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...
Autores principales: | , , |
---|---|
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 |