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Octaheme nitrite reductases: Structure and properties

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Abstract

Octaheme oxidoreductases are widespread among various bacterial taxa involved in the biogeochemical nitrogen cycle. The evolution of octaheme oxidoreductases of the nitrogen cycle from the evolutionarily more ancient pentaheme nitrite reductases was accompanied by changes in function from reduction of nitrogen oxides to their oxidation under changing environmental conditions. Octaheme nitrite reductases, which are the subject of the present review, are of a transitional form that combines structural and functional characteristics of pentaheme reductases and octaheme oxidases and possesses a number of unique features typical of only this family of enzymes. The review summarizes data on structure-function investigations of the family of octaheme nitrite reductases. Emphasis is given to comparison of the structures and functions of octaheme nitrite reductases and other multiheme oxidoreductases of the nitrogen cycle.

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Abbreviations

HAO:

octaheme hydroxylamine oxidoreductase

MCC:

multiheme cytochrome c

NrfA:

pentaheme cytochrome c nitrite reductase encoded by the nrfA gene (nitrite reduction with formate)

ONR:

octaheme nitrite reductase

OTR:

octaheme tetrathionate reductase

rmsd:

root mean square deviation

TvNiR:

octaheme nitrite reductase from Thioalkalivibrio nitratireducens

TvPaR:

octaheme nitrite reductase from Thioalkalivibrio paradoxus

References

  1. Simon, J., Kern, M., Hermann, B., Einsle, O., and Butt, J. N. (2011) Biochem. Soc. Trans., 39, 1864–1870.

    Article  PubMed  CAS  Google Scholar 

  2. Simon, J. (2002) FEMS Microbiol. Rev., 26, 285–309.

    Article  PubMed  CAS  Google Scholar 

  3. Kajie, S., and Anraku, Y. (1986) Eur. J. Biochem., 154, 457–463.

    Article  PubMed  CAS  Google Scholar 

  4. Almeida, M. G., Macieira, S., Goncalves, L. L., Huber, R., Cunha, C. A., Romao, M. J., Costa, C., Lampreia, J., Moura, J. J. G., and Moura, I. (2003) Eur. J. Biochem., 270, 3904–3915.

    Article  PubMed  CAS  Google Scholar 

  5. Pereira, I. A. C., LeGall, J., Xavier, A. V., and Teixeira, M. (2000) Biochim. Biophys. Acta, 1481, 119–130.

    Article  PubMed  CAS  Google Scholar 

  6. Stach, P., Einsle, O., Schumacher, W., Kurun, E., and Kroneck, P. M. H. (2000) J. Inorg. Biochem., 79, 381–385.

    Article  PubMed  CAS  Google Scholar 

  7. Rudolf, M., Einsle, O., Neese, F., and Kroneck, P. M. H. (2002) Biochem. Soc. Trans., 30, 649–653.

    Article  PubMed  CAS  Google Scholar 

  8. Angove, H. C., Cole, J. A., Richardson, D. J., and Butt, J. N. (2002) J. Biol. Chem., 277, 23374–23381.

    Article  PubMed  CAS  Google Scholar 

  9. Clarke, T. A., Hemmings, A. M., Burlat, B., Butt, J. N., Cole, J. A., and Richardson, D. J. (2006) Biochem. Soc. Trans., 34, 143–145.

    Article  PubMed  CAS  Google Scholar 

  10. Van Wonderen, J. H., Burlat, B., Richardson, D. J., Cheesman, M. R., and Butt, J. N. (2008) J. Biol. Chem., 283, 9587–9594.

    Article  PubMed  Google Scholar 

  11. Poock, S. R., Leach, E. R., Moir, J. W. B., Cole, J. A., and Richardson, D. J. (2002) J. Biol. Chem., 277, 23664–23669.

    Article  PubMed  CAS  Google Scholar 

  12. Liu, M.-C., and Peck, H. D., Jr. (1981) J. Biol. Chem., 256, 13159–13164.

    PubMed  CAS  Google Scholar 

  13. Pereira, I. C., Abreu, I. A., Xavier, A. V., LeGall, J., and Teixeira, M. (1996) Biochem. Biophys. Res. Commun., 224, 611–618.

    Article  PubMed  CAS  Google Scholar 

  14. Lukat, P., Rudolf, M., Stach, P., Messerschmidt, A., Kroneck, P. M. H., Simon, J., and Einsle, O. (2008) Biochemistry, 47, 2080–2086.

    Article  PubMed  CAS  Google Scholar 

  15. Kemp, G. L., Clarke, T. A., Marritt, S. J., Lockwood, C., Poock, S. R., Hemmings, A. M., Richardson, D. J., Cheesman, M. R., and Butt, J. N. (2010) Biochem. J., 431, 73–80.

