Tuning the photoexcitation response of cyanobacterial Photosystem I via reconstitution into Proteoliposomes

Abstract The role of natural thylakoid membrane housing of Photosystem I (PSI), the transmembrane photosynthetic protein, in its robust photoactivated charge separation with near unity quantum efficiency is not fundamentally understood. To this end, incorporation of suitable protein scaffolds for PS...

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Autores principales:	Hanieh Niroomand, Dibyendu Mukherjee, Bamin Khomami
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/4ae2f916054542a6bef9a143a9708e80
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spelling	oai:doaj.org-article:4ae2f916054542a6bef9a143a9708e802021-12-02T16:06:02ZTuning the photoexcitation response of cyanobacterial Photosystem I via reconstitution into Proteoliposomes10.1038/s41598-017-02746-52045-2322https://doaj.org/article/4ae2f916054542a6bef9a143a9708e802017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-02746-5https://doaj.org/toc/2045-2322Abstract The role of natural thylakoid membrane housing of Photosystem I (PSI), the transmembrane photosynthetic protein, in its robust photoactivated charge separation with near unity quantum efficiency is not fundamentally understood. To this end, incorporation of suitable protein scaffolds for PSI incorporation is of great scientific and device manufacturing interest. Areas of interest include solid state bioelectronics, and photoelectrochemical devices that require bio-abio interfaces that do not compromise the photoactivity and photostability of PSI. Therefore, the surfactant-induced membrane solubilization of a negatively charged phospholipid (DPhPG) with the motivation of creating biomimetic reconstructs of PSI reconstitution in DPhPG liposomes is studied. Specifically, a simple yet elegant method for incorporation of PSI trimeric complexes into DPhPG bilayer membranes that mimic the natural thylakoid membrane housing of PSI is introduced. The efficacy of this method is demonstrated via absorption and fluorescence spectroscopy measurements as well as direct visualization using atomic force microscopy. This study provides direct evidence that PSI confinements in synthetic lipid scaffolds can be used for tuning the photoexcitation characteristics of PSI. Hence, it paves the way for development of fundamental understanding of microenvironment alterations on photochemical response of light activated membrane proteins.Hanieh NiroomandDibyendu MukherjeeBamin KhomamiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hanieh Niroomand Dibyendu Mukherjee Bamin Khomami Tuning the photoexcitation response of cyanobacterial Photosystem I via reconstitution into Proteoliposomes
description	Abstract The role of natural thylakoid membrane housing of Photosystem I (PSI), the transmembrane photosynthetic protein, in its robust photoactivated charge separation with near unity quantum efficiency is not fundamentally understood. To this end, incorporation of suitable protein scaffolds for PSI incorporation is of great scientific and device manufacturing interest. Areas of interest include solid state bioelectronics, and photoelectrochemical devices that require bio-abio interfaces that do not compromise the photoactivity and photostability of PSI. Therefore, the surfactant-induced membrane solubilization of a negatively charged phospholipid (DPhPG) with the motivation of creating biomimetic reconstructs of PSI reconstitution in DPhPG liposomes is studied. Specifically, a simple yet elegant method for incorporation of PSI trimeric complexes into DPhPG bilayer membranes that mimic the natural thylakoid membrane housing of PSI is introduced. The efficacy of this method is demonstrated via absorption and fluorescence spectroscopy measurements as well as direct visualization using atomic force microscopy. This study provides direct evidence that PSI confinements in synthetic lipid scaffolds can be used for tuning the photoexcitation characteristics of PSI. Hence, it paves the way for development of fundamental understanding of microenvironment alterations on photochemical response of light activated membrane proteins.
format	article
author	Hanieh Niroomand Dibyendu Mukherjee Bamin Khomami
author_facet	Hanieh Niroomand Dibyendu Mukherjee Bamin Khomami
author_sort	Hanieh Niroomand
title	Tuning the photoexcitation response of cyanobacterial Photosystem I via reconstitution into Proteoliposomes
title_short	Tuning the photoexcitation response of cyanobacterial Photosystem I via reconstitution into Proteoliposomes
title_full	Tuning the photoexcitation response of cyanobacterial Photosystem I via reconstitution into Proteoliposomes
title_fullStr	Tuning the photoexcitation response of cyanobacterial Photosystem I via reconstitution into Proteoliposomes
title_full_unstemmed	Tuning the photoexcitation response of cyanobacterial Photosystem I via reconstitution into Proteoliposomes
title_sort	tuning the photoexcitation response of cyanobacterial photosystem i via reconstitution into proteoliposomes
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/4ae2f916054542a6bef9a143a9708e80
work_keys_str_mv	AT haniehniroomand tuningthephotoexcitationresponseofcyanobacterialphotosystemiviareconstitutionintoproteoliposomes AT dibyendumukherjee tuningthephotoexcitationresponseofcyanobacterialphotosystemiviareconstitutionintoproteoliposomes AT baminkhomami tuningthephotoexcitationresponseofcyanobacterialphotosystemiviareconstitutionintoproteoliposomes
_version_	1718385144724717568

Tuning the photoexcitation response of cyanobacterial Photosystem I via reconstitution into Proteoliposomes

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