685
Views
31
CrossRef citations to date
0
Altmetric
Original Articles

Electron Transfer Ability from NADH to Menaquinone and from NADPH to Oxygen of Type II NADH Dehydrogenase of Corynebacterium glutamicum

, , , , &
Pages 149-159 | Received 30 Aug 2004, Accepted 04 Nov 2004, Published online: 22 May 2014

  • 1) Yagi, T., Seo, B. B., Di Bernardo, S., Nakamura-Ogiso, E., Kao, M. C., and Matsuno-Yagi, A., NADH dehydrogenases: from basic science to biomedicine. J. Bioenerg. Biomembr., 33, 233–242 (2001).
  • 2) Videira, A., and Duarte, M., From NADH to ubiquinone in Neurospora mitochondria. Biochim. Biophys. Acta, 1364, 89–100 (2002).
  • 3) de Vries, S., and Grivell, L. A., Purification and characterization of a rotenone-insensitive NADH:Q6 oxidareductase from mitochondria of Saccharomyces cerevisiae. Eur. J. Biochem., 176, 377–384 (1988).
  • 4) Matsushita, K., Ohnishi, T., and Kaback, R., NADH–ubiquinone oxidoreductase of the Escherichia coli aerobic respiratory chain. Biochemistry, 26, 7732–7737 (1987).
  • 5) 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, 109–122 (1993).
  • 6) Young, I. G., Rogers, B. L., Campbell, H. D., Jaworowski, A., and Shaw, D. C., Nucleotide sequence coding for the respiratory NADH dehydrogenase of Escherichia coli. UUG initiation codon. Eur. J. Biochem., 116, 165–170 (1981).
  • 7) Yagi, T., Isolation of NADH dehydrogenase complex from Paracoccus membranes. Arch. Biochem. Biophys., 250, 302–311 (1986).
  • 8) Bergsma, J., Strijker, R., Alkema, J. Y., Seijen, H. G., and Koning, W. N., NADH dehydrogenase and NADH oxidation in membrane vesicle from Bacillus subtilis. Eur. J. Biochem., 120, 599–606 (1981).
  • 9) Leif, H., Sled, V. D., Ohnishi, T., Weiss, H., and Friedrich, T., Isolation and characterization of the proton translocating NADH:ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem., 230, 538–548 (1995).
  • 10) David, P., Baumann, M., Wikstrom, M., and Finel, M., Interaction of purified NDH-1 from Escherichia coli with ubiquinone analogues. Biochim. Biophys. Acta, 1553, 268–278 (2002).
  • 11) 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, 968–981 (1993).
  • 12) Yano, T., Magnitsky, S., Sled, V. D., Ohnishi, T., and Yagi, T., Characterization of the putative 2x[4Fe-4S]-binding NQO9 subunit of the proton-translocating NADH–quinone oxidoreductase (NDH-1) of Paracoccus denitrificans. Expression, reconstitution, and EPR characterization. J. Biol. Chem., 274, 28598–28605 (1999).
  • 13) Jaworowski, A., Campbell, H. D., Poulis, M. I., and Young, I. G., Genetic identification and purification of the respiratory NADH dehydrogenase from Escherichia coli. Biochemistry, 20, 2041–2047 (1981).
  • 14) Bjorklof, K., Zickermann, V., and Finel, M., Purification of the 45 kDa, membrane bound NADH dehydrogenase of Escherichia coli (NDH-2) and analysis of its interaction with ubiquinone analogues. FEBS Lett., 467, 105–110 (2000).
  • 15) Bergsma, J., Van Dongen, M. B., and Konings, W. N., Purification and characterization of NADH dehydrogenase from Bacillus subtilis. Eur. J. Biochem., 128, 151–157 (1982).
  • 16) Cook, S. A., and Shiemke, A. K., Evidence that a type-2 NADH:quinone oxidoreductase mediates electron transfer to particulate methane monooxygenase in Methylococcus capsulatus. Arch. Biochem. Biophys., 398, 32–40 (2002).
  • 17) Gomes, C. M., Bandeiras, T. M., and Teixeira, M., A new type-II NADH dehydrogenase from archaeon acidianus ambivalens: Characterization and in vitro reconstitution of the respiratory chain. J. Bioenerg. Biomembr., 33, 1–8 (2001).
  • 18) Bandeiras, T. M., Salgueiro, C. A., Huber, H., Gomes, C. M., and Teixeira, M., The respiratory chain of the thermophilic archaeon Sulfolobus metallicus: studies on the type-II NADH dehydrogenase. Biochim. Biophys. Acta, 1557, 13–19 (2003).
  • 19) Rapisarda, V. A., Chehin, R. N., De Las Rivas, J., Rodriguez-Montelongo, L., Farias, R. N., and Massa, E. M., Evidence for Cu(I)–thiolate ligation and prediction of a putative copper-binding site in the Escherichia coli NADH dehydrogenase-2. Arch. Biochem. Biophys., 405, 87–94 (2002).
