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Updated: Jun 28, 2026
05:51
Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
Published on: December 19, 2011
Detecting Vibrational Energy Transfer into an Enzyme Active Site via a Transition State Analog
Jan Gerrit Löffler1, Erhan Deniz1, Yunxia Shen1
1Institute of Biophysics, Johann Wolfgang Goethe-University, Max-von-Laue-Straße 1, 60438 Frankfurt am Main, Germany.
The Journal of Physical Chemistry Letters
|June 26, 2026
Summary
Enzyme active sites can sense vibrational energy using the azide anion as a sensor. This method, using formate dehydrogenase, allows for picosecond-scale studies of vibrational energy transfer in enzymes.
Area of Science:
- Biochemistry
- Chemical Physics
- Enzymology
Background:
- Vibrational energy transfer (VET) is relevant to enzyme catalysis.
- Experimentally probing VET requires non-disruptive sensors within enzyme active sites.
- Native substrates or inhibitors are ideal candidates for vibrational energy sensors.
Purpose of the Study:
- To demonstrate the azide anion as a sensitive vibrational energy sensor in an enzyme active site.
- To investigate the potential of using non-covalently bound ligands for VET studies.
- To establish a method for site-specific energy injection and detection in enzymes.
Main Methods:
- Utilized the azide anion (N3-) as an inhibitor and vibrational energy sensor in the formate dehydrogenase (FDH) active site.
- Introduced an azulenylalanine (AzAla) energy donor via genetic code expansion.
- Site-specifically injected vibrational energy by exciting the AzAla donor at a distance of 19 Å.
Main Results:
- The azide anion, non-covalently bound, effectively detected injected vibrational energy.
- Demonstrated successful site-specific energy transfer and detection within the enzyme.
- Established a proof-of-principle for picosecond-timescale VET investigations.
Conclusions:
- The azide anion is a viable, non-disruptive sensor for VET in enzyme active sites.
- This approach enables the study of VET dynamics on the picosecond timescale.
- The method is applicable to various enzymes utilizing azide or similar ligands.
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