    Article  PubMed  CAS  Google Scholar 

  16. Kern, M., Volz, J., and Simon, J. (2011) Environ. Microbiol., 13, 2478–2494.

    Article  PubMed  CAS  Google Scholar 

  17. Einsle, O., Messerschmidt, A., Stach, P., Bourenkov, G. P., Bartunik, H. D., Huber, R., and Kroneck, P. M. (1999) Nature, 400, 476–480.

    Article  PubMed  CAS  Google Scholar 

  18. Einsle, O., Stach, P., Messerschmidt, A., Simon, J., Kroger, A., Huber, R., and Kroneck, P. M. (2000) J. Biol. Chem., 275, 39608–39616.

    Article  PubMed  CAS  Google Scholar 

  19. Bamford, V. A., Angove, H. C., Seward, H. E., Thomson, A. J., Cole, J. A., Butt, J. N., Hemmings, A. M., and Richardson, D. J. (2002) Biochemistry, 41, 2921–2931.

    Article  PubMed  CAS  Google Scholar 

  20. Cunha, C. A., Macieira, S., Dias, J. M., Almeida, G., Goncalves, L. L., Costa, C., Lampreia, J., Huber, R., Moura, J. J., Moura, I., and Romao, M. J. (2003) J. Biol. Chem., 278, 17455–17465.

    Article  PubMed  CAS  Google Scholar 

  21. Rodrigues, M. L., Oliveira, T. F., Pereira, I. A., and Archer, M. (2006) EMBO J., 25, 5951–5960.

    Article  PubMed  CAS  Google Scholar 

  22. Lockwood, C. W. J., Clarke, T. A., Butt, J. N., Hemmings, A. M., and Richardson, D. J. (2011) Biochem. Soc. Trans., 39, 1871–1875.

    Article  PubMed  CAS  Google Scholar 

  23. Einsle, O., Messerschmidt, A., Huber, R., Kroneck, P. M. H., and Neese, F. (2002) J. Am. Chem. Soc., 124, 11737–11745.

    Article  PubMed  CAS  Google Scholar 

  24. Moser, C. C., Anderson, J. L., and Dutton, P. L. (2010) Biochim. Biophys. Acta, 1797, 1573–1586.

    Article  PubMed  CAS  Google Scholar 

  25. Fonseca, B. M., Paquete, C. M., Salgueiro, C. A., and Louro, R. O. (2012) FEBS Lett., 586, 504–509.

    Article  PubMed  CAS  Google Scholar 

  26. Lockwood, C., Butt, J. N., Clarke, T. A., and Richardson, D. J. (2011) Biochem. Soc. Trans., 39, 263–268.

    Article  PubMed  CAS  Google Scholar 

  27. Mowat, C. G., and Chapman, S. K. (2005) Dalton Trans., 3381–3389.

  28. Igarashi, N., Moriyama, H., Fujiwara, T., Fukumori, Y., and Tanaka, N. (1997) Nat. Struct. Biol., 4, 276–284.

    Article  PubMed  CAS  Google Scholar 

  29. Mowat, C. G., Rothery, E., Miles, C. S., McIver, L., Doherty, M. K., Drewette, K., Taylor, P., Walkinshaw, M. D., Chapman, S. K., and Reid, G. A. (2004) Nat. Struct. Mol. Biol., 11, 1023–1024.

    Article  PubMed  CAS  Google Scholar 

  30. Atkinson, S. J., Mowat, C. G., Reid, G. A., and Chapman, S. K. (2007) FEBS Lett., 581, 3805–3808.

    Article  PubMed  CAS  Google Scholar 

  31. Klotz, M. G., Schmid, M. C., Strous, M., Op den Camp, H. J. M., Jetten, M. S. M., and Hooper, A. B. (2008) Environ. Microbiol., 10, 3150–3163.

    Article  PubMed  CAS  Google Scholar 

  32. Bergmann, D. J., Hooper, A. B., and Klotz, M. G. (2005) Appl. Environ. Microbiol., 71, 5371–5382.

    Article  PubMed  CAS  Google Scholar 

  33. Tikhonova, T., Tikhonov, A., Trofimov, A., Polyakov, K., Boyko, K., Cherkashin, E., Rakitina, T., Sorokin, D., and Popov, V. (2012) FEBS J., in press.

  34. Tikhonova, T. V., Slutsky, A., Antipov, A. N., Boyko, K. M., Polyakov, K. M., Sorokin, D. Y., Zvyagilskaya, R. A., and Popov, V. O. (2006) Biochim. Biophys. Acta, 1764, 715–723.

    Article  PubMed  CAS  Google Scholar 

  35. Polyakov, K. M., Boyko, K. M., Tikhonova, T. V., Slutsky, A., Antipov, A. N., Zvyagilskaya, R. A., Popov, A. N., Bourenkov, G. P., Lamzin, V. S., and Popov, V. O. (2009) J. Mol. Biol., 389, 846–862.

