BMB Reports

Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
권호 표지
DOI QR코드

DOI QR Code

Enzymatic Properties of the Membrane-bound NADH Oxidase System in the Aerobic Respiratory Chain of Bacillus cereus

  • Kim, Man-Suk (Department of Microbiology, Changwon National University) ;
  • Kim, Young-Jae (Department of Microbiology, Changwon National University)
  • Published : 2004.11.30
Download PDF
⟨ Previous Next ⟩

Abstract

Membranes prepared from Bacillus cereus KCTC 3674, grown aerobically on a complex medium, oxidized NADH exclusively, whereas deamino-NADH was little oxidized. The respiratory chain-linked NADH oxidase exhibited an apparent $K_m$ value of approximately $65\;{\mu}m$ for NADH. The maximum activity of the NADH oxidase was obtained at about pH 8.5 in the presence of 0.1 M KCl (or NaCl). Respiratory chain inhibitor 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO) inhibited the activity of the NADH oxidase by about 90% at a concentration of $40\;{\mu}m$. Interestingly, rotenone and capsaicin inhibited the activity of the NADH oxidase by about 60% at a concentration of $40\;{\mu}m$ and the activity was also highly sensitive to $Ag^+$.

Keywords

References

  1. Asano, M., Hayashi, M., Unemoto, T. and Tokuda, H. (1985) $Ag^+$- sensitive NADH dehydrogenase in the $Na^+$-motive respiratory chain of the marine bacterium Vibrio alginolyticus. Agric. Biol. Chem. Biosci. Biotechnol. Biochem. 49, 2813-2817.
  2. Kim, S. S., Rhee, I. and Kim, Y. J. (2001) Purification and characterization of a novel extracellular protease from Bacillus cereus KCTC 3674. Arch. Microbiol. 175, 458-461. https://doi.org/10.1007/s002030100282
  3. Kim, S. S., Park, Y., Lee, J., Yoon, J., Shin, Y., Rhee, I. and Kim, Y. J. (1998) Taxonomic studies of the beta hemolysis-causing pathogen Bacillus cereus isolated from sea water. J. Microbiol. Biotech. 8, 67-73.
  4. Kim, Y. J., Song, K. and Rhee, S. (1995) A novel aerobic respiratory chain-linked NADH oxidase system in Zymomonas mobilis. J. Bacteriol. 177, 5176-5178.
  5. Kim, Y. J., Mizushima, S. and Tokuda, H. (1991) Fluorescence quenching studies on the characterization of energy generated at the NADH:quinone oxidoreductase and quinol oxidase segments of marine bacteria. J. Biochem. Tokyo 109, 616-621.
  6. Matsushita, K., Ohnishi, T. and Kaback, R. (1987) NADH: ubiquinone oxidoreductase of the Escherichia coli aerobic respiratory chain. Biochemistry 26, 7732-7737. https://doi.org/10.1021/bi00398a029
  7. Tokuda, H. (1983) Isolation of Vibrio alginolyticus mutants defective in the respiration-coupled $Na^+$ pump. Biochem. Biophys. Res. Commun. 114, 113-118. https://doi.org/10.1016/0006-291X(83)91601-7
  8. Tokuda, H and Unemoto, T. (1984) $Na^+$ is translocated at NADH:quinone oxidoreductase segment in the respiratory chain of Vibrio alginolyticus. J. Biol. Chem. 259, 7785-7790.
  9. Yagi, T. (1990) Inhibition by capsaicin of NADH-quinone oxidoreductases is correlated with the presence of energycoupling site 1 in various organisms. Arch. Biochem. Biophys. 281, 305-311. https://doi.org/10.1016/0003-9861(90)90448-8
  10. Yagi, T., Hoh-nami, K. and Ohnishi, T. (1988) Purification and characterization of two types of NADH-quinone reductase from Thermus thermophilus HB-8. Biochemistry 27, 2008-2013. https://doi.org/10.1021/bi00406a030
  11. Yagi, T., Yano, T., Bernardo, S. D. and Matsuno-Yagi, A. (1998) Procaryotic complex (NDH-1), an overview. Biochim. Biophys. Acta 1364, 125-133. https://doi.org/10.1016/S0005-2728(98)00023-1

Cited by

  1. Apoptosis-inducing Factor (AIF) and Its Family Member Protein, AMID, Are Rotenone-sensitive NADH:Ubiquinone Oxidoreductases (NDH-2) vol.290, pp.34, 2015, https://doi.org/10.1074/jbc.M115.641498
  2. NADH: flavin oxidoreductase/NADH oxidase and ROS regulate microsclerotium development in Nomuraea rileyi vol.30, pp.7, 2014, https://doi.org/10.1007/s11274-014-1610-7
  3. Breaking down the wall: Fractionation of mycobacteria vol.68, pp.1, 2007, https://doi.org/10.1016/j.mimet.2006.05.016
  4. Fluorescent properties of c-type cytochromes reveal their potential role as an extracytoplasmic electron sink in Geobacter sulfurreducens vol.10, pp.2, 2008, https://doi.org/10.1111/j.1462-2920.2007.01470.x
  5. Analyze and compare metabolic pathways of Bacillus cereus group vol.33, pp.10, 2011, https://doi.org/10.3724/SP.J.1005.2011.01057
  6. A secondary mode of action of polymyxins against Gram-negative bacteria involves the inhibition of NADH-quinone oxidoreductase activity vol.67, pp.2, 2014, https://doi.org/10.1038/ja.2013.111
  7. Comparison of alkyl hydroperoxide reductase and two water-forming NADH oxidases from Bacillus cereus ATCC 14579 vol.96, pp.5, 2012, https://doi.org/10.1007/s00253-012-3919-1
  8. Coenzyme regeneration catalyzed by NADH oxidase from Lactococcus lactis vol.88, 2014, https://doi.org/10.1016/j.bej.2014.04.001
  9. Molecular Mechanisms of Colistin-Induced Nephrotoxicity vol.24, pp.3, 2019, https://doi.org/10.3390/molecules24030653