Article
DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation.
The Journal of biological chemistry - 20 Feb 2004
Inaba Kenji, Takahashi Yoh-hei, Fujieda Nobutaka, Kano Kenji, Miyoshi Hideto, Ito Koreaki
Abstract excerpt
DsbB is an Escherichia coli plasma membrane protein that reoxidizes the Cys30-Pro-His-Cys33 active site of DsbA, the primary dithiol oxidant in the periplasm. Here we describe a novel activity of DsbB to induce an electronic transition of the bound ubiquinone molecule. This transition was characterized by a striking emergence of an absorbance peak at 500 nm giving rise to a visible pink color. The ubiquinone...
Topics
- Amino Acids
- Bacterial Proteins
- Binding Sites
- Cell Membrane
- Cysteine
- Disulfides
- Electron Transport
- Escherichia coli
- Histidine
- Hydrogen-Ion Concentration
- Kinetics
- Membrane Proteins
- Models, Biological
- Models, Chemical