Article
Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.
Proceedings of the National Academy of Sciences of the United States of America - 11 Oct 2005
Lin I-Jin, Gebel Erika B, Machonkin Timothy E, Westler William M, Markley John L
Abstract excerpt
The rubredoxin from Clostridium pasteurianum (CpRd) provides an excellent system for investigating how the protein sequence modulates the reduction potential of the active site in an iron-sulfur protein. (15)N NMR spectroscopy has allowed us to determine with unprecedented accuracy the strengths of all six key hydrogen bonds between protein backbone amides and the sulfur atoms of the four cysteine residues that...
Topics
- Binding Sites
- Biophysical Phenomena
- Biophysics
- Clostridium
- Genetic Variation
- Hydrogen Bonding
- Iron
- Models, Molecular
- Mutagenesis, Site-Directed
- Nitrogen
- Nuclear Magnetic Resonance, Biomolecular