Related references
Note: Only part of the references are listed.Strong excitonic interactions in the oxygen-reducing site of bd-type oxidase:: The Fe-to-Fe distance between hemes d and b595 is 10 Å
Alexander M. Arutyunyan et al.
BIOCHEMISTRY (2008)
Cytochrome bd from Azotobacter vinelandii:: Evidence for high-affinity oxygen binding
Ilya Belevich et al.
BIOCHEMISTRY (2007)
Discovery of the true peroxy intermediate in the catalytic cycle of terminal oxidases by real-time measurement
Ilya Belevich et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2007)
Kinetic mechanism of quinol oxidation by cytochrome bd studied with ubiquinone-2 analogs
Yushi Matsumoto et al.
JOURNAL OF BIOCHEMISTRY (2006)
Time-resolved electrometric and optical studies on cytochrome bd suggest a mechanism of electron-proton coupling in the di-heme active site
I Belevich et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2005)
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 activity
J Zhang et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (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 b595
J Zhang et al.
BIOCHEMISTRY (2001)
Interplay between three global regulatory proteins mediates oxygen regulation of the Escherichia coli cytochrome d oxidase (cydAB) operon
F Govantes et al.
MOLECULAR MICROBIOLOGY (2000)
Electrogenic reactions of cytochrome bd
A Jasaitis et al.
BIOCHEMISTRY (2000)