Topography and chemical reactivity of the active-inactive transition-sensitive SH-group in the mitochondrial NADH:ubiquinone oxidoreductase (Complex I)

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1757, Issue 9-10, 2006, Pages 1155-1161

  Gostimskaya, Irina S ^a   Cecchini, Gary ^b,c   Vinogradov, Andrei D ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b SAN FRANCISCO VETERANS AFFAIRS MEDICAL CENTER   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Active de active transition; Mitochondria; NADH:ubiquinone oxidoreductase; Respiratory Complex I; Sulfhydryl group

Indexed keywords

5,5' DITHIOBIS(2 NITROBENZOIC ACID); ALAMETHICIN; ANTIBIOTIC AGENT; GLUTATHIONE DISULFIDE; MITOCHONDRIAL ENZYME; N ETHYLMALEIMIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); THIOL DERIVATIVE; THIOL GROUP;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTICLE; CHEMICAL REACTION; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME LOCALIZATION; IONIC STRENGTH; MITOCHONDRION; NONHUMAN; PH; PRIORITY JOURNAL; RAT; SENSITIVITY ANALYSIS; SUBMITOCHONDRIAL PARTICLE;

ANIMALS; CATTLE; DITHIONITROBENZOIC ACID; ELECTRON TRANSPORT COMPLEX I; ETHYLMALEIMIDE; HYDROGEN-ION CONCENTRATION; KINETICS; MITOCHONDRIA, HEART; PERMEABILITY; RATS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBMITOCHONDRIAL PARTICLES; SULFHYDRYL COMPOUNDS;

EID: 33748975921     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.04.016     Document Type: Article

References (38)

