Mechanism of action of the copper(I) complex of 2,9-dimethyl-1,10-phenanthroline on Mycoplasma gallisepticum
| Autor: | M. W. G. De Bolster, H. Smit, R D Vis, W. T. Nauta, H. Timmerman, A H Stouthamer, H. Van Der Goot |
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| Rok vydání: | 1982 |
| Předmět: |
Mycoplasma gallisepticum
Copper Sulfate Inorganic chemistry chemistry.chemical_element Medicinal chemistry Cell membrane Biological pathway Mycoplasma Multienzyme Complexes medicine NADH NADPH Oxidoreductases Pharmacology (medical) Radioisotopes Pharmacology biology Ligand Cell Membrane Membrane transport biology.organism_classification Copper Infectious Diseases Membrane medicine.anatomical_structure chemistry Mechanism of action medicine.symptom Phenanthrolines Research Article |
| Zdroj: | Antimicrobial Agents and Chemotherapy. 21:881-886 |
| ISSN: | 1098-6596 0066-4804 |
| DOI: | 10.1128/aac.21.6.881 |
| Popis: | Evidence was found that the inhibitory action of Cu(DMP)2NO3, the copper(I) complex of 2,9-dimethyl-1,10-phenanthroline (DMP), on Mycoplasma gallisepticum is a consequence of the ultimate toxicity of copper, and not that of the ligand, DMP. From uptake studies with radiolabeled 67Cu and [14C]DMP, we concluded that significantly more copper than DMP is bound to the mycoplasmal cell. It appeared that dissociation of Cu(DMP)2+ occurred shortly after interaction with the cell membrane. Copper was transported across the cytoplasmic membrane. A strong dependence of copper uptake on the incubation medium was observed in the absence of DMP. The main function of the ligand DMP appeared to be as a vehicle for the transport of copper from nontoxic copper-medium complexes to membrane-buried cellular ligands. |
| Databáze: | OpenAIRE |
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