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Abstract Long emission wavelengths, high fluorescence quantum yields (FQYs), and large Stokes shifts are highly desirable features for fluorescent probes in biological imaging. However, the current development of many fluorescent probes remains largely trial‐and‐error and lacks efficiency. Moreover, to achieve far‐red/near‐infrared emission, a significant extension in the‐conjugation is usually adopted but accompanied by other drawbacks such as fluorescence loss. In this review, we discuss an effective red‐shifting strategy built upon the green fluorescent protein chromophore, which enables a synergistic tuning of both the electronic ground and excited states. This approach could shorten the path toward redder emission in comparison to the conventional intramolecular charge transfer (ICT) strategy. We envision that this spectroscopy and computation‐aided strategy may advance the noncanonical fluorescent protein design and be generalized to various fluorophore scaffolds for redder emission while preserving other superior properties such as high FQYs. 

Abstract A non‐aqueous proton electrolyte is devised by dissolving H₃PO₄into acetonitrile. The electrolyte exhibits unique vibrational signatures from stimulated Raman spectroscopy. Such an electrolyte exhibits unique characteristics compared to aqueous acidic electrolytes: 1) higher (de)protonation potential for a lower desolvation energy of protons, 2) better cycling stability by dissolution suppression, and 3) higher Coulombic efficiency owing to the lack of oxygen evolution reaction. Two non‐aqueous proton full cells exhibit better cycling stability, higher Coulombic efficiency, and less self‐discharge compared to the aqueous counterpart. 

The structure–function relationships of biomolecules have captured the interest and imagination of the scientific community and general public since the field of structural biology emerged to enable the molecular understanding of life processes. Proteins that play numerous functional roles in cellular processes have remained in the forefront of research, inspiring new characterization techniques. In this review, we present key theoretical concepts and recent experimental strategies using femtosecond stimulated Raman spectroscopy (FSRS) to map the structural dynamics of proteins, highlighting the flexible chromophores on ultrafast timescales. In particular, wavelength-tunable FSRS exploits dynamic resonance conditions to track transient-species-dependent vibrational motions, enabling rational design to alter functions. Various ways of capturing excited-state chromophore structural snapshots in the time and/or frequency domains are discussed. Continuous development of experimental methodologies, synergistic correlation with theoretical modeling, and the expansion to other nonequilibrium, photoswitchable, and controllable protein systems will greatly advance the chemical, physical, and biological sciences. 

Methylation occurs in a myriad of systems with protective and regulatory functions. 8-methoxypyrene-1,3,6-trisulfonate (MPTS), a methoxy derivative of a photoacid, serves as a model system to study effects of methylation on the excited state potential energy landscape. A suite of spectroscopic techniques including transient absorption, wavelength-tunable femtosecond stimulated Raman spectroscopy (FSRS), and fluorescence quantum yield measurements via steady-state electronic spectroscopy reveal the energy dissipation pathways of MPTS following photoexcitation. Various solvents enable a systematic characterization of the H-bonding interaction, viscosity, and dynamic solvation that influence the ensuing relaxation pathways. The formation of a charge-transfer state out of the Franck–Condon region occurs on the femtosecond-to-picosecond solvation timescale before encountering a rotational barrier. The rotational relaxation correlates with the H-bond donating strength of solvent, while the rotational time constant lengthens as solvent viscosity increases. Time-resolved excited-state FSRS, aided by quantum calculations, provides crucial structural dynamics knowledge and reveals the sulfonate groups playing a dominant role during solvation. Several prominent vibrational motions of the pyrene ring backbone help maneuver the population toward the more fluorescent state. These ultrafast correlated electronic and nuclear motions ultimately govern the fate of the photoexcited chromophore in solution. Overall, MPTS in water displays the highest probability to fluoresce, while the aprotic and more viscous dimethyl sulfoxide enhances the nonradiative pathways. These mechanistic insights may apply robustly to other photoexcited chromophores that do not undergo excited-state proton transfer or remain trapped in a broad electronic state and also provide design principles to control molecular optical responses with site-specific atomic substitution.