  • 20) Matsushita, K., Yamamoto, T., Toyama, H., and Adachi, O., NADPH oxidase system works as superoxide-generating cyanide-resistant pathway in the respiratory chain of Corynebacterium glutamicum. Biosci. Biotechnol. Biochem., 62, 1968–1977 (1998).
  • 21) Molenarr, D., Van der Rest, M. E., and Petrovic, S., Biochemical and genetic characterization of the membrane-associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum. Eur. J. Biochem., 254, 395–403 (1998).
  • 22) Niebisch, A., and Bott, M., Molecular analysis of the cytochrome bc 1-aa 3 branch of the Corynebacterium glutamicum respiratory chain containing an unusual diheme cytochrome c 1. Arch. Microbiol., 175, 282–294 (2001).
  • 23) Sakamoto, J., Shibata, T., Mine, T., Miyahara, R., Torigoe, T., Noguchi, S., Matsushita, K., and Sone, N., Cytochrome c oxidase contains an extra charged amino acid cluster in a new type of respiratory chain in the amino-acid-producing Gram-positive bacterium Corynebacterium glutamicum. Microbiology, 147, 2865–2871 (2001).
  • 24) Kusumoto, K., Sakiyama, M., Sakamoto, J., Noguchi, S., and Sone, N., Menaquinone oxidase activity and primary structure of cytochrome bd from the amino-acid fermenting bacterium Corynebacterium glutamicum. Arch. Microbiol., 173, 390–397 (2000).
  • 25) Matsushita, K., Otofuji, A., Iwahashi, M., Toyama, H., and Adachi, O., NADH dehydrogenase of Corynebacterium glutamicum. Purification of NADH dehydrogenase II homologue able to oxidize NADPH. FEMS Microbiol. Lett., 204, 271–276 (2001).
  • 26) Molenaar, D., Van der Rest, M. E., Drysch, A., and Yucel, R., Functions of the membrane-associated and cytoplasmic malate dehydrogenases in the citric acid cycle of Corynebacterium glutamicum. J. Bacteriol., 182, 6884–6891 (2000).
  • 27) Nantapong, N., Kugimiya, Y., Toyama, H., Adachi, O., and Matsushita, K., Effect of NADH dehydrogenase-disruption and over-expression on the respiratory-related metabolism in Corynebacterium glutamicum KY9714. App. Microbiol. Biotechnol., 66, 187–193 (2004).
  • 28) Messner, K. R., and Imlay, J. A., The identification of primary sites of superoxide and hydrogen peroxide formation in the aerobic respiratory chain and sulfite reductase complex of Escherichia coli. J. Biol. Chem., 274, 10119–10128 (1999).
  • 29) Vasquez-Vivar, J., Kalyanaraman, B., Martasek, P., Hogg, N., Masters, B. S., Karoui, H., Tordo, P., and Pritchard, K. A., Jr., Superoxide generation by endothelial nitric oxide synthase: the influence of cofactors. Proc. Natl. Acad. Sci. U.S.A., 95, 9220–9225 (1998).
  • 30) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685 (1970).
  • 31) Dulley, J. R., and Grieve, P. A., A simple technique for eliminating interference by detergents in the Lowry method of protein determination. Anal. Biochem., 64, 136–141 (1975).
  • 32) Siegel, L. M., Quantitative determination of noncovalently bound flavins: types and methods of analysis. Methods Enzymol., 53, 419–429 (1978).
  • 33) Fang, J., and Beattie, D. S., Rotenone-insensitive NADH dehydrogenase is a potential source of superoxide in procyclic Trypanosoma brucei mitochondria. Mol. Biochem. Parasitol., 123, 135–142 (2002).
  • 34) Fang, J., and Beattie, D. S., External alternative NADH dehydrogenase of Saccharomyces cerevisiae: a potential source of superoxide. Free Radical Biol. Med., 34, 478–488 (2003).
  • 35) Carneiro, P., Duarte, M., and Videira, A., The main external alternative NAD(P)H dehydrogenase of Neurospora crassa mitochondria. Biochim. Biophys. Acta, 1608, 45–52 (2004).
  • 36) Bandeiras, T. M., Salgueiro, C., Kletzin, A., Gomes, C. M., and Teixeira, M., Acidianus ambivalens type-II NADH dehydrogenase: genetic characterisation and identification of the flavin moiety as FMN. FEBS Lett., 531, 273–277 (2002).
  • 37) Melo, A. M., Duarte, M., Moller, I. M., Prokisch, H., Dolan, P. L., Pinto, L., Nelson, M. A., and Videira, A., The external calcium-dependent NADPH dehydrogenase from Neurospora crassa mitochondria. J. Biol. Chem., 276, 3947–3951 (2001).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.