The mitochondrial and prokaryotic proton-translocating NADH:ubiquinone oxidoreductases: Similarities and dissimilarities of the quinone-junction sites

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1607, Issue 2-3, 2003, Pages 79-90

  Grivennikova, Vera G ^a   Roth, Robert ^b   Zakharova, Natalia V ^a   Hägerhäll, Cecilia ^b   Vinogradov, Andrei D ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b LUND UNIVERSITY   (Sweden)

Author keywords

Bovine heart submitochondrial particle; Complex I; NADH:ubiquinone reductase; NDH 1; Paracoccus denitrificans membrane; Piericidin; Respiratory chain; Rhodobacter capsulatus membrane; Tightly bound inhibitor; Ubiquinone

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; NUCLEOTIDE; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); ROTENONE; TRITON X 100;

ARTICLE; BACTERIAL STRAIN; BINDING AFFINITY; CATALYSIS; CATTLE; CHEMICAL REACTION; COMPETITIVE INHIBITION; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME METABOLISM; HYDROPHOBICITY; INTERMETHOD COMPARISON; MITOCHONDRION; NONHUMAN; PARACOCCUS DENITRIFICANS; PRIORITY JOURNAL; PROKARYOTE; PROTEIN EXPRESSION; PROTEIN INTERACTION; PROTON TRANSPORT; RHODOBACTER CAPSULATUS; TISSUE PREPARATION;

BOS; BOS TAURUS; BOVINAE; MAMMALIA; PARACOCCUS DENITRIFICANS; PROKARYOTA; RHODOBACTER; RHODOBACTER CAPSULATUS;

EID: 0345059204     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.09.001     Document Type: Article

References (65)

