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- Title
Oxygenated complex of cytochrome bd from Escherichia coli: Stability and photolability
- Authors
Belevich, Ilya; Borisov, Vitaliy B.; Konstantinov, Alexander A.; Verkhovsky, Michael I.
- Abstract
Abstract: Cytochrome bd is one of the two terminal ubiquinol oxidases in the respiratory chain of Escherichia coli catalyzing reduction of O2 to H2O. The enzyme is expressed under low oxygen tension; due to high affinity for O2 it is isolated mainly as a stable oxygenated complex. Direct measurement of O2 binding to heme d in the one-electron reduced isolated enzyme gives K d(O2) of ∼280nM. It is possible to photolyse the heme d oxy-complex by illumination of the enzyme for several minutes under microaerobic conditions; the light-induced difference absorption spectrum is virtually identical to the inverted spectrum of O2 binding to heme d.
- Subjects
ESCHERICHIA coli; HEMOGLOBINS; PHOTOSYNTHETIC oxygen evolution; ENZYMES
- Publication
FEBS Letters, 2005, Vol 579, Issue 21, p4567
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2005.07.011