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Proceedings Paper

Time-resolved fluorescence study of electron transfer in a model peptide system
Author(s): Fiona Donald; Graham Hungerford; Barry D. Moore; David J. S. Birch
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Paper Abstract

At present there is a great deal of interest in the study of the transference of energy in biological systems. For example, electron transfer is of major importance in many synthetic and biological processes and in nature is mediated by proteins. Information regarding this process is therefore useful in leading to a greater understanding of phenomena such as photosynthesis and respiration. Previous work on protein systems has shown the electron transfer process to be complex to analyze because of the presence of competing pathways. This has led to the use of model systems to simplify the kinetics. We have synthesized novel model systems using peptides containing both a fluorescent methoxy- naphthalene donor and a dicyanoethylene group as a potential electron acceptor and observed fluorescence quenching for both dipeptide and oligopeptide systems. Biexponential fluorescence decay behavior was observed for all donor acceptor systems, with an increase in the amount of the shorter fluorescence decay component on increasing temperature.

Paper Details

Date Published: 17 August 1994
PDF: 10 pages
Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); doi: 10.1117/12.182751
Show Author Affiliations
Fiona Donald, Univ. of Strathclyde (United Kingdom)
Graham Hungerford, Univ. of Strathclyde (United Kingdom)
Barry D. Moore, Univ. of Strathclyde (United Kingdom)
David J. S. Birch, Univ. of Strathclyde (United Kingdom)


Published in SPIE Proceedings Vol. 2137:
Time-Resolved Laser Spectroscopy in Biochemistry IV
Joseph R. Lakowicz, Editor(s)

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