Thermodynamic behavior and conformational changes of alcohol oxidase from yeast Hansenula polymorpha |
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| Authors: | Yu. A. Kim V. A. Rykov V. V. Ashin N. V. Molochkov Yu. Yu. Skarga |
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| Affiliation: | 1.Institute of Cell Biophysics,Russian Academy of Sciences,Pushchino, Moscow Region,Russia;2.National Center of Biotechnology of Republic of Kazakhstan,Astana,Kazakhstan;3.Skryabin Institute of Biochemistry and Physiology of Microorganisms,Russian Academy of Sciences,Pushchino, Moscow Region,Russia;4.Institute of Theoretical and Experimental Biophysics,Russian Academy of Sciences,Pushchino, Moscow Region,Russia |
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| Abstract: | We studied the influence of heating, ethanol, and sodium azide on the structural and conformational changes in the alcohol oxidase from yeast Hansenula polymorpha. An increase in fluorescence of the alcohol oxidase cofactor, flavine adenine dinucleotide, was revealed upon heating to 60°C while the enzymatic activity of alcohol oxidase was preserved. Differential scanning microcalorimetry revealed that ethanol stabilized the protein structure and increased the melting temperature. Based on the data of circular dichroism, we concluded that the percentage of helicity in the secondary structure of alcohol oxidase was not influenced by ethanol or sodium azide, but ethanol significantly modified the circular dichroism spectrum associated with the tertiary structure of alcohol oxidase. |
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