Steady-state and time-resolved fluorescence quenching with transition metal ions as short-distance probes for protein conformation

A series of model dye-labeled histidine-containing peptides was used to investigate the nature of the quenching mechanism with Cu 2+ and Ni 2+. The strong reduction in steady-state fluorescence was found to be unaccompanied by any noticeable changes in lifetime kinetics. This static nature of quench...

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Bibliographic Details
Published in:Analytical biochemistry 2010-12, Vol.407 (2), p.284-286
Main Authors: Posokhov, Yevgen O., Kyrychenko, Alexander, Ladokhin, Alexey S.
Format: Article
Language:English
Subjects:
Fluorescence Resonance Energy Transfer
Fluorescent Dyes - chemistry
Histidine - chemistry
Peptides - chemistry
Protein Structure, Tertiary
Spectrometry, Fluorescence
Transition Elements - chemistry
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Summary:A series of model dye-labeled histidine-containing peptides was used to investigate the nature of the quenching mechanism with Cu 2+ and Ni 2+. The strong reduction in steady-state fluorescence was found to be unaccompanied by any noticeable changes in lifetime kinetics. This static nature of quenching is not consistent with the dynamic Förster resonance energy transfer (FRET) phenomenon, which was assumed to dominate the quenching mechanism, and is likely caused by shorter range orbital coupling. Our results indicate that the FRET-like sixth power of distance dependence of quenching cannot be automatically assumed for transition metal ions and that time-resolved measurements should be used to distinguish various quenching mechanisms.
ISSN:0003-2697
1096-0309
DOI:10.1016/j.ab.2010.07.035