76
Views
7
CrossRef citations to date
0
Altmetric
Original Articles

Gene Organization for Nitric Oxide Reduction in Alcaligenes faecalis S-6

, , &
Pages 852-857 | Received 30 Aug 1999, Accepted 03 Dec 1999, Published online: 22 May 2014

  • 1) Kakutani, T., Beppu, T., and Arima, K., Regulation of nitrite reductase in the denitrifying bacterium Alcaligenes faecalis. Agric. Biol. Chem., 45, 23-28 (1981).
  • 2) Kakutani, T., Watanabe, H., Arima, K., and Beppu, T., Purification and properties of a copper-containing nitrite reductase from a denitrifying bacterium, Alcaligenes faecalis. J. Biochem., 89, 453-461 (1981).
  • 3) Kakutani, T., Watanabe, H., Arima, K., and Beppu, T., A blue protein as an inactivating factor for nitrite reductase from Alcaligenes faecalis. J. Biochem., 89, 463-472 (1981).
  • 4) Nishiyama, M., Suzuki, J., Kukimoto, M., Ohnuki, T., Horinouchi, S., and Beppu, T., Cloning and characterization of a nitrite reductase gene from Alcaligenes faecalis and its expression in Escherichia coli. J. Gen. Microbiol., 139, 725-733 (1993).
  • 5) Yamamoto, K., Uozumi, T., and Beppu, T., The blue copper protein gene of Alcaligenes faecalis S-6 directs secretion of blue copper protein from Escherichia coli cells. J. Bacteriol., 169, 5648-5652 (1987).
  • 6) Kukimoto, M., Nishiyama, M., Murphy, M. E. P., Turley, S., Adman, E. T., Horinouchi, S., and Beppu, T., X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: roles of two copper atoms in nitrite reduction. Biochemistry, 33, 5246-5252 (1994).
  • 7) Kukimoto, M., Nishiyama, M., Ohnuki, T., Turley, S., Adman, E. T., Horinouchi, S., and Beppu, T., Identification of interaction site of pseudoazurin with its redox partner, copper-containing nitrite reductase from Alcaligenes faecalis S-6. Protein Eng., 8, 153-158 (1995).
  • 8) Kukimoto, M., Nishiyama, M., Tanokura, M., Adman, E. T., and Horinouchi, S., Studies on protein-protein interaction between copper-containing nitrite reductase and pseudoazurin from Alcaligenes faecalis S-6. J. Biol. Chem., 271, 13680-13683 (1996).
  • 9) Kukimoto, M., Nishiyama, M., Tanokura, M., Murphy, M. E. P., Adman, E. T., and Horinouchi, S., Site-directed mutagenesis of azurin from Pseudomonas aeruginosa enhances the formation of an electron-transfer complex with a copper-containing nitrite reductase from Alcaligenes faecalis S-6. FEBS Lett., 394, 87-90 (1996).
  • 10) Ye, R. W., Averill, B. A., and Tiedje, J. M., Denitrification: production and consumption of nitric oxide. Appl. Environ. Microbiol., 60, 1053-1058 (1994).
  • 11) Zumft, W. G., The biological role of nitric oxide in bacteria. Arch. Microbiol., 160, 253-264 (1993).
  • 12) Ye, R. W., Arunakumari, A., Averill, B. A., and Tiedje, J. M., Mutants of Pseudomonas fluorescens deficient in dissimilatory nitrite reduction are also altered in nitric oxide reduction. J. Bacteriol., 174, 2560-2564 (1992).
  • 13) Ye, R. W., Averill, B. A., and Tiedje, J. M., Characterization of Tn5 mutants deficient in dissimilatory nitrite reduction in Pseudomonas sp. strain G-179, which contains a copper nitrite reductase. J. Bacteriol., 174, 6653-6658 (1992).
  • 14) Heiss, B., Frunzke, K., and Zumft, W. G., Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri. J. Bacteriol., 171, 3288-3297 (1989).
  • 15) Carr, G. J. and Ferguson, S., The nitric oxide reductase of Paracoccus denitrificans. Biochem. J., 269, 423-429 (1990).
