Article
Site-directed replacement of the coaxial heme ligands of bacterioferritin generates heme-free variants.
The Journal of biological chemistry - 6 Oct 1995
Andrews S C, Le Brun N E, Barynin V, Thomson A J, Moore G R, Guest J R, Harrison P M
Abstract excerpt
The bacterioferritin (BFR) of Escherichia coli is a heme-containing iron storage molecule. It is composed of 24 identical subunits, which form a roughly spherical protein shell surrounding a central iron storage cavity. Each of the 12 heme moieties of BFR possesses bis-methionine axial ligation,...
Topics
- Amino Acid Sequence
- Bacterial Proteins
- Base Sequence
- Binding Sites
- Cytochrome b Group
- DNA Primers
- Electron Spin Resonance Spectroscopy
- Escherichia coli
- Ferritins
- Genes, Bacterial
- Genetic Variation
- Heme
- Iron
- Ligands
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Oxidation-Reduction
- Spectrophotometry