A reductase/isomerase subunit of mitochondrial NADH:ubiquinone oxidoreductase (complex I) carries an NADPH and is involved in the biogenesis of the complex

Journal of Molecular Biology

Volumn 292, Issue 3, 1999, Pages 569-580

  Schulte, Ulrich ^a   Haupt, Verena ^a   Abelmann, Anke ^a   Fecke, Wolfgang ^a   Brors, Benedikt ^a   Rasmussen, Tim ^a   Friedrich, Thorsten ^a   Weiss, Hanns ^a  

^a HEINRICH HEINE UNIVERSITY   (Germany)

Author keywords

Complex I; NADH:ubiquinone oxidoreductase; Proton translocation; Quinoprotein; Respiratory chain

Indexed keywords

ISOMERASE; OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; BACTERIUM; BINDING SITE; BIOGENESIS; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; ENZYME SUBUNIT; GENE DISRUPTION; MITOCHONDRION; MOLECULAR WEIGHT; NEUROSPORA CRASSA; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTON TRANSPORT; RESPIRATORY CHAIN; ULTRAVIOLET SPECTROSCOPY;

EID: 0033600871     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3096     Document Type: Article

References (66)

1. Bakker P. T. A., Albracht S. P. J. Evidence for two independent pathways of electron transfer in mitochondrial NADH:Q oxidoreductase. I. Pre-steady-state kinetics with NADPH. Biochim. Biophys. Acta. 850:1986;413-422.
2. Baker M. E., Blasco R. Expansion of the mammalian 3β-hydroxysteroid dehydrogenase/plant dihydroflavonol reductase superfamily to include a bacterial cholesterol dehydrogenase, a bacterial UDP-galactose-4-epimerase, and open reading frames in vaccinia virus and fish lymphocystis disease virus. FEBS Letters. 301:1992;89-93.
3. Baumgarten B., Horst J. Spectroscopic investigation of dihydronicotinamides - II. Dihydronicotinamide adenine nucleotide complexes with dehydrogenases. Photochem. Photobiol. 47:1988;201-205.
4. Beecham J. Global analysis of biochemical and biophysical data. Methods Enzymol. 210:1991;37-54.
5. Brito F., de Moos J. A., Doubourdieu M. Isolation and identification of menaquinone-9 from purified nitrate reductase of Escherichia coli. J. Bacteriol. 177:1995;3728-3735.
6. Deckert G., Warren P. V., Graasterland T., Young W. G., Lenox A. L., Graham D. E., Overbeek R., Snead M. A., Keller M., Aujay M., Huber R., Feldman R. A., Short J. M., Olsen G. J., Swanson R. V. et al. The complete genome of the hyperthermophilic bacterium Aquifax aeolicus. Nature. 392:1998;353-358.
7. de Vries S., Grivell L. A. Purification and characterisation of a rotenone-insensitive NADH:Q6 oxidoreductase from mitochondria ofSaccharomyces cerevisae. Eur. J. Biochem. 176:1988;377-384.
8. osite model. Biochemistry. 31:1992;3144-3158.
9. Duarte M., Sousa R., Videira A. Inactivation of genes encoding subunits of the peripheral and membrane arms of Neurospora mitochondrial complex I and effects on enzyme assembly. Genetics. 139:1995;1211-1221.
10. Duarte M., Mota N., Pinto L., Videira A. Inactivation of the gene coding for the 30.4-kDa subunit of respiratory chain NADH dehydrogenase: is the enzyme essential for Neurospora ? Mol. Gen. Genet. 257:1998;368-375.
11. Ernster L., Glaser E., Norling B. Extraction and reincorporation of ubiquinone in submitochondrial particles. Methods Enzymol. 53:1978;573-578.
12. 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.
13. Fecke W., Sled V. D., Ohnishi T., Weiss H. Disruption of the gene encoding the NADH-binding subunit of NADH:ubiquinone oxidoreductase in Neurospora crassa. Formation of a partially assembled enzyme without FMN and the iron- sulphur cluster N3. Eur. J. Biochem. 220:1994;551-558.
14. Felsenstein J. PHYLIP - phylogeny interference package (version 3.2). Cladistics. 5:1989;164-166.
15. Finel M., Skehel J. M., Albracht S. P. J., Fearnley J. M., Walker J. E. Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centres of the enzyme. Biochemistry. 31:1992;11425-11434.
16. Fish W. W. Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. Methods Enzymol. 158:1988;357-364.
17. Friedrich T., Hofhaus G., Ise W., Nehls U., Schmitz B., Weiss H. A small isoform of NADH:ubiquinone oxidoreductase (complex I) without mitochondrially encoded subunits is made in chloramphenicol-treated Neurospora crassa. Eur. J. Biochem. 180:1989;173-180.
