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Related Experiment Video

Updated: Mar 24, 2026

Separation of Spinach Thylakoid Protein Complexes by Native Green Gel Electrophoresis and Band Characterization using Time-Correlated Single Photon Counting

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Published on: February 14, 2019

pH-Dependent Excited-State Dynamics of a Large Stokes Shift Photobasic Complex.

Jiajia Meng¹, Gaoshang Li¹, Siteng Zhao¹

¹Center for Quantum Technology Research, Key Laboratory of Advanced Optoelectronic Quantum Architecture and Measurements (MOE), School of Physics, Beijing Institute of Technology, Beijing, China.

Chemistry (Weinheim an Der Bergstrasse, Germany)

|March 23, 2026

Summary

Researchers developed a novel large Stokes shift (LSS) fluorescent protein using a photobasic fluorophore. This advancement offers new insights into protein-chromophore interactions and pH-responsive biosensors.

Keywords:

excited‐state photo transfer photobase ultrafast dynamic

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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy

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Published on: June 27, 2014

Area of Science:

Biophysics
Spectroscopy
Protein Engineering

Background:

Large Stokes shift (LSS) fluorescent proteins are crucial for biological imaging due to their large energy gaps between absorption and emission.
Existing LSS systems primarily use photoacidic chromophores, leaving photobasic variants underexplored.

Purpose of the Study:

To construct and characterize a novel LSS complex utilizing a photobasic fluorophore.
To investigate the pH-dependent excited-state proton transfer (ESPT) dynamics within the engineered protein.

Main Methods:

Incorporation of the photobasic fluorophore FR-1V into an engineered rhodopsin mimic (hCRBPII mutant M1).
Ultrafast spectroscopy, including transient absorption spectroscopy (TAS) and time-correlated single-photon counting (TCSPC).
Molecular dynamics (MD) simulations to analyze protein-chromophore interactions and conformational states.

Main Results:

The engineered LSS complex exhibited pH-dependent ESPT dynamics.
At pH 8, ESPT occurred as a single kinetic process (1.8 ps).
At pH 11, ESPT proceeded via two distinct processes (1.0 ps and 13 ps), suggesting pH-induced heterogeneity in hydrogen-bonding networks.

Conclusions:

The study elucidates the mechanism of pH-dependent ESPT in photobasic LSS systems.
Findings support a model of pH-dependent heterogeneity in ground-state Schiff base hydrogen-bonding networks.
This work provides a mechanistic framework for developing advanced pH-responsive biosensors and deepens understanding of protein-chromophore interactions.