Ethyl p-(dimethylamino)cinnamate (EDAC) has been used as a fluorescence probe for monitoring the interaction between a model water-soluble protein, bovine serum albumin (BSA), and an anionic surfactant, sodium dodecyl sulfate (SDS). The probe EDAC undergoes intramolecular charge transfer (ICT) in the excited state in water and other polar solvents. The emission from the ICT state becomes more intense and blue-shifted due to reduced polarity in the hydrophobic environments of BSA and SDS micelles relative to that in pure water. The intensity of the ICT emission from EDAC increases with surfactant concentration and reaches a maximum at the critical micelle concentration of SDS, which can be employed as a simple technique for following micellization. Analysis of the fluorescence spectra of the probe provide evidences in favor of surfactant-induced protein uncoiling due to massive binding of the SDS molecules to BSA in the cooperative binding region of the binding curve, describing protein (BSA)−surfactant (SDS) interaction. The polarity of the BSA−SDS aggregate formed is intermediate between that of hydrophobic regions of BSA and SDS micelles as sensed by the intramolecular charge-transfer (ICT) probe, EDAC.

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We report here on the steady-state and time-resolved fluorescence studies on proton-transfer (PT) reaction of 4-methyl 2,6-diformyl phenol (MFOH) in confined nanocavities in three solvents, dimethyl sulfoxide (DMSO), dimethyl formamide (DMF), and water. Though DMSO and DMF individually interact with MFOH in a similar fashion, their modes of interaction get significantly modified in the presence of cyclodextrin (CD) nanocages. In DMSO, in the ground state, the solvated molecular anion of MFOH forms 1:1 inclusion complex with beta- or gamma-CD and attains greater stability compared to the normal form. In DMF, the solvated molecular anion gets converted to the H-bonded complex within the CD cavity resulting in a 50-nm blue shift in the absorption spectra. In the excited state, the anionic species gets more stabilized in DMSO while in DMF it is significantly destabilized in the presence of CDs. However, in case of water, MFOH gets trapped inside the water cages so that the CDs fail to complex with it effectively. There are also no changes in the excited-state lifetimes in water in the presence of CDs, but in case of DMSO and DMF, because of restricted rotation of the formyl group within the CD cavity, the contribution of the shorter lifetime components reduce significantly increasing the larger components. Some theoretical calculations at the AM1 level of approximation have also been carried out to demonstrate how the dipolar nature of the solvent influences excited-state PT in confined media.

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The “push–pull” effects associated with heme enzymes manifest themselves through highly evolved distal amino acid environments and axial ligands to the heme. These conserved residues enhance their reactivities by orders of magnitude relative to small molecules that mimic the primary coordination. An instance of a mononuclear iron porphyrin with covalently attached pendent phenanthroline groups is reported which exhibit reactivity indicating a pH dependent “push” to “pull” transition in the same molecule. The pendant phenanthroline residues provide proton transfer pathways into the iron site, ensuring selective 4e–/4H+ reduction of O2 to water. The protonation of these residues at lower pH mimics the pull effect of peroxidases, and a coordination of an axial hydroxide ligand at high pH emulates the push effect of P450 monooxygenases. Both effects enhance the rate of O2 reduction by orders of magnitude over its value at neutral pH while maintaining exclusive selectivity for 4e–/4H+ oxygen reduction reaction.