Characterization of a hexammineruthenium-stimulated external NADH oxidase from rat liver mitochondria

The existence of an external hexammineruthenium-stimulated NADH oxidase in rat liver mitochondria is postulated. This enzyme is localized on the outer surface of the inner mitochondrial membrane, is specific for NADH and requires oxygen. The apparent affinity of the enzyme for NADH amounts to about...

Full description

Saved in:
Bibliographic Details
Published inBiochemistry international Vol. 23; no. 3; p. 489
Main Authors Linke, B, Dubiel, W, Henke, W, Gerber, G
Format Journal Article
LanguageEnglish
Published Australia 01.02.1991
Subjects
Animals
Male
Mitochondria, Liver - drug effects
Mitochondria, Liver - enzymology
Multienzyme Complexes - analysis
Multienzyme Complexes - drug effects
NADH, NADPH Oxidoreductases - analysis
NADH, NADPH Oxidoreductases - drug effects
Rats
Rats, Inbred Strains
Ruthenium - pharmacology
Ruthenium Compounds
Online AccessGet more information

Cover

More Information
Summary:The existence of an external hexammineruthenium-stimulated NADH oxidase in rat liver mitochondria is postulated. This enzyme is localized on the outer surface of the inner mitochondrial membrane, is specific for NADH and requires oxygen. The apparent affinity of the enzyme for NADH amounts to about 4 microM. Furthermore, the enzyme is characterized by an alkaline pH optimum and a linear Arrhenius plot (14 kJ/mol). The electron transfer from NADH to oxygen is not linked with the respiratory chain but is connected with the formation of superoxide radicals.
ISSN:0158-5231