Abstract
The effect of solvent phase transitions on catalytic activity and structure of the active site of laccase produced by the Basidiomycetes Coriolus hirsutus 072 was studied. As shown by small-angle X-ray scattering, laccase exists in solution as a mixture of monomeric and aggregated particles in the percent ratio 85: 15. This ratio did not change on phase transitions. A complex nature of laccase activity dynamics during thawing and further heating to 20°C was shown. Spontaneous oxidation of T1 copper center in the temperature range 12–20°C was not observed. According to spectral data, the structure of laccase active sites including all copper centers of types T1, T2, and T3 changes during the phase transition.
Similar content being viewed by others
References
Solomon, E. I., Sundaram, U. M., and Machonkin, T. E. (1996) Chem. Rev., 96, 2563–2605.
Yaropolov, A. I., Skorobogat’ko, O. V., Vartanov, S. S., and Varfolomeyev, S. D. (1994) Appl. Biochim. Biotech., 49, 257–280.
Xu, F. (1999) in Encyclopedia of Bioprocess Technology: Fermentation, Biocatalysis, Bioseparation (Flickinger, M. C., and Drew, S. W., eds.) John Wiley & Sons Inc., New York, pp. 1545–1554.
Smith, M., and Thurnston, C. F. (1997) in Multi-Copper Oxidases (Messerschmidt, A., ed.) World Scientific, Singapore-New Jersey-London-Hong Kong, pp. 253–259.
Piontek, K., Antorini, M., and Choinowski, T. (2002) J. Biol. Chem., 277, 37663–37669.
Nakamura, K., and Go, N. (2005) Cell. Mol. Life Sci., 62, 2050–2066.
Xu, F., Shin, W., Brown, S. H., Wahleithner, J. A., Sundaram, U. M., and Solomon, E. I. (1996) Biochim. Biophys. Acta, 1292, 303–311.
Eggert, C., LaFayette, P. R., Temp, U., Eriksson, K. E., and Dean, J. F. (1998) Appl. Environ. Microbiol., 64, 1766–1772.
Koroleva (Skorobogat’ko), O., Stepanova, E., Gavrilova, V., Morozova, O., Lubimova, N., Dzchafarova, A., Jaropolov, A., and Makower, A. (1998) J. Biotechnol. Appl. Biochem. (Moscow), 28, 47–54.
Koroleva (Skorobogat’ko), O., Stepanova, E., Gavrilova, V., Biniukov, V., Jaropolov, A., Varfolomeyev, S., Scheller, F., Makower, A., and Otto, A. (1998) Appl. Biochem. Biotechnol., 61, 618–627.
Stepanova, E. V., Gavrilova, V. P., Landesman, E. O., Pegasova, T. V., and Koroleva, O. V. (2003) Prikl. Biokhim. Mikrobiol., 39, 375–381.
Koroleva, O. V., Stepanova, E. V., Binukov, V. I., Timofeev, V. P., and Pfeil, W. (2001) Biochim. Biophys. Acta, 1547, 397–407.
Stepanova, E. V., Koroleva, O. V., Gavrilova, V. P., Landesman, E. O., Makover, A., and Papkovsky, D. B. (2003) Prikl. Biokhim. Mikrobiol., 39, 549–554.
Gibson, T. D., and Woodward, J. R. (1992) in Biosensors and Chemical Sensors (Eldman, P. G., and Wang, J., eds.) ACS Books, pp. 40–55.
Alden, M., and Magnusson, A. (1997) Pharm. Res., 4, 426–430.
Huang, H.-W., Sakurai, T., Monjushiro, H., and Takeda, S. (1998) Biochim. Biophys. Acta, 1384, 160–170.
Huang, H.-W., Sakurai, T., Maritano, S., Marchesini, A., and Suzuki, S. (1999) J. Inorg. Biochem., 75, 19–25.
Sakurai, T., and Takahashi, J. (1995) Biochem. Biophys. Res. Commun., 215, 235–240.
Calabrese, L., Carbonaro, M., and Musci, G. (1988) J. Biol. Chem., 263, 6480–6483.
Shleev, S., Reimann, C. T., Serezhenkov, V., Burbaev, D., Yaropolov, A. I., Gorton, L., and Ruzgas, T. (2006) Biochimie, 88, 1275–1285.
Baldrian, P. (2006) FEMS Microbiol. Rev., 30, 215–242.
Koroleva, O. V., Stepanova, E. V., Gavrilova, V. P., Yakovleva, N. S., Landesman, E. O., Yavmetdinov, I. S., and Yaropolov, A. I. (2002) J. Biosci. Bioeng., 93, 449–455.
Westermeier, R. (1993) Electrophoresis in Practice, VCH Verlags-gesellschaft, Weinheim and VCH Publishers Inc., New York.
Varfolomeev, S. D., Naki, A., and Yaropolov, A. I. (1985) Biokhimiya, 50, 1411–1419.
Gorbatova, O. N., Stepanova, E. V., and Koroleva, O. V. (2000) Prikl. Biokhim. Mikrobiol., 36, 272–277.
Svergun, D. I., and Feigin, L. A. (1987) X-Ray and Neutron Low-Angle Scattering [in Russian], Nauka, Moscow, p. 280.
Svergun, D. I., Semenyuk, A. V., and Feigin, L. A. (1988) Acta Cryst. A., 24, 244–251.
Maritano, S., Carsughi, F., Fontana, M. P., and Marchesini, A. (1996) J. Mol. Struct., 383, 261–265.
Svergun, D. I., Volkov, V. V., Kozin, M. B., Stuhrmann, H. B., Barberato, C., and Koch, M. H. (1997) J. Appl. Cryst., 30, 798–802.
Lee, S. K., George, S. D., Antholine, W. E., Hedman, B., Hodgson, K. O., and Solomon, E. I. (2002) J. Am. Chem. Soc., 124, 6180–6193.
Palmer, A. E., Lee, S. K., and Solomon, E. I. (2001) J. Am. Chem. Soc., 123, 6591–6599.
Yoon, J., Liboiron, B. D., Sarangi, R., Hodgson, K. O., Hedman, B., and Solomon, E. I. (2007) PNAS, 104, 13609–13614.
Cordi, L., Minussi, R. C., Freire, R. S., and Duran, N. (2007) Afr. J. Biotechnol., 6, 1255–1259.
Cole, A. P., Root, D. E., Mukherjee, P., Solomon, E. I., and Stack, T. D. P. (1996) Science, 273, 1848–1850.
Gromov, I., Marchesini, A., Farver, O., Pecht, I., and Goldfard, D. (1999) FEBS Eur. J. Biochem., 266, 820–830.
Author information
Authors and Affiliations
Corresponding author
Additional information
Original Russian Text © E. V. Stepanova, T. V. Fedorova, O. N. Sorokina, V. V. Volkov, O. V. Koroleva, A. T. Dembo, 2009, published in Biokhimiya, 2009, Vol. 74, No. 4, pp. 476–485.
Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM08-245, December 28, 2008.
Rights and permissions
About this article
Cite this article
Stepanova, E.V., Fedorova, T.V., Sorokina, O.N. et al. Effect of solvent phase transitions on enzymatic activity and structure of laccase from Coriolus hirsutus . Biochemistry Moscow 74, 385–392 (2009). https://doi.org/10.1134/S0006297909040051
Received:
Revised:
Published:
Issue Date:
DOI: https://doi.org/10.1134/S0006297909040051