1. Fearnley I.M., Walker J.E. Conservation of sequences of subunits of mitochondrial Complex I and their relationships with other proteins. Biochim. Biophys. Acta. 1140:1992;105-134.
2. Carroll J., Shannon R.J., Fearnley I.M., Walker J.E., Hirst J. Definition of the nuclear encoded protein composition of bovine heart mitochondrial Complex I: identification of two new subunits. J. Biol. Chem. 277:2002;50311-50317.
3. Ohnishi T., Sled V.D., Yano T., Yagi T., Burbaev D.S., Vinogradov A.D. Structure-function studies of iron-sulfur clusters and semiquinones in the NADH:Q oxidoreductase segment of the respiratory chain. Biochim. Biophys. Acta. 1365:1998;301-308.
4. Friedrich T., Steinmuller K., Weiss H. The proton-pumping respiratory Complex I of bacteria and mitochondria and its homologue in chloroplasts. FEBS Lett. 367:1995;107-111.
5. Yagi T., Yano T., Matsuno-Yagi A. Characteristics of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans as revealed by biochemical, biophysical, and molecular biological approaches. J. Bioenerg. Biomembranes. 25:1993;339-345.
6. Dupuis A., Chevallet M., Darrouzet E., Duborjal H., Lunardi J., Issartel J.P. The Complex I from Rhodobacter capsulatus. Biochim. Biophys. Acta. 1364:1998;147-165.
7. Walker J.E. The NADH:ubiquinone oxidoreductase (Complex I) of respiratory chains. Q. Rev. Biophys. 25:1992;253-324.
8. Suzuki H., King T.E. Evidence of an ubisemiquinone radical(s) from the NADH-ubiquinone reductase of the mitochondrial respiratory chain. J. Biol. Chem. 258:1983;352-358.
9. Ragan C.I. Structure of NADH-ubiquinone reductase (Complex I). Curr. Top. Bioenerg. 15:1987;1-36.
10. Krishnamoorthy G., Hinkle P.C. Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase. J. Biol. Chem. 263:1988;17566-17575.
11. Vinogradov A.D. Kinetics, control, and mechanism of ubiquinone reduction by the mammalian respiratory chain-linked NADH-ubiquinone reductase. J. Bioenerg. Biomembranes. 25:1993;367-375.
12. Dutton P.L., Moser C.C., Sled V.D., Daldal F., Ohnishi T. A reductant-induced oxidation mechanism for Complex I. Biochim. Biophys. Acta. 1364:1998;245-257.
13. Brandt U. Proton-translocation by membrane-bound NADH:ubiquinone- oxidoreductase (Complex I) through redox-gated ligand conduction. Biochim. Biophys. Acta. 1318:1997;79-91.
14. 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.
15. Vernon L.P., White F.G. Terminal oxidases of Micrococcus denitrificans. Biochim. Biophys. Acta. 25:1957;321-328.
16. Naik M.S., Nicholas D.J.D. Phosphorylation associated with nitrate and nitrite reduction in Micrococcus denitrificans and Pseudomonas denitrificans. Biochim. Biophys. Acta. 113:1966;490-497.
17. Imai K., Asano A., Sato R. Oxidative phosphorylation in Micrococcus denitrificans: I. Preparation and properties of phosphorylating membrane fragments. Biochim. Biophys. Acta. 143:1967;462-476.
18. Imai K., Asano A., Sato R. Oxidative phosphorylation in Micrococcus denitrificans: IV. Further characterization of electron-transfer pathway and phosphorylation activity in NADH oxidation. J. Biochem. 63:1968;207-218.
19. Scholes P.B., Smith L. Composition and properties of the membrane-bound respiratory chain system of Micrococcus denitrificans. Biochim. Biophys. Acta. 153:1968;363-375.
20. Baccarini-Melandri A., Zannoni D., Melandri B.A. Energy transduction in photosynthetic bacteria: VI. Respiratory sites of energy conservation in membranes from dark-grown cells of Rhodopseudomonas capsulata. Biochim. Biophys. Acta. 314:1973;298-311.
21. Herter S.M., Kortluke C.M., Drews G. Complex I of Rhodobacter capsulatus and its role in reverted electron transport. Arch. Microbiol. 169:1998;98-105.
22. Albracht S.P.J., van Verseveld H.W., Hagen W.R., Kalkman M.L. A comparison of the respiratory chain in particles from Paracoccus denitrificans and bovine heart mitochondria by EPR spectroscopy. Biochim. Biophys. Acta. 593:1980;173-186.
23. 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.
24. Zickermann V., Kurki S., Kervinen M., Hassinen I., Finel M. The NADH oxidation domain of Complex I: do bacterial and mitochondrial enzymes catalyze ferricyanide reduction similarly? Biochim. Biophys. Acta. 1459:2000;61-68.
25. Grivennikova V.G., Serebryanaya D.V., Isakova E.P., Belozerskaya T.A., Vinogradov A.D. Active/de-active transition of NADH:ubiquinone oxidoreductase (Complex I) in the mitochondrial membrane of Neurospora crassa. Biochem. J. 369:2003;619-626.
26. John P., Whatley F.R. Oxidative phosphorylation coupled to oxygen uptake and nitrate reduction in Micrococcus denitrificans. Biochim. Biophys. Acta. 216:1970;342-352.
27. Darrouzet E., Dupuis A. Genetic evidence for the existence of two quinone related inhibitor binding sites in NADH-CoQ reductase. Biochim. Biophys. Acta. 1319:1997;1-4.
28. Darrouzet E., Issartel J.-P., Lunardi J., Dupuis A. The 49-kDa subunit of NADH-ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone-related inhibitors. FEBS Lett. 431:1998;34-38.
29. Kotlyar A.B., Vinogradov A.D. Slow active/inactive transition of the NADH:ubiquinone reductase. Biochim. Biophys. Acta. 1019:1990;151-158.
30. Burbaev D.S., Moroz I.A., Kotlyar A.B., Sled V.D., Vinogradov A.D. Ubisemiquinone in the NADH-ubiquinone reductase region of the mitochondrial respiratory chain. FEBS Lett. 254:1989;47-51.
