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The mitochondrial respiratory chain of Rhizopus stolonifer (Ehrenb.:Fr.) Vuill
Authors:Leobarda Robles-Martínez  María Guadalupe Guerra-Sánchez  Oscar Flores-Herrera  Ana Niurka Hernández-Lauzardo  Miguel Gerardo Velázquez-Del Valle  Juan Pablo Pardo
Affiliation:1. Departamento de Microbiología, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Mexico, D. F., Mexico
2. Departamento de Bioquímica, Facultad de Medicina, Universidad Nacional Autónoma de México, Apartado Postal 70-159, Coyoacán, 04510, Mexico, D. F., Mexico
3. CEPROBI, Instituto Politécnico Nacional, Yautepec, Morelos, Mexico
Abstract:Rhizopus stolonifer (Ehrenb.:Fr.) Vuill mitochondria contain the complete system for oxidative phosphorylation, formed by the classical components of the electron transport chain (complexes I, II, III, and IV) and the F1F0-ATP synthase (complex V). Using the native gel electrophoresis, we have shown the existence of supramolecular associations of the respiratory complexes. The composition and stoichiometry of the oxidative phosphorylation complexes were similar to those found in other organisms. Additionally, two alternative routes for the oxidation of cytosolic NADH were identified: the alternative NADH dehydrogenase and the glycerol-3-phosphate shuttles. Residual respiratory activity after inhibition of complex IV by cyanide was inhibited by low concentrations of n-octyl gallate, indicating the presence of an alternative oxidase. The K0.5 for the respiratory substrates NADH, succinate, and glycerol-3-phosphate in permeabilized cells was higher than in isolated mitochondria, suggesting that interactions of mitochondria with other cellular elements might be important for the function of this organelle.
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