The hyperthermophilic nature of the metallo-oxidase from Aquifex aeolicus.

摘要: Abstract The stability of the Aquifex aeolicus multicopper oxidase (McoA) was studied by spectroscopy, calorimetry and chromatography to understand its thermophilic nature. enzyme is hyperthermostable as deconvolution differential scanning trace shows that thermal unfolding characterized temperature values at mid-point 105, 110 114 °C. Chemical denaturation revealed however a very low room (2.8 kcal/mol) because copper bleaching/depletion occur before tertiary structure McoA highly prone aggregate. Indeed, kinetics measured with stopped-flow technique quantified stabilizing effect on (1.5 kcal/mol) quite an uncommon observation further confirmed light scattering gel filtration chromatography: aggregates in presence guanidinium hydrochloride, i.e., under conditions. aggregation process results from accumulation quasi-native state binds ANS main determinant curve McoA. Kinetic partitioning between leads heat capacity change determines flat dependence temperature.