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The models are described for complex ∞uorescence decay of tyrosine in proteins involving continuous distribution of ∞uorescence lifetimes and electron transfer processes. We introduce the analytical decay function with a power-like term, which provides good flts to highly complex ∞uorescence decays. Moreover, the power-like term in the proposed decay functions is a manifestation of so-called Tsallis nonextensive statistics and is suitable for description of the systems with long-range interactions, memory efiect, as well as with ∞uctuations of the characteristic lifetime of ∞uorescence. The proposed decay functions were applied to analysis of ∞uorescence decays of tyrosine in a protein, i.e. the enzyme purine nucleoside phosphorylase from E. coli, free in aqueous solution and in the complex with formycin A (an inhibitor) and orthophosphate (a co-substrate), and demonstrated that both models re∞ect the enzymeiligand interactions. Direct measure of heterogeneity of the enzyme systems is provided by a variance of ∞uorescence lifetime distribution. The possible number of deactivation channels and excited state mean lifetime can be easily derived without a priori knowledge of the complexity of studied system.

Fluorescence Decay Heterogeneity Model Based on Electron Transfer Processes in an Enzyme-Ligand Complex