Enhanced photocurrent in engineered bacteriorhodopsin monolayer.

The integration of the transmembrane protein bacteriorhodopsin (BR) with man-made electrode surfaces has attracted a great deal of interest for some two decades or more and holds significant promise from the perspective of derived photoresponse or energy capture interfaces. Here we demonstrate that...

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Autores principales: Patil, A, Premaruban, T, Berthoumieu, O, Watts, A, Davis, J
Formato: Journal article
Lenguaje:English
Publicado: 2012
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author Patil, A
Premaruban, T
Berthoumieu, O
Watts, A
Davis, J
author_facet Patil, A
Premaruban, T
Berthoumieu, O
Watts, A
Davis, J
author_sort Patil, A
collection OXFORD
description The integration of the transmembrane protein bacteriorhodopsin (BR) with man-made electrode surfaces has attracted a great deal of interest for some two decades or more and holds significant promise from the perspective of derived photoresponse or energy capture interfaces. Here we demonstrate that a novel and strategically engineered cysteine site (M163C) can be used to intimately and effectively couple delipidated BR to supporting metallic electrode surfaces. By virtue of the combined effects of the greater surface molecular density afforded by delipidation, and the vicinity of the electrostatic changes associated with proton pumping to the transducing metallic continuum, the resulting films generate a considerably greater photocurrent density on wavelength-selective illumination than previously achievable with monolayers of BR. Given the uniquely photoresponsive, wavelength-selective, and photostable characteristics of this protein, the work has implications for utilization in solar energy capture and photodetector devices.
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spelling oxford-uuid:f2e7b66c-d639-47f3-b6ee-c04058ebe04d2022-03-27T12:07:46ZEnhanced photocurrent in engineered bacteriorhodopsin monolayer.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f2e7b66c-d639-47f3-b6ee-c04058ebe04dEnglishSymplectic Elements at Oxford2012Patil, APremaruban, TBerthoumieu, OWatts, ADavis, JThe integration of the transmembrane protein bacteriorhodopsin (BR) with man-made electrode surfaces has attracted a great deal of interest for some two decades or more and holds significant promise from the perspective of derived photoresponse or energy capture interfaces. Here we demonstrate that a novel and strategically engineered cysteine site (M163C) can be used to intimately and effectively couple delipidated BR to supporting metallic electrode surfaces. By virtue of the combined effects of the greater surface molecular density afforded by delipidation, and the vicinity of the electrostatic changes associated with proton pumping to the transducing metallic continuum, the resulting films generate a considerably greater photocurrent density on wavelength-selective illumination than previously achievable with monolayers of BR. Given the uniquely photoresponsive, wavelength-selective, and photostable characteristics of this protein, the work has implications for utilization in solar energy capture and photodetector devices.
spellingShingle Patil, A
Premaruban, T
Berthoumieu, O
Watts, A
Davis, J
Enhanced photocurrent in engineered bacteriorhodopsin monolayer.
title Enhanced photocurrent in engineered bacteriorhodopsin monolayer.
title_full Enhanced photocurrent in engineered bacteriorhodopsin monolayer.
title_fullStr Enhanced photocurrent in engineered bacteriorhodopsin monolayer.
title_full_unstemmed Enhanced photocurrent in engineered bacteriorhodopsin monolayer.
title_short Enhanced photocurrent in engineered bacteriorhodopsin monolayer.
title_sort enhanced photocurrent in engineered bacteriorhodopsin monolayer
work_keys_str_mv AT patila enhancedphotocurrentinengineeredbacteriorhodopsinmonolayer
AT premarubant enhancedphotocurrentinengineeredbacteriorhodopsinmonolayer
AT berthoumieuo enhancedphotocurrentinengineeredbacteriorhodopsinmonolayer
AT wattsa enhancedphotocurrentinengineeredbacteriorhodopsinmonolayer
AT davisj enhancedphotocurrentinengineeredbacteriorhodopsinmonolayer