Medical College of Wisconsin
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Reactions of reduced cellobiose oxidase with oxygen. Is cellobiose oxidase primarily an oxidase? Biochem J 1990 Aug 15;270(1):265-7

Date

08/15/1990

Pubmed ID

2396987

Pubmed Central ID

PMC1131709

DOI

10.1042/bj2700265

Scopus ID

2-s2.0-0025029798 (requires institutional sign-in at Scopus site)   34 Citations

Abstract

We report rapid-mixing experiments in which cellobiose oxidase, fully reduced with cellobiose, is allowed to react with excess molecular O2. Analysis of the progress curves and their comparison with computer simulations suggests that O2 reacts only with the cytochrome b-type haem and with a rate constant of approx. 0.5 s-1. In steady state the cytochrome b is partially oxidized, whereas the flavin remains largely reduced. This situation may be contrasted with that when dichloroindophenol is substituted for O2. Under these conditions the reactions are rapid (millisecond time range), and the redox centres in the enzyme appear to be oxidized simultaneously.

Author List

Wilson MT, Hogg N, Jones GD

Author

Neil Hogg PhD Sr Associate Dean, Professor in the Biophysics department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Anaerobiosis
Carbohydrate Dehydrogenases
Cellobiose
Computer Simulation
Disaccharides
Oxidation-Reduction
Oxygen
Sporothrix