Dynamic velocity response of E. coli powered by proteorhodopsin

Escherichia coli swimming motility is powered by the flagellar motor, a rotary nanomachine driven by inward proton flux through its torque-generating stators. How these proton currents arise from proton motive force is often described using a simple circuit model, in which the membrane acts as a capacitor discharging through the flagellar motors and other resistive proton channels. By monitoring the swimming activity of E. coli expressing a light-driven outward proton pump, we probe the dynamical response of the system under tunable optical driving and test the limits of simplified circuit-based description. Our results show that the flagellar motors are not the main sink for proton motive force discharge. Instead, other membrane channels carry a larger proton current and exhibit a nonlinear resistive behavior. Using the same experimental approach, we directly quantify proteorhodopsin pumping activity as a function of illumination wavelength and compare it with previously reported absorption spectra.

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Publication Details

Journal
Biophysical Reports
Published
2026-02-24
DOI
https://doi.org/10.1016/j.bpr.2026.100254
Primary Topic
Photoreceptor and optogenetics research
Type
article
Field-Weighted Citation Impact
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article

Dynamic velocity response of E. coli powered by proteorhodopsin

S. Bianchi, Giacomo Donini, Giacomo Frangipane, Maria Cristina Cannarsa et al.
Biophysical Reports
Photoreceptor and optogenetics research
article

Dynamic velocity response of E. coli powered by proteorhodopsin

S. Bianchi, Giacomo Donini, Giacomo Frangipane, Maria Cristina Cannarsa, Roberto Di Leonardo
article en

Abstract

Escherichia coli swimming motility is powered by the flagellar motor, a rotary nanomachine driven by inward proton flux through its torque-generating stators. How these proton currents arise from proton motive force is often described using a simple circuit model, in which the membrane acts as a capacitor discharging through the flagellar motors and other resistive proton channels. By monitoring the swimming activity of E. coli expressing a light-driven outward proton pump, we probe the dynamical response of the system under tunable optical driving and test the limits of simplified circuit-based description. Our results show that the flagellar motors are not the main sink for proton motive force discharge. Instead, other membrane channels carry a larger proton current and exhibit a nonlinear resistive behavior. Using the same experimental approach, we directly quantify proteorhodopsin pumping activity as a function of illumination wavelength and compare it with previously reported absorption spectra.

Biophysical ReportsVol. 6(2)
Istituto di Nanotecnologia (IT), Sapienza University of Rome (IT)
Openalex Percentile: Top 45%
Photoreceptor and optogenetics research
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