Initial Photophysical Characterization of the Proteorhodopsin Optical Proton Sensor (PROPS)

Fluorescence is not frequently used as a tool for investigating the photocycles of rhodopsins, largely because of the low quantum yield of the retinal chromophore. However, a new class of genetically encoded voltage sensors is based upon rhodopsins and their fluorescence. The first such sensor repor...

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Main Author: Jay eNadeau
Format: Article
Language:English
Published: Frontiers Media S.A. 2015-09-01
Series:Frontiers in Neuroscience
Subjects:
Online Access:http://journal.frontiersin.org/Journal/10.3389/fnins.2015.00315/full
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author Jay eNadeau
author_facet Jay eNadeau
author_sort Jay eNadeau
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description Fluorescence is not frequently used as a tool for investigating the photocycles of rhodopsins, largely because of the low quantum yield of the retinal chromophore. However, a new class of genetically encoded voltage sensors is based upon rhodopsins and their fluorescence. The first such sensor reported in the literature was the proteorhodopsin optical proton sensor (PROPS), which is capable of indicating membrane voltage changes in bacteria by means of changes in fluorescence. However, the properties of this fluorescence, such as its lifetime decay components and its origin in the protein photocycle, remain unknown. This paper reports steady-state and nanoscale time-resolved emission of this protein expressed in two strains of Escherichia coli, before and after membrane depolarization. The voltage-dependence of a particularly long lifetime component is established. Additional work to improve quantum yields and improve the general utility of PROPS is suggested.
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spelling doaj.art-cb0504534827409a9bb5395ab738009b2022-12-21T22:46:34ZengFrontiers Media S.A.Frontiers in Neuroscience1662-453X2015-09-01910.3389/fnins.2015.00315158355Initial Photophysical Characterization of the Proteorhodopsin Optical Proton Sensor (PROPS)Jay eNadeau0California Institute of TechnologyFluorescence is not frequently used as a tool for investigating the photocycles of rhodopsins, largely because of the low quantum yield of the retinal chromophore. However, a new class of genetically encoded voltage sensors is based upon rhodopsins and their fluorescence. The first such sensor reported in the literature was the proteorhodopsin optical proton sensor (PROPS), which is capable of indicating membrane voltage changes in bacteria by means of changes in fluorescence. However, the properties of this fluorescence, such as its lifetime decay components and its origin in the protein photocycle, remain unknown. This paper reports steady-state and nanoscale time-resolved emission of this protein expressed in two strains of Escherichia coli, before and after membrane depolarization. The voltage-dependence of a particularly long lifetime component is established. Additional work to improve quantum yields and improve the general utility of PROPS is suggested.http://journal.frontiersin.org/Journal/10.3389/fnins.2015.00315/fullElectrophysiologyoptical recordingGenetically-encoded voltage sensorstime-resolved fluorescenceproteorhodopin
spellingShingle Jay eNadeau
Initial Photophysical Characterization of the Proteorhodopsin Optical Proton Sensor (PROPS)
Frontiers in Neuroscience
Electrophysiology
optical recording
Genetically-encoded voltage sensors
time-resolved fluorescence
proteorhodopin
title Initial Photophysical Characterization of the Proteorhodopsin Optical Proton Sensor (PROPS)
title_full Initial Photophysical Characterization of the Proteorhodopsin Optical Proton Sensor (PROPS)
title_fullStr Initial Photophysical Characterization of the Proteorhodopsin Optical Proton Sensor (PROPS)
title_full_unstemmed Initial Photophysical Characterization of the Proteorhodopsin Optical Proton Sensor (PROPS)
title_short Initial Photophysical Characterization of the Proteorhodopsin Optical Proton Sensor (PROPS)
title_sort initial photophysical characterization of the proteorhodopsin optical proton sensor props
topic Electrophysiology
optical recording
Genetically-encoded voltage sensors
time-resolved fluorescence
proteorhodopin
url http://journal.frontiersin.org/Journal/10.3389/fnins.2015.00315/full
work_keys_str_mv AT jayenadeau initialphotophysicalcharacterizationoftheproteorhodopsinopticalprotonsensorprops