Article
Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme-ligand interactions.
Biochemistry - 22 Oct 1996
Barker P D, Freund S M
Abstract excerpt
Previous work has shown that, in variants of cytochrome b562 containing the H102M mutation, methionine residues provide both axial ligands to the heme iron. NMR spectroscopic studies of such bis-methionine-coordinated cytochrome have not previously been feasible, since the only other cytochrome w...
Topics
- Cytochrome b Group
- Escherichia coli
- Escherichia coli Proteins
- Ferric Compounds
- Ferrous Compounds
- Heme
- Hydrogen-Ion Concentration
- Iron
- Ligands
- Magnetic Resonance Spectroscopy
- Methionine
- Models, Molecular
- Mutation
- Oxidation-Reduction
- Protein Conformation
- Temperature