2007 Volume 80 Issue 6 Pages 1033-1043
Ultrafast chemical dynamics in a nano-confined system is very different from that in a bulk liquid. In this account, we give an overview on recent femtosecond study on dynamics of ultrafast chemical processes in the nanocavity of a biological system. Dynamics in a biological system crucially depends on the location of the fluorescent probe. We show that one can study solvation dynamics in different regions (i.e. spatially resolve) by variation of the excitation wavelength. We discuss two interesting cases of how structure affects dynamics. First, solvation dynamics of two protein folding intermediates of cytochrome c is found to be differ significantly in the ultrafast initial part (< 20 ps). Second, methyl substitution of the OH group in a cyclodextrin is shown to slow down the initial part of solvation dynamics quite dramatically. The most interesting observation is the discovery of the ultraslow component of solvation dynamics which is 100–1000 times slower compared to bulk water. The electron- and proton-transfer processes in a nano-confined system are found to be markedly retarded because of slow solvation and structural constraints. Close proximity of the reactants in a confined system is expected to accelerate dynamics of bi-molecular processes. This is illustrated by ultrafast fluorescence resonance energy transfer (FRET) in ≈1 ps time scale between a donor and an acceptor in a micelle. Finally, it is demonstrated that the decay of fluorescence anisotropy provides structural information (e.g. size of a cyclodextrin inclusion complex) and may be used to detect formation of a nano-aggregate.
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