  • 16) Dermastia, M., Turk, T., and Hollocher, T. C., Nitric oxide reductase: purification from Paracoccus denitrificans with use of a single column and some characteristics. J. Biol. Chem., 266, 10899-10905 (1992).
  • 17) Jones, A. M. and Hollocher, T. C., Nitric oxide reductase of Achromobacter cycloclastes. Biochim. Biophys. Acta, 1144, 359-366 (1993).
  • 18) Nakahara, K., Tanimoto, T., Hatano, K., Usuda, K., and Shoun, H., Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor. J. Biol. Chem., 268, 8350-8355 (1993).
  • 19) Thomas, P. E., Ryan, D., and Levin, W., An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal. Biochem., 75, 168-176 (1976).
  • 20) Bedzyk, L., Wang, T., and Ye, R. W., The periplasmic nitrate reductase in Pseudomonas sp. strain G-179 catalyzes the first step of denitrificaion. J. Bacteriol., 181, 2802-2806 (1999).
  • 21) De Boer, A. P. N., Van der Oost, J., Reijnders, W. N. M., Westerhoff, H. V., Stouthamer, A. H., and Spanning, R. J. M., Mutational analysis of the nor gene cluster which encodes nitric-oxide reductase from Paracoccus denitrificans. Eur. J. Biochem., 242, 592-600 (1996).
  • 22) Bartnikas, T. B., Tosques, I. E., Laratta, W. P., Shi, J., and Shapleigh, J. P., Characterization of the nitric oxide reductase-encoding region in Rhodobacter sphaeroides 2.4.3. J. Bacteriol., 179, 3534-3540 (1997).
  • 23) Arai, H., Igarashi, Y., and Kodama, T., The structural genes for nitric oxide reductase from Pseudomonas aeruginosa. Biochim. Biophys. Acta, 1261, 279-284 (1995).
  • 24) Zumft, W. G., Braun, C., and Cuypers, H., Nitric oxide reductase from Pseudomonas stutzeri: primary structure and gene organization of a novel bacterial cytochrome bc complex. Eur. J. Biochem., 219, 481-490 (1994).
  • 25) Arai, H., Igarashi, Y., and Kodama, T., Structure and ANR-dependent transcription of the nir genes for denitrification from Pseudomonas aeruginosa. Biosci. Biotechnol. Biochem., 58, 1286-1291 (1994).
  • 26) Spiro, S. and Guest, J. R., FNR and its role in oxygen-regulated gene expression in Escherichia coli. FEMS Microbiol. Rev., 75, 399-428 (1990).
  • 27) Vollack, K. U., Xie, J., Hartig, E., Romling, U., and Zumft, W. G., Localization of denitrification genes on the chromosomal map of Pseudomonas aeruginosa. Microbiology, 144, 441-448 (1998).
  • 28) Spanning, R. J. M., De Boer, A. P. N., Reijnders, W. N. M., Spiro, S., Westerhoff, H. V., Stouthamer, A. H., and Van der Oost, J., Nitrite and nitric oxide reduction in Paracoccus denitrificans is under the controle of NNR, a regulatory protein that belongs to the FNR family of transcriptional activators. FEBS Lett., 360, 151-154 (1995).
  • 29) Jüngst, A. and Zumft, W. G., Interdependence of respiratory NO reduction and nitrite reduction revealed by mutagenesis of nirQ, a novel gene in the denitrification gene cluster of Pseudomonas stutzeri. FEBS Lett., 314, 308-314 (1992).
  • 30) Arai, H., Kodama, T., and Igarashi, Y., The role of the nirQOP genes in energy conservation during anaerobic growth of Pseudomonas aeruginosa. Biosci. Biotechnol. Biochem., 62, 1995-1999 (1998).
  • 31) Vollack, K. U., Hartig, E., Korner, H., and Zumft, W. G., Multiple transcription factors of the FNR family in denitrifying Pseudomonas stutzeri: characterization of four fnr-like genes, regulatory responses and cognate metabolic processes. Mol. Microbiol., 31, 1681-1694 (1999).

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.