Silvio Bianchi, Giacomo Donini, Maria Cristina Cannarsa, Giacomo Frangipane, Roberto Di Leonardo
{"title":"Dynamic velocity response of E. coli powered by proteorhodopsin.","authors":"Silvio Bianchi, Giacomo Donini, Maria Cristina Cannarsa, Giacomo Frangipane, Roberto Di Leonardo","doi":"10.1016/j.bpr.2026.100254","DOIUrl":null,"url":null,"abstract":"<p><p>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.</p>","PeriodicalId":72402,"journal":{"name":"Biophysical reports","volume":" ","pages":"100254"},"PeriodicalIF":2.6000,"publicationDate":"2026-06-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12994061/pdf/","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biophysical reports","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1016/j.bpr.2026.100254","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2026/2/24 0:00:00","PubModel":"Epub","JCR":"Q3","JCRName":"BIOPHYSICS","Score":null,"Total":0}
引用次数: 0
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.