1. Carroll J., Fearnley I.M., Shannon R.J., Hirst J., and Walker J.E. Analysis of the subunit composition of complex I from bovine heart mitochondria. Mol. Cell. Proteomics 2 (2003) 117-126
2. Xu X., Matsuno-Yagi A., and Yagi T. DNA sequencing of the seven remaining structural genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans. Biochemistry 32 (1993) 968-981
3. Weidner U., Geier S., Ptock A., Friedrich T., Leif H., and Weiss H. The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I. J. Mol. Biol. 233 (1993) 109-122
4. Dupuis A., Chevallet M., Darrouzet E., Duborjal H., Lunardi J., and Issartel J.P. The complex I from Rhodobacter capsulatus. Biochim. Biophys. Acta 1364 (1998) 147-165
5. Abdrakhmanova A., Zickermann V., Bostina M., Radermacher M., Schagger H., Kerscher S., and Brandt U. Subunit composition of mitochondrial complex I from the yeast Yarrowia lipolytica. Biochim. Biophys. Acta 1658 (2004) 148-156
6. Videira A., and Duarte M. From NADH to ubiquinone in Neurospora mitochondria. Biochim. Biophys. Acta 1555 (2002) 187-191
7. Cardol P., Vanrobaeys F., Devreese B., Van Beeumen J., Matagne R.F., and Remacle C. Higher plant-like subunit composition of mitochondrial complex I from Chlamydomonas reinhardtii: 31 conserved components among eukaryotes. Biochim. Biophys. Acta 1658 (2004) 212-224
8. Heazlewood J.L., Howell K.A., and Millar A.H. Mitochondrial complex I from Arabidopsis and rice: orthologs of mammalian and fungal components coupled with plant-specific subunits. Biochim. Biophys. Acta 1604 (2003) 159-169
9. 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
10. Grivennikova V.G., Serebryanaya D.V., Isakova E.P., Belozerskaya T.A., and 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
11. Grivennikova V.G., Roth R., Zakharova N.V., Hagerhall C., and Vinogradov A.D. The mitochondrial and prokaryotic proton-translocating NADH:ubiquinone oxidoreductases: similarities and dissimilarities of the quinone-junction sites. Biochim. Biophys. Acta 1607 (2003) 79-90
12. Galkin A.S., Grivennikova V.G., and Vinogradov A.D. H+/2e-stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles. FEBS Lett. 451 (1999) 157-161
13. Grivennikova V.G., Ushakova A.V., Hagerhall C., and Vinogradov A.D. Proton translocation catalyzed by Paracoccus denitrificans NADH:quinone oxidoreductase (NDH-1). Biochim. Biophys. Acta: EBEC Short Reports 12 (2002) 209
14. Papa S., Sardanelli A.M., Cocco T., Speranza F., Scacco S.C., and Technikova-Dobrova Z. The nuclear-encoded 18 kDa (IP) AQDQ subunit of bovine heart complex I is phosphorylated by the mitochondrial cAMP-dependent protein kinase. FEBS Lett. 379 (1996) 299-301
15. Scacco S., Vergari R., Scarpulla R.C., Technikova-Dobrova Z., Sardanelli A., Lambo R., Lorusso V., and Papa S. cAMP-dependent phosphorylation of the nuclear encoded 18-kDa (IP) subunit of respiratory complex I and activation of the complex in serum-starved mouse fibroblast cultures. J. Biol. Chem. 275 (2000) 17578-17582
16. Papa S., Sardanelli A.M., Scacco S., Petruzzella V., Technikova-Dobrova Z., Vergari R., and Signorile A. The NADH: ubiquinone oxidoreductase (complex I) of the mammalian respiratory chain and the cAMP cascade. J. Bioenerg. Biomembr. 34 (2002) 1-10
17. Chen R., Fearnley I.M., Peak-Chew S.Y., and Walker J.E. The phosphorylation of subunits of complex I from bovine heart mitochondria. J. Biol. Chem. 279 (2004) 26036-26045
18. Schulenberg B., Aggeler R., Beechem J.M., Capaldi R.A., and Patton W.F. Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye. J. Biol. Chem. 278 (2003) 27251-27255
19. Schilling B., Aggeler R., Schulenberg B., Murray J., Row R.H., Capaldi R.A., and Gibson B.W. Mass spectrometric identification of a novel phosphorylation site in subunit NDUFA10 of bovine mitochondrial complex I. FEBS Lett. 579 (2005) 2485-2490
20. Vinogradov A.D., and Grivennikova V.G. The mitochondrial complex I: progress in understanding of catalytic properties. IUBMB Life 52 (2001) 129-134
21. Kotlyar A.B., and Vinogradov A.D. Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase. Biochim. Biophys. Acta 1019 (1990) 151-158
22. Kotlyar A.B., Sled V.D., and Vinogradov A.D. Effect of Ca2+ ions on the slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase. Biochim. Biophys. Acta 1098 (1992) 144-150
23. Loskovich M.V., Grivennikova V.G., Cecchini G., and Vinogradov A.D. Inhibitory effect of palmitate on the mitochondrial NADH:ubiqinon oxidoreductase (Complex I) as related to the active-de-active enzyme transition. Biochem. J. 387 (2005) 677-683
24. Maklashina E.O., Sled' V.D., and 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. Biokhimiia 59 (1994) 946-957
25. Grivennikova V.G., Kapustin A.N., and 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
26. Maklashina E., Sher Y., Zhou H.Z., Gray M.O., Karliner J.S., and 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
27. Maklashina E., Kotlyar A.B., and Cecchini G. Active/de-active transition of respiratory complex I in bacteria, fungi, and animals. Biochim. Biophys. Acta 1606 (2003) 95-103
28. Kotlyar A.B., Albracht S.P., and van Spanning R.J. Comparison of energization of complex I in membrane particles from Paracoccus denitrificans and bovine heart mitochondria. Biochim. Biophys. Acta 1365 (1998) 53-59
29. Gavrikova E.V., and 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
30. Burbaev D.Sh., Moroz I.A., Kotlyar A.B., Sled V.D., and Vinogradov A.D. Ubisemiquinone in the NADH:ubiquinone reductase region of the mitochondrial respiratory chain. FEBS Lett. 254 (1989) 47-51
31. Jacobus W.E., and Saks V.A. Creatine kinase of heart mitochondria: changes in its kinetic properties induced by coupling to oxidative phosphorylation. Arch. Biochem. Biophys. 219 (1982) 167-178
32. Riddles P.W., Blakeley R.L., and Zerner B. Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid)-A reexamination. Anal. Biochem. 94 (1979) 75-81
33. Gostimskaya I.S., Grivennikova V.G., Zharova T.V., Bakeeva L.E., and Vinogradov A.D. In situ assay of the intramitochondrial enzymes: use of alamethicin for permeabilization of mitochondria. Anal. Biochem. 313 (2003) 46-52
34. Grivennikova V.G., Maklashina E.O., Gavrikova E.V., and 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
35. Swatditat A., and Tsen C.C. Determining simple sulfhydryl compounds (low molecular weight) and their contents in biological samples by using 2,2′-dithiobis-(5-nitropyridine). Anal. Biochem. 45 (1972) 349-356
36. Grivennikova V.G., Ushakova A.V., Cecchini G., and Vinogradov A.D. Unidirectional effect of lauryl sulfate on the reversible NADH:ubiquinone oxidoreductase (Complex I). FEBS Lett. 549 (2003) 39-42
37. Taylor E.R., Hurrell F., Shannon R.J., Lin T.K., Hirst J., and Murphy M.P. Reversible glutathionylation of complex I increases mitochondrial superoxide formation. J. Biol. Chem. 278 (2003) 19603-19610
38. Ushakova A.V., Duarte M., Vinogradov A.D., and Videira A. The 29.9 kDa subunit of mitochondrial complex I is involved in the enzyme active/de-active transitions. J. Mol. Biol. 351 (2005) 327-333