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Related Experiment Video

Updated: May 23, 2026

Electromechanical Assessment of Optogenetically Modulated Cardiomyocyte Activity

Electromechanical Assessment of Optogenetically Modulated Cardiomyocyte Activity

Published on: March 5, 2020

Engineered bacteriorhodopsin: a molecular scale potential switch.

Amol V Patil¹, Thenuhan Premaraban, Olivia Berthoumieu

¹Department of Chemistry, University of Oxford, UK.

Chemistry (Weinheim an Der Bergstrasse, Germany)

|March 29, 2012

Summary

This summary is machine-generated.

This study presents a new method for immobilizing bacteriorhodopsin (BR) on gold surfaces, enabling precise measurements of its light-induced proton pumping activity. This advance facilitates novel applications for this photoresponsive biomolecule in electronics.

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Area of Science:

Biophysics
Materials Science
Biotechnology

Background:

Bacteriorhodopsin (BR) is a photoresponsive biomolecule with potential applications in data storage, imaging, and sensing.
Its membrane-bound nature presents challenges for integration with metallic electronic surfaces.
Uniformly oriented and active BR monolayers are crucial for such applications.

Purpose of the Study:

To develop a facile method for creating uniformly oriented, anchored, and active monolayers of BR on metallic electrodes.
To engineer BR for stable, covalent immobilization on gold surfaces.
To investigate the light-induced proton accumulation and surface potential changes at the molecular scale.

Main Methods:

Engineered cysteine on the cytoplasmic side of BR for covalent immobilization on gold surfaces.
Lipid removal to achieve largely lipid-free, orientation-specific monolayers.
Kelvin probe force microscopy (KPFM) for non-invasive measurement of light-induced proton accumulation.

Main Results:

Successful generation of uniformly oriented, covalently immobilized, and active BR monolayers on gold electrodes.
Detection of light-induced proton accumulation at the extracellular protein surface at molecular scales.
Substantially larger photoinduced surface potential switching ((20.4 ± 7.5) mV) observed with delipidated mutant BR trimers compared to wild-type BR.
Highly unidirectional proton pumping detected with the oriented protein.

Conclusions:

A facile method for orienting and immobilizing bacteriorhodopsin on gold surfaces was established.
Delipidation and covalent immobilization enhance the light-induced proton pumping activity and surface potential switching of BR.
This approach enables precise molecular-scale characterization of BR function, paving the way for advanced biomolecular electronic devices.