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

• Authors: J. Wlodarczyk , B. Kierdaszuk
• Languages of publication: EN

Abstracts

EN

The models are described for complex fluorescence decay of tyrosine in proteins involving continuous distribution of fluorescence lifetimes and electron transfer processes. We introduce the analytical decay function with a power-like term, which provides good fits to highly complex fluorescence 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 effect, as well as with fluctuations of the characteristic lifetime of fluorescence. The proposed decay functions were applied to analysis of fluorescence 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 reflect the enzyme-ligand interactions. Direct measure of heterogeneity of the enzyme systems is provided by a variance of fluorescence 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.

Keywords

EN

33.50.-j

Discipline

• 33.50.-j: Fluorescence and phosphorescence; radiationless transitions, quenching (intersystem crossing, internal conversion)(for energy transfer, see also section 34; for biophysical applications, see 87.64.kv)

• Publisher: Institute of Physics, Polish Academy of Sciences
• Journal: Acta Physica Polonica A
• Year: 2005
• Volume: 107
• Issue: 6
• Pages: 883-894

Dates

published

2005-06

received

2004-12-28

(unknown)

2005-02-07

Contributors

author

J. Wlodarczyk

• University of Warsaw, Institute of Experimental Physics, Department of Biophysics, Żwirki i Wigury 93, 02-089 Warsaw, Poland

author

B. Kierdaszuk

• University of Warsaw, Institute of Experimental Physics, Department of Biophysics, Żwirki i Wigury 93, 02-089 Warsaw, Poland

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Identifiers

DOI

10.12693/APhysPolA.107.883