Antibiotic mucidin, a new antimycin A-like inhibitor of electron transport in rat liver mitochondria
Autor: | Miroslav Behúň, V. Musílek, Julius Subik |
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Rok vydání: | 1974 |
Předmět: |
Time Factors
Biophysics Antimycin A Cytochrome c Group Mitochondria Liver Oxidative phosphorylation Mitochondrion Biochemistry Oxidative Phosphorylation Electron Transport chemistry.chemical_compound Oxygen Consumption Animals Molecular Biology Adenosine Triphosphatases Substrate (chemistry) Succinates Cell Biology NAD Strobilurins Electron transport chain Anti-Bacterial Agents Rats Kinetics EGTA chemistry Spectrophotometry Fatty Acids Unsaturated Cytochromes Phosphorylation NAD+ kinase Oxidation-Reduction Dinitrophenols Polarography |
Zdroj: | Biochemical and Biophysical Research Communications. 57:17-22 |
ISSN: | 0006-291X |
DOI: | 10.1016/s0006-291x(74)80351-7 |
Popis: | Summary Mucidin at concentration 1 μg/mg mitochondrial protein completely inhibited the oxidation of succinate and NADH-linked substrates in rat liver mitochondria. In succinate oxidizing mitochondria mucidin induced a crossover point between cytochromes b and c + c 1 . Under these conditions mucidin had no effect on the ATPase activity as well as on the phosphorylation efficiency of rat liver mitochondria measured with TMPD plus ascorbate as substrate. These properties of mucidin resemble those of other inhibitors of mitochondrial electron transport such as antimycin A and HQNO. |
Databáze: | OpenAIRE |
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