Related Experiment Video
Updated: Jan 6, 2026

08:20
Optical Control of a Neuronal Protein Using a Genetically Encoded Unnatural Amino Acid in Neurons
Published on: March 28, 2016
8.3K
A Novel Optical Method To Reversibly Control Enzymatic Activity Based On Photoacids
Heike Kagel1, Frank F Bier2, Marcus Frohme3
1Technical University of Applied Sciences, Department of Molecular Biology and Functional Genomics, Hochschulring 1, Wildau, 15745, Germany.
Scientific Reports
|October 9, 2019
Summary
Researchers developed a novel optical method to control biochemical reactions using light. This approach reversibly alters pH with a photoacid, enabling precise control of enzymatic activity via simple light switching.
Area of Science:
- Biochemistry
- Photochemistry
- Enzymology
Background:
- Biochemical reactions are highly pH-dependent, with many favoring acidic conditions.
- Precise, non-invasive pH control for regulating these reactions has been a significant challenge.
- Existing methods often lack reversibility or require invasive manipulation.
Purpose of the Study:
- To introduce a novel optical method for reversible pH control in biochemical reactions.
- To demonstrate the feasibility of using a photoacid for light-induced pH modulation.
- To enable precise temporal control over enzymatic activity using non-invasive optical triggers.
Main Methods:
- Utilized a reversible photoacid (G-acid) as a proton donor.
- Employed high-power UV LEDs to initiate rapid and reversible pH changes.
- Used acid phosphatase as a model enzyme to demonstrate reaction control.
Main Results:
- Successfully demonstrated reversible pH control through light on/off switching.
- Showcased precise regulation of the model acid phosphatase enzymatic reaction.
- Validated the optical approach for non-invasive control of pH-dependent processes.
Conclusions:
- The developed optical method offers a powerful tool for controlling pH-sensitive biochemical reactions.
- This technique enables precise, reversible, and non-invasive regulation of enzymatic activity.
- The approach holds potential for miniaturization and parallelization in various biochemical applications.
Related Concept Videos
Enzyme Inhibition
91.0K
Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.
91.0K
Photochemical Electrocyclic Reactions: Stereochemistry
2.2K
The absorption of UV–visible light by conjugated systems causes the promotion of an electron from the ground state to the excited state. Consequently, photochemical electrocyclic reactions proceed via the excited-state HOMO rather than the ground-state HOMO. Since the ground- and excited-state HOMOs have different symmetries, the stereochemical outcome of electrocyclic reactions depends on the mode of activation; i.e., thermal or photochemical.
Selection Rules: Photochemical Activation
Selection Rules: Photochemical Activation
2.2K

