4.5 Article

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

Related references

Note: Only part of the references are listed.
Article Biochemistry & Molecular Biology

Cytochrome bd from Azotobacter vinelandii:: Evidence for high-affinity oxygen binding

Ilya Belevich et al.

BIOCHEMISTRY (2007)

Article Biochemistry & Molecular Biology

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)

Article Biochemistry & Molecular Biology

Kinetic mechanism of quinol oxidation by cytochrome bd studied with ubiquinone-2 analogs

Yushi Matsumoto et al.

JOURNAL OF BIOCHEMISTRY (2006)

Article Multidisciplinary Sciences

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)

Article Biochemistry & Molecular Biology

Electrogenic reactions of cytochrome bd

A Jasaitis et al.

BIOCHEMISTRY (2000)