Article
Molecular structure of redox metal centers of the cytochrome bo complex from Escherichia coli. Spectroscopic characterizations of the subunit I histidine mutant oxidases.
The Journal of biological chemistry - 9 Dec 1994
Tsubaki M, Mogi T, Hori H, Hirota S, Ogura T, Kitagawa T, Anraku Y
Abstract excerpt
A site-directed mutagenesis study on the conserved subunit I histidines of the cytochrome bo complex in Escherichia coli identified ligands of the low spin heme B and CuB centers; however, the assignment of the proximal ligand of the high spin heme O was ambiguous (Minagawa, J., Mogi, T., Gennis,...
Topics
- Copper
- Cytochrome b Group
- Cytochromes
- Electron Spin Resonance Spectroscopy
- Escherichia coli
- Escherichia coli Proteins
- Histidine
- Iron
- Mutation
- Oxidation-Reduction
- Oxidoreductases