TY - JOUR
T1 - The mitochondrial respiratory chain of Rhizopus stolonifer (Ehrenb.:Fr.) Vuill
AU - Robles-Martínez, Leobarda
AU - Guerra-Sánchez, María Guadalupe
AU - Flores-Herrera, Oscar
AU - Hernández-Lauzardo, Ana Niurka
AU - Velázquez-Del Valle, Miguel Gerardo
AU - Pardo, Juan Pablo
N1 - Funding Information:
Acknowledgments This work was supported by grants from Consejo Nacional de Ciencia y Tecnología (CONACyT 59855) and Programa de Apoyo a Proyectos de Investigación e Innovación Tecnológica (PAPIIT IN210311-3) from Universidad Nacional Autónoma de México, and Secretaría de Investigación y Posgrado (SIP), Instituto Politécnico Nacional, grants 20070822, 20080183,
Funding Information:
and 20080561. Leobarda Robles-Martínez is a Ph.D. student in the Quimicobiológicas Program from Escuela Nacional de Ciencias Bi-ológicas of Instituto Politécnico Nacional and was supported by grants from CONACyT (206876) and SIP (Programa Institucional de Formación de Investigadores).
PY - 2013/1
Y1 - 2013/1
N2 - 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 F 1 F 0 -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 ofanalternative oxidase. The K 0 .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.
AB - 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 F 1 F 0 -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 ofanalternative oxidase. The K 0 .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.
KW - F1F0-ATP synthase
KW - Glycerol-3-phosphate shuttle
KW - NADH dehydrogenase
KW - Oxidative phosphorylation
KW - Respiratory supercomplexes
UR - http://www.scopus.com/inward/record.url?scp=84872257425&partnerID=8YFLogxK
U2 - 10.1007/s00203-012-0845-7
DO - 10.1007/s00203-012-0845-7
M3 - Artículo
C2 - 23064442
SN - 0302-8933
VL - 195
SP - 51
EP - 61
JO - Archives of Microbiology
JF - Archives of Microbiology
IS - 1
ER -