Abstract
Steady-state and time-resolved fluorescences were studied in alcohol oxidase from methylotropic yeast in the presence of substrate (ethanol). The fluorescence decay was found to be non-exponential and to reflect the heterogeneity of the microenvironment of the emitting tryptophanyls. The fluorescence decay of FAD located in the active centre can be described by the sum of two exponential components. The reason for this is suggested to be the presence of two different coenzyme conformations related to alcohol oxidase. The intensity of FAD fluorescence considerably increased as the protein denaturated and could serve as a criterion of enzyme nativity.
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