Paper
17 August 1994 Time-resolved fluorescence study of electron transfer in a model peptide system
Fiona Donald, Graham Hungerford, Barry D. Moore, David J. S. Birch
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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.
© (1994) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Fiona Donald, Graham Hungerford, Barry D. Moore, and David J. S. Birch "Time-resolved fluorescence study of electron transfer in a model peptide system", Proc. SPIE 2137, Time-Resolved Laser Spectroscopy in Biochemistry IV, (17 August 1994); https://doi.org/10.1117/12.182751
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KEYWORDS
Luminescence

Systems modeling

Proteins

Time resolved spectroscopy

Absorption

Data modeling

Dielectrics

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