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Impact of the lipid bilayer on energy transfer kinetics in the photosynthetic protein LH2

Photosynthetic purple bacteria convert solar energy to chemical energy with near unity quantum efficiency. The light-harvesting process begins with absorption of solar energy by an antenna protein called Light-Harvesting Complex 2 (LH2). Energy is subsequently transferred within LH2 and then through...

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Autores principales: Ogren, John I., Tong, Ashley L., Gordon, Samuel C., Chenu, Aurélia, Lu, Yue, Blankenship, Robert E., Cao, Jianshu, Schlau-Cohen, Gabriela S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5914429/
https://www.ncbi.nlm.nih.gov/pubmed/29732092
http://dx.doi.org/10.1039/c7sc04814a
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author Ogren, John I.
Tong, Ashley L.
Gordon, Samuel C.
Chenu, Aurélia
Lu, Yue
Blankenship, Robert E.
Cao, Jianshu
Schlau-Cohen, Gabriela S.
author_facet Ogren, John I.
Tong, Ashley L.
Gordon, Samuel C.
Chenu, Aurélia
Lu, Yue
Blankenship, Robert E.
Cao, Jianshu
Schlau-Cohen, Gabriela S.
author_sort Ogren, John I.
collection PubMed
description Photosynthetic purple bacteria convert solar energy to chemical energy with near unity quantum efficiency. The light-harvesting process begins with absorption of solar energy by an antenna protein called Light-Harvesting Complex 2 (LH2). Energy is subsequently transferred within LH2 and then through a network of additional light-harvesting proteins to a central location, termed the reaction center, where charge separation occurs. The energy transfer dynamics of LH2 are highly sensitive to intermolecular distances and relative organizations. As a result, minor structural perturbations can cause significant changes in these dynamics. Previous experiments have primarily been performed in two ways. One uses non-native samples where LH2 is solubilized in detergent, which can alter protein structure. The other uses complex membranes that contain multiple proteins within a large lipid area, which make it difficult to identify and distinguish perturbations caused by protein–protein interactions and lipid–protein interactions. Here, we introduce the use of the biochemical platform of model membrane discs to study the energy transfer dynamics of photosynthetic light-harvesting complexes in a near-native environment. We incorporate a single LH2 from Rhodobacter sphaeroides into membrane discs that provide a spectroscopically amenable sample in an environment more physiological than detergent but less complex than traditional membranes. This provides a simplified system to understand an individual protein and how the lipid–protein interaction affects energy transfer dynamics. We compare the energy transfer rates of detergent-solubilized LH2 with those of LH2 in membrane discs using transient absorption spectroscopy and transient absorption anisotropy. For one key energy transfer step in LH2, we observe a 30% enhancement of the rate for LH2 in membrane discs compared to that in detergent. Based on experimental results and theoretical modeling, we attribute this difference to tilting of the peripheral bacteriochlorophyll in the B800 band. These results highlight the importance of well-defined systems with near-native membrane conditions for physiologically-relevant measurements.
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spelling pubmed-59144292018-05-04 Impact of the lipid bilayer on energy transfer kinetics in the photosynthetic protein LH2 Ogren, John I. Tong, Ashley L. Gordon, Samuel C. Chenu, Aurélia Lu, Yue Blankenship, Robert E. Cao, Jianshu Schlau-Cohen, Gabriela S. Chem Sci Chemistry Photosynthetic purple bacteria convert solar energy to chemical energy with near unity quantum efficiency. The light-harvesting process begins with absorption of solar energy by an antenna protein called Light-Harvesting Complex 2 (LH2). Energy is subsequently transferred within LH2 and then through a network of additional light-harvesting proteins to a central location, termed the reaction center, where charge separation occurs. The energy transfer dynamics of LH2 are highly sensitive to intermolecular distances and relative organizations. As a result, minor structural perturbations can cause significant changes in these dynamics. Previous experiments have primarily been performed in two ways. One uses non-native samples where LH2 is solubilized in detergent, which can alter protein structure. The other uses complex membranes that contain multiple proteins within a large lipid area, which make it difficult to identify and distinguish perturbations caused by protein–protein interactions and lipid–protein interactions. Here, we introduce the use of the biochemical platform of model membrane discs to study the energy transfer dynamics of photosynthetic light-harvesting complexes in a near-native environment. We incorporate a single LH2 from Rhodobacter sphaeroides into membrane discs that provide a spectroscopically amenable sample in an environment more physiological than detergent but less complex than traditional membranes. This provides a simplified system to understand an individual protein and how the lipid–protein interaction affects energy transfer dynamics. We compare the energy transfer rates of detergent-solubilized LH2 with those of LH2 in membrane discs using transient absorption spectroscopy and transient absorption anisotropy. For one key energy transfer step in LH2, we observe a 30% enhancement of the rate for LH2 in membrane discs compared to that in detergent. Based on experimental results and theoretical modeling, we attribute this difference to tilting of the peripheral bacteriochlorophyll in the B800 band. These results highlight the importance of well-defined systems with near-native membrane conditions for physiologically-relevant measurements. Royal Society of Chemistry 2018-02-09 /pmc/articles/PMC5914429/ /pubmed/29732092 http://dx.doi.org/10.1039/c7sc04814a Text en This journal is © The Royal Society of Chemistry 2018 http://creativecommons.org/licenses/by-nc/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution Non Commercial 3.0 Unported Licence (CC BY-NC 3.0)
spellingShingle Chemistry
Ogren, John I.
Tong, Ashley L.
Gordon, Samuel C.
Chenu, Aurélia
Lu, Yue
Blankenship, Robert E.
Cao, Jianshu
Schlau-Cohen, Gabriela S.
Impact of the lipid bilayer on energy transfer kinetics in the photosynthetic protein LH2
title Impact of the lipid bilayer on energy transfer kinetics in the photosynthetic protein LH2
title_full Impact of the lipid bilayer on energy transfer kinetics in the photosynthetic protein LH2
title_fullStr Impact of the lipid bilayer on energy transfer kinetics in the photosynthetic protein LH2
title_full_unstemmed Impact of the lipid bilayer on energy transfer kinetics in the photosynthetic protein LH2
title_short Impact of the lipid bilayer on energy transfer kinetics in the photosynthetic protein LH2
title_sort impact of the lipid bilayer on energy transfer kinetics in the photosynthetic protein lh2
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5914429/
https://www.ncbi.nlm.nih.gov/pubmed/29732092
http://dx.doi.org/10.1039/c7sc04814a
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