    Article  PubMed  CAS  Google Scholar 

  36. Foti, M., Ma, S., Sorokin, D. Y., Rademaker, J. L. W., Kuenen, J. G., and Muyzer, G. (2006) FEMS Microbiol. Ecol., 56, 95–101.

    Article  PubMed  CAS  Google Scholar 

  37. Sorokin, D. Yu., Tourova, T. P., Lysenko, A. M., Mityushina, L. L., and Kuenen, J. G. (2002) Int. J. Syst. Evol. Microbiol., 52, 657–664.

    PubMed  CAS  Google Scholar 

  38. Sorokin, D. Yu., Tourova, T. P., Sjollema, K. A., and Kuenen, J. G. (2003) Int. J. Syst. Evol. Microbiol., 53, 1779–1783.

    Article  PubMed  CAS  Google Scholar 

  39. Hendrich, M. P., Upadhyay, A. K., Riga, J., Arciero, D. M., and Hooper, A. B. (2002) Biochemistry, 41, 4603–4611.

    Article  PubMed  CAS  Google Scholar 

  40. Fernandez, M. L., Estrin, D. A., and Bari, S. E. (2008) J. Inorg. Biochem., 102, 1523–1530.

    Article  PubMed  CAS  Google Scholar 

  41. Kostera, J., Youngblut, M. D., Slosarczyk, J. M., and Pacheco, A. A. (2008) J. Biol. Inorg. Chem., 13, 1073–1083.

    Article  PubMed  CAS  Google Scholar 

  42. Kostera, J., McGarry, J., and Pacheco, A. A. (2010) Biochemistry, 49, 8546–8553.

    Article  PubMed  CAS  Google Scholar 

  43. Trofimov, A. A., Polyakov, K. M., Boyko, K. M., Tikhonova, T. V., Safonova, T. N., Tikhonov, A. V., Popov, A. N., and Popov, V. O. (2010) Acta Crystallogr. D Biol. Crystallogr., 66, 1043–1047.

    Article  PubMed  Google Scholar 

  44. Tikhonova, T. V., Slutskaya, E. S., Filimonenkov, A. A., Boyko, K. M., Kleimenov, S. Y., Konarev, P. V., Polyakov, K. M., Svergun, D. I., Trofimov, A. A., Khomenkov, V. G., Zvyagilskaya, R. A., and Popov, V. O. (2008) Biochemistry (Moscow), 73, 164–170.

    Article  CAS  Google Scholar 

  45. Trofimov, A. A., Polyakov, K. M., Tikhonova, T. V., Tikhonov, A. V., Safonova, T. N., Boyko, K. M., Dorovatovsky, P. V., and Popov, V. O. (2012) Acta Crystallogr. D Biol. Crystallogr., 68, 144–153.

    Article  PubMed  Google Scholar 

  46. Clarke, T. A., Kemp, G. L., van Wonderen, J. H., Doyle, R. M., Cole, J. A., Tovell, N., Cheesman, M. R., Butt, J. N., Richardson, D. J., and Hemmings, A. M. (2008) Biochemistry, 47, 3789–3799.

    Article  PubMed  CAS  Google Scholar 

  47. Trofimov, A. A., Polyakov, K. M., Boyko, K. M., Filimonenkov, A. A., Dorovatovskii, P. V., Tikhonova, T. V., Popov, V. O., and Kovalchuk, M. V. (2010) Crystallogr. Rep., 55, 58–64.

    Article  CAS  Google Scholar 

  48. Sorokin, D. Y., Antipov, A. N., and Kuenen, J. G. (2003) Arch. Microbiol., 180, 127–133.

    Article  PubMed  CAS  Google Scholar 

  49. Clarke, T. A., Cole, J. A., Richardson, D. J., and Hemmings, A. M. (2007) Biochem. J., 406, 19–30.

    Article  PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Bach Institute of Biochemistry, Russian Academy of Sciences, Leninsky pr. 33, 119071, Moscow, Russia

    T. V. Tikhonova, A. A. Trofimov & V. O. Popov

  2. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, ul. Vavilova 32, 119991, Moscow, Russia

    A. A. Trofimov

  3. Russian National Research Center “Kurchatov Institute”, pl. Kurchatova 1, 123182, Moscow, Russia

    V. O. Popov

Authors
  1. T. V. Tikhonova
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  2. A. A. Trofimov
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  3. V. O. Popov
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Corresponding authors

Correspondence to T. V. Tikhonova or V. O. Popov.

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Original Russian Text © T. V. Tikhonova, A. A. Trofimov, V. O. Popov, 2012, published in Biokhimiya, 2012, Vol. 77, No. 10, pp. 1362–1373.

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Tikhonova, T.V., Trofimov, A.A. & Popov, V.O. Octaheme nitrite reductases: Structure and properties. Biochemistry Moscow 77, 1129–1138 (2012). https://doi.org/10.1134/S0006297912100057

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