Article
Effects of subunit I mutations on redox-linked conformational changes of the Escherichia coli bo-type ubiquinol oxidase revealed by Fourier-transform infrared spectroscopy.
Journal of biochemistry - 1 Jul 1999
Yamazaki Y, Kandori H, Mogi T
Abstract excerpt
Cytochrome bo is the heme-copper terminal ubiquinol oxidase in the aerobic respiratory chain of Escherichia coli, and functions as a redox-coupled proton pump. As an extension to our mutagenesis and Fourier-transform infrared studies on ion pumps, we examined the effects of subunit I mutations on redox-linked protein structural changes in cytochrome bo. Upon photo-reduction in the presence of riboflavin, Y288F...
Topics
- Binding Sites
- Copper
- Cyanides
- Cytochrome b Group
- Cytochromes
- Escherichia coli
- Escherichia coli Proteins
- Glutamic Acid
- Heme
- Mutation
- Oxidation-Reduction
- Protein Conformation
- Riboflavin
- Spectroscopy, Fourier Transform Infrared
- Spectrum Analysis