title: Effect of solvent phase transitions on enzymatic activity and structure of laccase from Coriolus hirsutus.
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 degrees C was shown. Spontaneous oxidation of T1 copper center in the temperature range 12-20 degrees 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.
authors.affiliation: Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, 119071, Russia.
authors.forename: E V
authors.initials: EV
authors.lastname: Stepanova
authors.forename: T V
authors.initials: TV
authors.lastname: Fedorova
authors.forename: O N
authors.initials: ON
authors.lastname: Sorokina
authors.forename: V V
authors.initials: VV
authors.lastname: Volkov
authors.forename: O V
authors.initials: OV
authors.lastname: Koroleva
authors.forename: A T
authors.initials: AT
authors.lastname: Dembo
mesh_terms: D005656:Fungal Proteins / Q000737:chemistry* / Q000378:metabolism*; D042845:Laccase / Q000737:chemistry* / Q000378:metabolism*; D044367:Phase Transition; D012997:Solvents / Q000737:chemistry*; D055454:Trametes / Q000737:chemistry / Q000201:enzymology*
chemical_list: D005656:Fungal Proteins; D012997:Solvents; D042845:Laccase