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Publication Detail
Activated barrier crossing dynamics in the non-radiative decay of NADH and NADPH
  • Publication Type:
    Journal article
  • Publication Sub Type:
  • Authors:
    Bain AJ
  • Publisher:
  • Journal:
    Chemical Physics
  • Keywords:
    NADH, NADPH, NAD(P)H, Fluorescence lifetime, Fluorescence anisotropy, Rotational dynamics, Non-radiative decay, Activated barrier crossing, Kramers equation, Kramers–Hubbard equation, Conformational relaxation
  • Notes:
    Article is in press, has been published on the web on Feb 28th 2013 http://www.sciencedirect.com/science/article/pii/S030101041300116X
In live tissue, alterations in metabolism induce changes in the fluorescence decay of the biological coenzyme NAD(P)H, the mechanism of which is not well understood. In this work, the fluorescence and anisotropy decay dynamics of NADH and NADPH were investigated as a function of viscosity in a range of water–glycerol solutions. The viscosity dependence of the non-radiative decay is well described by Kramers and Kramers–Hubbard models of activated barrier crossing over a wide viscosity range. Our combined lifetime and anisotropy analysis indicates common mechanisms of non-radiative relaxation in the two emitting states (conformations) of both molecules. The low frequencies associated with barrier crossing suggest that non-radiative decay is mediated by small scale motion (e.g. puckering) of the nicotinamide ring. Variations in the fluorescence lifetimes of NADH and NADPH when bound to different enzymes may therefore be attributed to differing levels of conformational restriction upon binding.
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