R J
Abstract excerpt
An NMR study of the cytochrome c variant Asn52Ile is used to show how the redox state change in native cytochrome c is coupled to a rearrangement of a proton network which runs through the cytochrome c molecule. The substitution breaks the H-bond network and removes the coupling. The uncovering o...
Topics
- Amino Acid Sequence
- Asparagine
- Cytochrome c Group
- Hydrogen Bonding
- Ion Channels
- Isoleucine
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Molecular Structure
- Mutation
- Oxidation-Reduction
- Protein Conformation
- Protons
- Saccharomyces cerevisiae