18. Friedrich T., van Heek P., Leif H., Ohnishi T., Forche E., Kunze B., Janssen R., Trowitzsch-Kienast W., Höfle G., Reichenbach H., Weiss H. Two binding sites of inhibitors in NADH:ubiquinone oxidoreductase (complex I). Eur. J. Biochem. 219:1994;691-698.
19. Friedrich T., Steinmüller K., Weiss H. The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue of chloroplasts. FEBS Letters. 367:1995;107-111.
20. Friedrich T., Abelmann A., Brors B., Guénebaut V., Kintscher L., Leonard L., Rasmussen T., Scheide D., Schlitt A., Schulte U., Weiss H. Redox components and structure of the respiratory NADH:ubiquinone oxidoreductase (complex I). Biochim. Biophys. Acta. 1365:1998;215-219.
21. Guénebaut V., Vincentelli R., Mills D., Weiss H., Leonard K. R. Three-dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction. J. Mol. Biol. 265:1997;409-418.
22. Guénebaut V., Schlitt A., Weiss H., Leonard K., Friedrich T. Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Mol. Biol. 276:1998;105-112.
23. Hofhaus G., Weiss H., Leonard K. Electron microscopic analysis of the peripheral and the membrane parts of mitochondrial NADH dehydrogenase (complex I). J. Mol. Biol. 221:1991;1027-1043.
24. Holm L., Sander C., Murzin A. Three sisters, different names. Nature Struct. Biol. 1:1994;421-422.
25. Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitfificans. Nature. 376:1995;660-669.
26. 1complex. Science. 281:1998;64-71.
27. Jörnvall H., Persson B., Krook M., Atrian S., Gonzàles-Duarte R., Jeffery J., Ghosh D. Short-chain dehydrogenases/reductases (SDR). Biochemistry. 34:1995;6003-6013.
28. Koziol J. Fluorometric analyses of riboflavin and its coenzymes. Methods Enzymol. 89:1971;253-285.
29. Kröger A. Determination of contents and redox states of ubiquinone and menaquinone. Methods Enzymol. 53:1978;570-590.
30. Leif H., Sled V. D., Ohnishi T., Weiss H., Friedrich T. Isolation and characterization of the proton-translocating NADH:ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 230:1995;538-548.
31. Linke P., Bechmann G., Gothe A., Weiss H. Dimeric ubiquinol:cytochrome c reductase of Neurospora mitochondria contain one co-operative ubiquinone reduction centre. Eur. J. Biochem. 158:1986;615-621.
32. Maeder M., Zuberbühler A. D. Non-linear least-squares fitting of multivariate absorption data. Anal. Chem. 193:1990;265-275.
33. Matsushita K., Ohnishi T., Kaback H. R. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry. 26:1987;7732-7737.
34. Nehls U., Friedrich T., Schmiede A., Ohnishi T., Weiss H. Characterization of assembly intermediates of NADH:ubiquinone oxidoreductase (complex I) accumulated inNeurospora mitochondria by gene disruption. J. Mol. Biol. 227:1992;1032-1042.
35. Orbach M. J., Porro E. B., Yanovsky C. Cloning and characterization of the gene for β-tubulin from a benomyl-resistant mutant of Neurospora crassa and its use as a dominant selectable marker. Mol. Cell. Biol. 6:1986;2452-2461.
36. Rabinowitz J. C. Analysis of acid-labile sulfide and sulfhydryl groups. Methods Enzymol. 54:1978;275-277.
37. Rasmusson A. G., Heiser V., Zabaleta E., Brennicke A., Grohmann L. Physiological, biochemical and molecular aspects of mitochondrial complex I in plants. Biochim. Biophys. Acta. 1364:1998;101-112.
38. Röhlen D. A., Hoffmann J., van der Pas J. C., Nehls U., Preis D., Sackmann U., Weiss H. Relationship between a subunit of NADH dehydrogenase (complex I) and a protein family including subunits of cytochrome reductase and processing protease from mitochondria. FEBS Letters. 278:1991;75-78.
39. Runswick M. J., Fearnley I. M., Skehel J. M., Walker J. E. Presence of an acyl-carrier protein in NADH:ubiquinone oxidoreductase from bovine heart mitochondria. FEBS Letters. 286:1991;121-124.
40. Sackmann U., Zensen R., Röhlen D., Jahnke U., Weiss H. The acyl-carrier protein in Neurospora crassa mitochondria is a subunit of NADH:Rubiquinone reductase (complex I). Eur. J. Biochem. 200:1991;463-469.
