Coenzyme Q-pool function in glycerol-3-phosphate oxidation in hamster brown adipose tissue mitochondria
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
1326518
DOI
10.1007/bf00762682
Knihovny.cz E-resources
- MeSH
- Antimycin A pharmacology MeSH
- Glycerolphosphate Dehydrogenase antagonists & inhibitors metabolism MeSH
- Glycerophosphates metabolism MeSH
- Adipose Tissue, Brown enzymology ultrastructure MeSH
- Carbohydrate Dehydrogenases antagonists & inhibitors metabolism MeSH
- Cricetinae MeSH
- Mesocricetus MeSH
- Methacrylates MeSH
- Mitochondria enzymology MeSH
- Oxidation-Reduction MeSH
- Palmitoyl Coenzyme A pharmacology MeSH
- Electron Transport Complex III antagonists & inhibitors metabolism MeSH
- Thiazoles pharmacology MeSH
- Ubiquinone metabolism MeSH
- Animals MeSH
- Check Tag
- Cricetinae MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- 3-glycerophosphate dehydrogenase MeSH Browser
- alpha-glycerophosphoric acid MeSH Browser
- Antimycin A MeSH
- Glycerolphosphate Dehydrogenase MeSH
- Glycerophosphates MeSH
- Carbohydrate Dehydrogenases MeSH
- Methacrylates MeSH
- myxothiazol MeSH Browser
- Palmitoyl Coenzyme A MeSH
- Electron Transport Complex III MeSH
- Thiazoles MeSH
- Ubiquinone MeSH
We have investigated the role of the Coenzyme Q pool in glycerol-3-phosphate oxidation in hamster brown adipose tissue mitochondria. Antimycin A and myxothiazol inhibit glycerol-3-phosphate cytochrome c oxidoreductase in a sigmoidal fashion, indicating that CoQ behaves as a homogeneous pool between glycerol-3-phosphate dehydrogenase and complex III. The inhibition of ubiquinol cytochrome c reductase is linear at low concentrations of both inhibitors, indicating that sigmoidicity of antimycin A and myxothiazol inhibition is not a direct property of antimycin A and myxothiazol binding. Glycerol-3-phosphate cytochrome c oxidoreductase is strongly stimulated by added CoQ3, indicating that endogenous CoQ is not saturating. Application of the pool equation for nonsaturating ubiquinone allows calculation of the Km for endogenous CoQ of glycerol-3-phosphate dehydrogenase of 3.14 mM. The results of this investigations reveal that CoQ behaves as a homogeneous pool between glycerol-3-phosphate dehydrogenase and complex III in brown adipose tissue mitochondria; moreover, its concentration is far below saturation for maximal electron transfer activity in comparison with other branches of the respiratory chain connected with the CoQ pool. HPLC analysis revealed a lower amount of CoQ in brown adipose mitochondria (0.752 nmol/mg protein) in comparison with mitochondria from other tissues and the presence of both CoQ9 and CoQ10.
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