31. John P., Hamilton W.A. Respiratory control in membrane particles from Micrococcus denitrificans. FEBS Lett. 10:1970;246-248.
32. Sholes P.B., Smith L. The isolation and properties of the cytoplasmic membrane of Micrococcus denitrificans. Biochim. Biophys. Acta. 153:1968;350-362.
33. Weaver P.F., Wall J.D., Gest H. Characterization of Rhodopseudomonas capsulata. Arch. Microbiol. 105:1975;207-216.
34. 2+ ions on the slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase. Biochim. Biophys. Acta. 1098:1992;144-150.
35. Nichols W.W., Hamilton W.A. The preparation of tightly coupled membrane vesicles from Paracoccus denitrificans. Anal. Biochem. 87:1978;91-96.
36. Gornall A.G., Bardawill C.J., David M.M. Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177:1949;751-756.
37. Burnell J.N., John P., Whatley F.R. The reversibility of active sulphate transport in membrane vesicles of Paracoccus dinitrificans. Biochem. J. 150:1975;527-536.
38. + reduction catalysed by tightly coupled inside-out vesicles from Paracoccus denitrificans. Eur. J. Biochem. 269:2002;4020-4024.
39. 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.
40. Burgos J., Redfearn E.R. The inhibition of mitochondrial reduced nicotinamide-adenine dinucleotide oxidation by rotenoids. Biochim. Biophys. Acta. 110:1965;475-483.
41. 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.
42. Ushakova A.V., Grivennikova V.G., Ohnishi T., Vinogradov A.D. Triton X-100 as a specific inhibitor of the mammalian NADH-ubiquinone oxidoreductase (Complex I). Biochim. Biophys. Acta. 1409:1999;143-153.
43. Videira A., Duarte M. From NADH to ubiquinone in Neurospora mitochondria. Biochim. Biophys. Acta. 1555:2002;187-191.
44. 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.
45. Sled V.D., Friedrich T., Leif H., Weiss H., Meinhardt S.W., Fukumori Y., Calhoun M., Gennis R.B., Ohnishi T. Bacterial NADH-quinone oxidoreductases: iron-sulfur clusters and related problems. J. Bioenerg. Biomembranes. 25:1993;347-355.
46. +/2e stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles. FEBS Lett. 451:1999;157-161.
47. Grivennikova V.G., Ushakova A.V., Hägerhäll C., Vinogradov A.D. Proton translocation catalyzed by Paracoccus denitrificans NADH:quinone oxidoreductase (NDH-1). BBA EBEC Short Rep. 12:2002;209.
48. Zharova T.V., Vinogradov A.D. A competitive inhibition of the mitochondrial NADH-ubiquinone oxidoreductase (Complex I) by ADP-ribose. Biochim. Biophys. Acta. 1320:1997;256-264.
49. Zakharova N.V., Zharova T.V., Vinogradov A.D. Kinetics of transhydrogenase reaction catalyzed by the mitochondrial NADH-ubiquinone oxidoreductase (Complex I) imply more than one catalytic nucleotide-binding sites. FEBS Lett. 444:1999;211-216.
50. Yamaguchi M., Belogrudov G.I., Matsuno-Yagi A., Hatefi Y. The multiple nicotinamide nucleotide-binding subunits of bovine heart mitochondrial NADH:ubiquinone oxidoreductase (Complex I). Eur. J. Biochem. 267:2000;329-336.
51. Walker J.E. The NADH:ubiquinone oxidoreductase (Complex I) of respiratory chains. Q. Rev. Biophys. 25:1992;253-324.
52. Bellamacina C.R. The nicotinamide dinucleotide binding motif: a comparison of nucleotide binding proteins. FASEB J. 10:1996;1257-1269.
53. +/2e stoichiometry of the NADH:ubiquinone reductase reaction catalyzed by submitochondrial particles. Biochemistry (Mosc.). 66:2001;435-443.
54. + on the interaction of rotenone with Complex I of submitochondrial particles. Biochim. Biophys. Acta. 1140:1992;169-174.
55. Jeng M., Hall C., Crane F.L., Takahashi N., Tamura S., Folkers K. Inhibition of mitochondrial electron transport by piericidin A and related compounds. Biochemistry. 7:1968;1311-1322.
56. Horgan D.J., Singer T.P. Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase: XIII. Binding sites of rotenone, piericidin A, and amytal in the respiratory chain. J. Biol. Chem. 243:1968;834-843.
57. Horgan D.J., Ohno H., Singer T.P. Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase: XV. Interactions of piericidin with the mitochondrial respiratory chain. J. Biol. Chem. 243:1968;5967-5976.
58. Gutman M., Singer T.P. Studies on the respiratory chain-linked reduced nicotinamide adenine dinucleotide dehydrogenase: XVII. Reaction sites of piericidin A and rotenone. J. Biol. Chem. 245:1970;1992-1997.
59. Gutman M., Coles C.J., Singer T.P., Casida J.E. On the functional organization of the respiratory chain at the dehydrogenase-coenzyme Q junction. Biochemistry. 10:1971;2036-2043.
60. van Belzen R., van Gaalen M.C.M., Cuypers P.A., Albracht S.P.J. New evidence for the dimeric nature of NADH:Q oxidoreductase in bovine-heart submitochondrial particles. Biochim. Biophys. Acta. 1017:1990;152-159.
61. Vinogradov A.D., Grivennikova V.G. The mitochondrial Complex I: progress in understanding of catalytic properties. UIBMB-Life. 52:2001;1-6.
62. Bechmann G., Weiss H., Rich P.R. Non-linear inhibition curves for tight-binding inhibitors of dimeric ubiquinol-cytochrome c oxidoreductases. Evidence for rapid inhibitor mobility. Eur. J. Biochem. 208:1992;315-325.
63. Trigatti B.L., Gerber G.E. A direct role of serum albumin in the cellular uptake of long-chain fatty acids. Biochem. J. 308:1995;155-159.
64. Cha S. Tight-binding inhibitors: I. Kinetic behavior. Biochem. Pharmacol. 24:1975;2177-2185.
65. Vinogradov A.D., King T.E. The Keilin-Hartree heart muscle preparation. Methods Enzymol. 55:1979;118-127.