Journal
FEBS LETTERS
Volume 582, Issue 25-26, Pages 3705-3709Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2008.09.038
Keywords
Cytochrome bd; Ubiquinol; Respiration
Funding
- National Institutes of Health [HL16101]
- Wenner-Gren Foundations
- Civilian Research and Development Fund [RUB1-2836-MO-06]
- Howard Hughes Medical Institute [55005615]
- Russian Foundation for Basic Research [08-04-00093]
Ask authors/readers for more resources
Cytochrome bd catalyzes the two-electron oxidation of either ubiquinol or menaquinol and the four-electron reduction of O-2 to H2O. In the current work, the rates of reduction of the fully oxidized and oxoferryl forms of the enzyme by the 2-electron donor ubiquinol-1 and single electron donor N,N,N',N'- tetramethyl-p- phenylendiamine ( TMPD) have been examined by stopped-flow techniques. Reduction of the all-ferric form of the enzyme is 1000-fold slower than required for a step in the catalytic cycle, whereas the observed rates of reduction of the oxoferryl and singly-reduced forms of the cytochrome are consistent with the catalytic turnover. The data support models of the catalytic cycle which do not include the fully oxidized form of the enzyme as an intermediate. (c) 2008 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available