Active/de-active transition of respiratory complex I in bacteria, fungi, and animals

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1606, Issue 1-3, 2003, Pages 95-103

  Maklashina, Elena ^a,b   Kotlyar, Alexander B ^c   Cecchini, Gary ^a,b  

^a VETERANS AFFAIRS MEDICAL CENTER   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c TEL AVIV UNIVERSITY   (Israel)

Author keywords

Active de active transition; Complex I; Mitochondrial respiration; NADH:ubiquinone oxidoreductase

Indexed keywords

BACTERIAL ENZYME; FUNGAL ENZYME; INSECT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); VEGETABLE PROTEIN;

ANIMAL TISSUE; ARTICLE; BACTERIUM; CARP; CATTLE; CHICKEN; CONTROLLED STUDY; CORRELATION ANALYSIS; EARTHWORM; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME REGULATION; ENZYME SUBUNIT; ESCHERICHIA COLI; EUKARYOTE; FROG; FUNGUS; INSECT; LOBSTER; MAMMAL; MITOCHONDRIAL RESPIRATION; NEUROSPORA CRASSA; NONHUMAN; PARACOCCUS DENITRIFICANS; PRIORITY JOURNAL; PROTEIN FUNCTION; SPECIES COMPARISON; SPECIES DIFFERENCE; THERMODYNAMICS; YARROWIA LIPOLYTICA;

ANIMALIA; ANURA; BACTERIA (MICROORGANISMS); BOS TAURUS; BOVINAE; CYPRINUS CARPIO; ESCHERICHIA COLI; EUKARYOTA; FUNGI; GALLUS GALLUS; INSECTA; LOBSTER; MAMMALIA; NEUROSPORA; NEUROSPORA CRASSA; PARACOCCUS DENITRIFICANS; PHERETIMA SIEBOLDI; VERTEBRATA; YARROWIA LIPOLYTICA;

EID: 0142106477     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(03)00087-2     Document Type: Article

References (35)

