CuB promotes both binding and reduction of dioxygen at the heme-copper binuclear center in the Escherichia coli bo-type ubiquinol oxidase.

doi:10.1016/0014-5793(95)00852-z

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Article

CuB promotes both binding and reduction of dioxygen at the heme-copper binuclear center in the Escherichia coli bo-type ubiquinol oxidase.

FEBS letters - 21 Aug 1995

Mogi T, Hirano T, Nakamura H, Anraku Y, Orii Y

Abstract excerpt

A CuB-deficient mutant of the Escherichia coli bo-type ubiquinol oxidase exhibits a very low oxidase activity that is consistent with a decreased dioxygen binding rate. During the turnover, a photolabile reaction intermediate persists for a few hundred milliseconds, due to much slower heme o-to-l...

Topics

Carbon Monoxide
Copper
Electron Transport Complex IV
Escherichia coli
Hemeproteins
Kinetics
Mutation
Oxidation-Reduction
Oxygen
Spectrum Analysis
Time Factors

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