The fully oxidized form of the cytochrome bd quinol oxidase from E. coli does not participate in the catalytic cycle: Direct evidence from rapid kinetics studies
Open Access
- 26 September 2008
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 582 (25-26), 3705-3709
- https://doi.org/10.1016/j.febslet.2008.09.038
Abstract
Cytochrome bd catalyzes the two-electron oxidation of either ubiquinol or menaquinol and the four-electron reduction of O2 to H2O. In the current work, the rates of reduction of the fully oxidized an...Keywords
This publication has 22 references indexed in Scilit:
- Strong Excitonic Interactions in the Oxygen-Reducing Site of bd-Type Oxidase: The Fe-to-Fe Distance between Hemes d and b595 is 10 ÅBiochemistry, 2008
- Kinetic Mechanism of Quinol Oxidation by Cytochrome bd Studied with Ubiquinone-2 AnalogsThe Journal of Biochemistry, 2006
- Arginine 391 in Subunit I of the Cytochrome bd Quinol Oxidase from Escherichia coli Stabilizes the Reduced Form of the Hemes and Is Essential for Quinol Oxidase ActivityPublished by Elsevier ,2004
- Site-Directed Mutation of the Highly Conserved Region near the Q-Loop of the Cytochrome bd Quinol Oxidase from Escherichia coli Specifically Perturbs Heme b595Biochemistry, 2001
- Interplay between three global regulatory proteins mediates oxygen regulation of the Escherichia coli cytochrome d oxidase (cydAB) operonMolecular Microbiology, 2000
- Electron Transfer Process in Cytochrome bd-Type Ubiquinol Oxidase from Escherichia coli Revealed by Pulse RadiolysisBiochemistry, 1999
- Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coliBiochemistry, 1995
- The room temperature reaction of carbon monoxide and oxygen with the cytochrome bd quinol oxidase from Escherichia coliBiochemistry, 1994
- The aerobic respiratory chain of Escherichia coliTrends in Biochemical Sciences, 1987
- Coulometric and spectroscopic analysis of the purified cytochrome d complex of Escherichia coli: evidence for the identification of "cytochrome a1" as cytochrome b595Biochemistry, 1986