41. Schneider R., Massow M., Lisowsky T., Weiss H. Different respiratory-defective phenotypes of Neurospora crassa and Saccharomyces cerevisiae after inactivation of the gene encoding the mitochondrial acyl carrier protein. Curr. Genet. 29:1995;10-17.
42. Schneider R., Brors B., Massow M., Weiss H. Fatty acid synthesis in mitochondria: a relic of endosymbiontic origin and a specialized means for respiration. FEBS Letters. 407:1997;249-252.
43. Schulte U., Weiss H. Generation and characterization of NADH:ubiquinone oxidoreductase mutants in Neurospora crassa. Methods Enzymol. 260:1995;3-14.
44. Schulte U., Fecke W., Krüll C., Nehls U., Schmiede A., Schneider R., Ohnishi T., Weiss H. In vivo dissection of the mitochondrial respiratory chain NADH:ubiquinone oxidoreductase (complex I). Biochim. Biophys. Acta. 1187:1994;121-124.
45. Schulte U., Abelmann A., Amling N., Brors B., Friedrich T., Kintscher L., Rasmussen T., Weiss H. Search for novel redox groups in mitochondrial NADH:ubiquinone oxidoreductase (complex I) by diode array UV/VIS spectroscopy. Biofactors. 8:1998;177-186.
46. Schwitzguebel J.-P., Palmer J. M. Properties of mitochondria as a function of growth stage of Neurospora crassa. J. Bacteriol. 149:1982;612-619.
47. Scott T. G., Spencer R. D., Leonard N. J., Weber G. Emission properties of NADH. Studies of fluorescence, lifetime and quantum efficiencies of NADH, AcPyADH, and simplified synthetic models. J. Am. Chem. Soc. 92:1970;687-695.
48. Singer T. P. Mitochondrial electron-transport inhibitors. Methods Enzymol. 55:1979;454-465.
49. Staben C., Jensen B., Singer M., Pollock J. Use of a bacterial hygromycin B resistance gene as a dominant selectable marker in Neurospora crassa transformation. Fungal. Genet. Newsl. 36:1989;79-81.
50. 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.
51. Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H., Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S. The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 Å Science. 272:1996;1136-1144.
52. Tuschen G., Sackmann U., Nehls U., Haiker H., Buse G., Weiss H. Assembly of NADH:ubiquinone reductase (complex I) in Neurospora mitochondria: independent pathways of nuclear and mitochondrially encoded subunits. J. Mol. Biol. 213:1990;845-857.
53. 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.
54. Vinogradov A. D., Sled V. D., Burbaer D. S., Grivennikova V. G., Moroz I. A., Minishu T. Energy-dependent complex I-associated ubisemiquinones in submitochondrial particles. FEBS Letters. 370:1995;83-87.
55. Walker J. E. The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Quart. Rev. Biophys. 25:1992;253-324.
56. Wan Y.-P., Folkers K. Coenzyme Q and analogues for coenzymic activity. Methods Enzymol. 53:1978;591-609.
57. Wang D. C., Meinhardt S. W., Sackmann U., Weiss H., Ohnishi T. The iron-sulfur clusters in the two related forms of mitochondrial NADH:ubiquinone oxidoreductase made by Neurospora crassa. Eur. J. Biochem. 197:1991;257-264.
58. Weidner U., Geier S., Ptock A., Friedrich T., Leif H., 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.
59. Weiss H., von Jagow G., Klingenberg M., Bücher T. Characterization of Neurospora crassa mitochondria prepared with a grind-mill. Eur. J. Biochem. 14:1970;75-82.
60. 1complex from bovine heart mitochondria. Science. 277:1997;60-66.
61. Xu X., Matsuno-Yagi A., 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.
62. Yagi T. The bacterial energy-transducing NADH-quinone oxidoreductases. Biochim. Biophys. Acta. 1141:1993;1-17.
63. Yamaguchi M., Belogrudov G. I., Hatefi Y. Mitochondrial NADH-ubiquinone oxidoreductase (complex I), effect of substrates on the fragmentation of subunits by trypsin. J. Biol. Chem. 273:1998;8094-8098.
64. Yan T., Chu S. C., Sled V. D., Ohnishi T., Yagi T. The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8. J. Biol. Chem. 272:1997;4201-4211.
65. Yoshikawa S., Shinanzawa-Itoh K., Nakashima R., Yaono R., Yamashita E., Inoue N., Yao M., Fei M. J., Libeu C. P., Mizushima T., Yamaguchi H., Tomizaki T., Tsukihara T. Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Science. 280:1998;1723-1729.
66. 1. Nature. 392:1998;677-684.