ArticleNature2009
Mapping GFP structure evolution during proton transfer with femtosecond Raman spectroscopy.
Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed, 454 citations in OpenAlex.
- Ultrafast Charge Transfer Dynamics of Thioflavin T Probed by Time-Resolved Raman Spectroscopy.ACS physical chemistry Au · 2026Article
- Tracking coherent vibronic and vibrational motions in ultrafast proton transfer.Nature communications · 2026Article
- Vibrational snapshots of ultrafast C-H bond photoactivation inside a water-soluble nanocage.Chemical science · 2026Article
- Physical Mechanisms of an Unconventional Green Fluorescent Protein Indicator for Chloride.The journal of physical chemistry. B · 2026Article
- Ultrafast spectroscopic signatures forChemical science · 2026Article
- Electronic and Steric Tuning of Molecular Acidity toward Unified Models for Excited State Proton Transfer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Shell-isolated nanoparticle-enhanced femtosecond stimulated Raman spectroscopy reveals ultrafast molecular dynamics of surface reactions.Nature communications · 2025Article
- Acid-Base Chemistry of Short Hydrogen Bonds: A Tale of Schrödinger's Cat in Glutamine-Derived Crystals.The journal of physical chemistry letters · 2025Article
- A twisted chromophore powers a turn-on fluorescent protein chloride sensor.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Photon-counting Raman spectroscopy at a MHz spectral rate for biochemical imaging of an entire organism.Nature communications · 2025Article
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
- Engineering the ChlorON Series: Turn-On Fluorescent Protein Sensors for Imaging Labile Chloride in Living Cells.ACS central science · 2024Article
- Mastering Femtosecond Stimulated Raman Spectroscopy: A Practical Guide.ACS physical chemistry Au · 2024Review
- Editorial: Hot topic: excited state processes in biomolecules.Frontiers in chemistry · 2024Article
- Optical control of ultrafast structural dynamics in a fluorescent protein.Nature chemistry · 2023Article
- Structural Characterization of Fluorescent Proteins Using Tunable Femtosecond Stimulated Raman Spectroscopy.International journal of molecular sciences · 2023Article
- Structural origin and rational development of bright red noncanonical variants of green fluorescent protein.Physical chemistry chemical physics : PCCP · 2023Article
- Investigation of Excited-State Intramolecular Proton Transfer and Structural Dynamics in Bis-Benzimidazole Derivative (BBM).International journal of molecular sciences · 2023Article
- Ultrafast Dynamics Revealed with Time-Resolved Scanning Tunneling Microscopy: A Review.ACS applied optical materials · 2023Review
- The Role of H-Bonds in the Excited-State Properties of Multichromophoric Systems: Static and Dynamic Aspects.Molecules (Basel, Switzerland) · 2023Review
31 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tracing the transient atomic motions that lie at the heart of chemical reactions requires high-resolution multidimensional structural information on the timescale of molecular vibrations, which commonly range from 10 fs to 1 ps. For simple chemical systems, it has been possible to map out in considerable detail the reactive potential-energy surfaces describing atomic motions and resultant reaction dynamics, but such studies remain challenging for complex chemical and biological transformations. A case in point is the green fluorescent protein (GFP) from the jellyfish Aequorea victoria, which is a widely used gene expression marker owing to its efficient bioluminescence. This feature is known to arise from excited-state proton transfer (ESPT), yet the atomistic details of the process are still not fully understood. Here we show that femtosecond stimulated Raman spectroscopy provides sufficiently detailed and time-resolved vibrational spectra of the electronically excited chromophore of GFP to reveal skeletal motions involved in the proton transfer that produces the fluorescent form of the protein. In particular, we observe that the frequencies and intensities of two marker bands, the C-O and C = N stretching modes at opposite ends of the conjugated chromophore, oscillate out of phase with a period of 280 fs; we attribute these oscillations to impulsively excited low-frequency phenoxyl-ring motions, which optimize the geometry of the chromophore for ESPT. Our findings illustrate that femtosecond simulated Raman spectroscopy is a powerful approach to revealing the real-time nuclear dynamics that make up a multidimensional polyatomic reaction coordinate.
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