Cargando…

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

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 incorpo...

Descripción completa

Detalles Bibliográficos
Autores principales: Niroomand, Hanieh, Mukherjee, Dibyendu, Khomami, Bamin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5449388/
https://www.ncbi.nlm.nih.gov/pubmed/28559589
http://dx.doi.org/10.1038/s41598-017-02746-5
_version_ 1783239759748923392
author Niroomand, Hanieh
Mukherjee, Dibyendu
Khomami, Bamin
author_facet Niroomand, Hanieh
Mukherjee, Dibyendu
Khomami, Bamin
author_sort Niroomand, Hanieh
collection PubMed
description 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 Online
Article
Text
id pubmed-5449388
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher Nature Publishing Group UK
record_format MEDLINE/PubMed
spelling pubmed-54493882017-06-01 Tuning the photoexcitation response of cyanobacterial Photosystem I via reconstitution into Proteoliposomes Niroomand, Hanieh Mukherjee, Dibyendu Khomami, Bamin Sci Rep Article 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. Nature Publishing Group UK 2017-05-30 /pmc/articles/PMC5449388/ /pubmed/28559589 http://dx.doi.org/10.1038/s41598-017-02746-5 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Niroomand, Hanieh
Mukherjee, Dibyendu
Khomami, Bamin
Tuning the photoexcitation response of cyanobacterial Photosystem I via reconstitution into Proteoliposomes
title 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_short 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
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5449388/
https://www.ncbi.nlm.nih.gov/pubmed/28559589
http://dx.doi.org/10.1038/s41598-017-02746-5
work_keys_str_mv AT niroomandhanieh tuningthephotoexcitationresponseofcyanobacterialphotosystemiviareconstitutionintoproteoliposomes
AT mukherjeedibyendu tuningthephotoexcitationresponseofcyanobacterialphotosystemiviareconstitutionintoproteoliposomes
AT khomamibamin tuningthephotoexcitationresponseofcyanobacterialphotosystemiviareconstitutionintoproteoliposomes