1. Walker J.E. The NADH: ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 25:1992;253-254.
2. Yagi T., Matsuno-Yagi A. The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: the secret unlocked. Biochemistry. 42:2003;2266-2274.
3. Kotlyar A.B., Vinogradov A.D. Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase. Biochim. Biophys. Acta. 1019:1990;151-158.
4. Vinogradov A.D. Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (complex I) and the pseudo-reversible active/inactive enzyme transition. Biochim. Biophys. Acta. 1364:1998;169-185.
5. 2+ ions on the slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase. Biochim. Biophys. Acta. 1098:1992;144-150.
6. Gavrikova E.V., Vinogradov A.D. Active/de-active state transition of the mitochondrial complex I as revealed by specific sulfhydryl group labeling. FEBS Lett. 455:1999;36-40.
7. Maklashina E.O., Sled V.D., Vinogradov A.D. Hysteresis behavior of complex I from bovine heart mitochondria: kinetic and thermodynamic parameters of retarded reverse transition from the inactive to active state. Biochemistry/Biokhimiia. 59:1994;946-957.
8. Grivennikova V.G., Kapustin A.N., Vinogradov A.D. Catalytic activity of NADH-ubiquinone oxidoreductase (complex I) in intact mitochondria. Evidence for the slow active/inactive transition. J. Biol. Chem. 276:2001;9038-9044.
9. Maklashina E., Sher Y., Zhou H.-Z., Gray M.O., Karliner J.S., Cecchini G. Effect of anoxia/reperfusion on the reversible active/de-active transition of NADH-ubiquinone oxidoreductase (complex I) in rat heart. Biochim. Biophys. Acta. 1556:2002;6-12.
10. Yagi T., Yano T., Di Bernardo S., Matsuno-Yagi A. Prokaryotic complex I (NDH-1), an overview. Biochim. Biophys. Acta. 1364:1998;125-133.
11. van Belzen R., Kotlyar A.B., Moon N., Dunham W.R., Albracht S.P.J. The iron-sulfur clusters 2 and ubisemiquinone radicals of NADH: ubiquinone oxidoreductase are involved in energy coupling in submitochondrial particles. Biochemistry. 36:1997;886-893.
12. Kotlyar A.B., Albracht S.P.J., van Spanning R.J.M. Comparison of energization of complex I in membrane particles from Paracoccus denitrificans and bovine heart mitochondria. Biochim. Biophys. Acta. 1365:1998;53-59.
13. Sazanov L.A., Carroll J., Holt P., Toime L., Fearnley I.M. A role for native lipids in the stabilization and two-dimensional crystallization of the Escherichia coli NADH-ubiquinone oxidoreductase (Complex I). J. Biol. Chem. 278:2003;19483-19491.
14. Yano T., Yagi T. H(+)-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans. Studies on topology and stoichiometry of the peripheral subunits. J. Biol. Chem. 274:1999;28606-28611.
15. Carroll J., Fearnley I.M., Shannon R.J., Hirst J., Walker J.E. Analysis of the subunit composition of complex I from bovine heart mitochondria. Mol. Cell, Proteomics. 2:2003;117-126.
16. Friedrich T. The NADH: ubiquinone oxidoreductase (complex I) from Escherichia coli. Biochim. Biophys. Acta. 1364:1998;134-146.
17. Beinert H., Albracht S.P.J. New insights, ideas and unanswered questions concerning iron-sulfur clusters in mitochondria. Biochim. Biophys. Acta. 683:1982;245-277.
18. Ohnishi T. Iron-sulfur clusters/semiquinones in complex I. Biochim. Biophys. Acta. 1364:1998;186-206.
19. Albracht S.P.J., van der Linden E., Farber B.W. Quantitative amino acid analysis of bovine NADH: ubiquinone oxidoreductase (Complex I) and related enzymes. Consequences for the number of prosthetic groups. Biochim. Biophys. Acta. 1557:2003;41-49.
20. Videira A. Complex I from the fungus Neurospora crassa. Biochim. Biophys. Acta. 1364:1998;89-100.
21. Friedrich T. Complex I: a chimera of a redox and conformation-driven proton pump. J. Bioenerg. Biomembranes. 33:2001;169-177.
22. Maklashina E., Berthold D.A., Cecchini G. Anaerobic expression of Escherichia coli succinate dehydrogenase: functional replacement of fumarate reductase in the respiratory chain during anaerobic growth. J. Bacteriol. 180:1998;5989-5996.
23. Djafarzadeh R., Kerscher S., Zwicker K., Radermacher M., Lindahl M., Schägger H., Brandt U. Biophysical and structural characterization of proton-translocating NADH-dehydrogenase (complex I) from the strictly aerobic yeast Yarrowia lipolytica. Biochim. Biophys. Acta. 1459:2000;230-238.
24. Van den Bergh S.G. Insect mitochondria. Methods Enzymol. 10:1967;117-122.
25. Ernster L., Nordenbrand K. Skeletal muscle mitochondria. Methods Enzymol. 10:1967;86-94.
26. Johnson D., Lardy H. Isolation of liver or kidney mitochondria. Methods Enzymol. 10:1967;94-96.
27. Blair P.V. The large-scale preparation and properties of heart mitochondria from slaughterhouse material. Methods Enzymol. 10:1967;78-81.
28. Kerscher S.J., Eschemann A., Okun P.M., Brandt U. External alternative NADH: ubiquinone oxidoreductase redirected to the internal face of the mitochondrial inner membrane rescues complex I deficiency in Yarrowia lipolytica. J. Cell Sci. 114:2001;3915-3921.
29. Grivennikova V.G., Serebryanaya D.V., Isakova E.P., Belozerskaya T.A., Vinogradov A.D. The transition between active and de-activated forms of NADH: ubiquinone oxidoreductase (Complex I) in the mitochondrial membrane of Neurospora crassa. Biochem. J. 369:2003;619-626.
30. Grivennikova V.G., Maklashina E.O., Gavrikova E.V., Vinogradov A.D. Interaction of the mitochondrial NADH-ubiquinone reductase with rotenone as related to the enzyme active/inactive transition. Biochim. Biophys. Acta. 1319:1997;223-232.
31. Schuler F., Yano T., Di Bernardo S., Yagi T., Yankovskaya V., Singer T.P., Casida J.E. NADH-quinone oxidoreductase: PSST subunit couples electron transfer from iron-sulfur cluster N2 to quinone. Proc. Natl. Acad. Sci. U. S. A. 96:1999;4149-4153.
32. Schuler F., Casida J.E. Functional coupling of PSST and ND1 subunits in NADH: ubiquinone oxidoreductase established by photoaffinity labeling. Biochim. Biophys. Acta. 1506:2001;79-87.
33. Nakamaru-Ogiso E., Sakamoto K., Matsuno-Yagi A., Miyoshi H., Yagi T. The ND5 subunit was labeled by a photoaffinity analogue of fenpyroximate in bovine mitochondrial complex I. Biochemistry. 42:2003;746-754.
34. Kerscher S.J. Diversity and origin of alternative NADH: ubiquinone oxidoreductases. Biochim. Biophys. Acta. 1459:2000;274-283.
35. Papa S. The NDUFS4 nuclear gene of complex I of mitochondria and the cAMP cascade. Biochim. Biophys. Acta. 1555:2002;147-153.