The presence of the iron-sulfur protein (subunit V) of complex III in mitochondria of heme-deficient yeast cells lacking iron-sulfur clusters detectable by electron paramagnetic resonance
| Autor: | Liviu Clejan, Ching-I. P. Lin, Diana S. Beattie, Tomoko Ohnishi |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Iron-Sulfur Proteins
Immunoprecipitation Protein subunit Respiratory chain Heme Saccharomyces cerevisiae Biochemistry Sulfite reductase Fungal Proteins chemistry.chemical_compound Electron Transport Complex III Multienzyme Complexes Metalloproteins NADH NADPH Oxidoreductases Quinone Reductases ATP synthase biology Succinate dehydrogenase Immunochemistry Electron Spin Resonance Spectroscopy Mitochondria chemistry Coenzyme Q – cytochrome c reductase biology.protein |
| Zdroj: | European journal of biochemistry. 137(1-2) |
| ISSN: | 0014-2956 |
| Popis: | The presence of subunit V, the iron-sulfur protein, of complex III has been demonstrated in mitochondria from a mutant of Saccharomyces cerevisiae which lacks 5-aminolevulinic acid synthase and, hence, is devoid of heme. The mature form (24 kDa) of the iron-sulfur protein was observed in equal amounts in the heme-deficient and heme-sufficient cells with antiserum against subunit V and either the sensitive immuno-transfer technique or immunoprecipitation from dodecylsulfate-solubilized mitochondria. In addition, a slight shoulder with a molecular mass 1.5 kDa larger than the mature form was present in mitochondria from the heme-deficient cells. Electron paramagnetic resonance spectroscopy revealed the absence of iron-sulfur signals due to clusters S-1, S-2 and S-3 of succinate dehydrogenase or to Rieske's iron-sulfur cluster of complex III in mitochondria from the hemedeficient cells. The lack of iron-sulfur centers in these cells may be a consequence of the absence of sulfite reductase in the cells without heme. |
| Databáze: | OpenAIRE |
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