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Solvation dynamics in a neat ionic liquid, 1-pentyl-3-methyl-imidazolium tetra-flouroborate ([pmim][BF4]) and its microemulsion in Triton X-100 (TX-100)/benzene is studied using femtosecond up-conversion. In both the neat ionic liquid and the microemulsion, the solvation dynamics is found to depend on excitation wavelength (lambda(ex)). The lambda(ex) dependence is attributed to structural heterogeneity in neat ionic liquid (IL) and in IL microemulsion. In neat IL, the heterogeneity arises from clustering of the pentyl groups which are surrounded by a network of cation and anions. Such a nanostructural organization is predicted in many recent simulations and observed recently in an X-ray diffraction study. In an IL microemulsion, the surfactant (TX-100) molecules aggregate in form of a nonpolar peripheral shell around the polar pool of IL. The micro-environment in such an assembly varies drastically over a short distance. The dynamic solvent shift (and average solvation time) in neat IL as well as in IL microemulsions decreases markedly as lambda(ex) increases from 375 to 435 nm. In a [pmim][BF4]/water/TX-100/benzene quaternary microemulsion, the solvation dynamics is slower than that in a microemulsion without water. This is ascribed to the smaller size of the water containing microemulsion. The anisotropy decay in an IL microemulsion is found to be faster than that in neat IL.

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Fluorescence anisotropy decay and solvation dynamics of coumarin 153 (C153) are studied in dimethyl beta-cyclodextrin (DIMEB) and trimethyl beta-cyclodextrin (TRIMEB) nanocavity in water. C153 binds to DIMEB and TRIMEB to form both 1:1 and 1:2 (C153:cyclodextrin) complexes. The anisotropy decays of C153 in DIMEB and TRIMEB are found to be biexponential. The fast component of anisotropy decay (approximately 1000 ps) is attributed to the 1:1 complex and the slower one (approximately 2500 ps) to the 1:2 complex. From the components of the anisotropy decay, the length of the 1:1 and 1:2 complexes are estimated. Solvation dynamics of C153 in DIMEB exhibits a very fast (2.4 ps) component (41%) and two slower components of 50 ps (29%) and 1450 ps (30%). Solvation dynamics in TRIMEB is described by three slow components of 10.3 ps (24%), 240 ps (45%), and 2450 ps (31%). Possible origins of the ultraslow components are discussed.

Solvation dynamics at the active site of an enzyme, glutaminyl-tRNA synthetase (GlnRS), was studied using a fluorescence probe, acrylodan, site-specifically attached at cysteine residue C229, near the active site. The picosecond time-dependent fluorescence Stokes shift indicates slow solvation dynamics at the active site of the enzyme, in the absence of any substrate. The solvation dynamics becomes still slower when the substrate (glutamine or tRNA(Gln)) binds to the enzyme. A mutant Y211H-GlnRS was constructed in which the glutamine binding site is disrupted. The mutant Y211H-GlnRS labeled at C229 with acrylodan exhibited significantly different solvent relaxation, thus demonstrating that the slow dynamics is indeed associated with the active site. Implications for catalysis and specificity have been discussed.

Excitation wavelength (lambdaex) dependence of solvation dynamics of coumarin 480 (C480) in the micellar core of a water soluble triblock copolymer, PEO20-PPO70-PEO20 (Pluronic P123), is studied by femtosecond and picosecond time resolved emission spectroscopies. In the P123 micelle, the width of the emission spectrum of C480 is found to be much larger than that in bulk water. This suggests that the P123 micelle is more heterogeneous than bulk water. The steady state emission maximum of C480 in P123 micelle shows a significant red edge excitation shift by 25 nm from 453 nm at lambdaex=345 nm to 478 nm at lambdaex=435 nm. The solvation dynamics in the interior of the triblock copolymer micelle is found to depend strongly on the excitation wavelength. The excitation wavelength dependence is ascribed to a wide distribution of locations of C480 molecules in the P123 micelle with two extreme environments-a bulklike peripheral region with very fast solvent response and a very slow core region. With increase in lambdaex, contribution of the bulklike region having an ultrafast component (< or =2 ps) increases from 7% at lambdaex=375 nm to 78% at lambda(ex)=425 nm while the contribution of the ultraslow component (4500 ps) decreases from 79% to 17%.

Temperature dependence of solvation dynamics and fluorescence anisotropy decay of 8-anilino-1-naphthalenesulfonate (ANS) bound to a protein, bovine serum albumin (BSA), are studied. Solvation dynamics of ANS bound to BSA displays a component (300 ps) which is independent of temperature in the range of 278-318 K and a long component which decreases from 5800 ps at 278 K to 3600 ps at 318 K. The temperature independent part is ascribed to a dynamic exchange of bound to free water with a low barrier. The temperature variation of the long component of solvation dynamics corresponds to an activation energy of 2.1 kcal mol(-1). The activation energy is ascribed to local segmental motion of the protein along with the associated water molecules and polar residues. The time scale of solvation dynamics is found to be very different from the time scale of anisotropy decay. The anisotropy decays are analyzed in terms of the wobbling motion of the probe (ANS) and the overall tumbling of the protein.

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