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Title: Excitation energy transfer between monomolecular layers of light harvesting LH2 and LH1-reaction centre complexes printed on a glass substrate

Abstract

Light-harvesting 2 (LH2) and light-harvesting 1 – reaction centre (RCLH1) complexes purified from the photosynthetic bacterium Rhodobacter (Rba.) sphaeroides were cross-patterned on glass surfaces for energy transfer studies. Atomic force microscopy (AFM) images of the RCLH1 and LH2 patterns show the deposition of monomolecular layers of complexes on the glass substrate. Spectral imaging and fluorescence life-time imaging microscopy (FLIM) revealed that RCLH1 and LH2 complexes, sealed under physiological conditions, retained their native light-harvesting and energy transfer functions. Measurements of the amplitude and lifetime decay of fluorescence emission from LH2 complexes, the energy transfer donors, and gain of fluorescence emission from acceptor RCLH1 complexes, provide evidence for excitation energy transfer from LH2 to RCLH1. Directional energy transfer on the glass substrate was unequivocally established by using LH2-carotenoid complexes and RCLH1 complexes with genetically removed carotenoids. Specific excitation of carotenoids in donor LH2 complexes elicited fluorescence emission from RCLH1 acceptors. To explore the longevity of this novel nanoprinted photosynthetic unit, RCLH1 and LH2 complexes were cross-patterned on a glass surface and sealed under a protective argon atmosphere. The results show that both complexes retained their individual and collective functions and are capable of directional excitation energy transfer for at least 60 days.

Authors:
 [1]; ORCiD logo [2];  [2]
  1. Department of Molecular Biology and Biotechnology;University of Sheffield;Sheffield S10 2TN;UK;CAS Key Lab of Bio-Medical Diagnostics
  2. Department of Molecular Biology and Biotechnology;University of Sheffield;Sheffield S10 2TN;UK
Publication Date:
Research Org.:
Washington Univ., St. Louis, MO (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES); Biotechnology and Biological Sciences Research Council (BBSRC UK)
OSTI Identifier:
1633684
Alternate Identifier(s):
OSTI ID: 1676408
Grant/Contract Number:  
SC0001035; BB/M000265/1
Resource Type:
Published Article
Journal Name:
Lab on a chip (Print)
Additional Journal Information:
Journal Name: Lab on a chip (Print) Journal Volume: 20 Journal Issue: 14; Journal ID: ISSN 1473-0197
Publisher:
Royal Society of Chemistry
Country of Publication:
France
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Huang, Xia, Vasilev, Cvetelin, and Hunter, C. Neil. Excitation energy transfer between monomolecular layers of light harvesting LH2 and LH1-reaction centre complexes printed on a glass substrate. France: N. p., 2020. Web. https://doi.org/10.1039/d0lc00156b.
Huang, Xia, Vasilev, Cvetelin, & Hunter, C. Neil. Excitation energy transfer between monomolecular layers of light harvesting LH2 and LH1-reaction centre complexes printed on a glass substrate. France. https://doi.org/10.1039/d0lc00156b
Huang, Xia, Vasilev, Cvetelin, and Hunter, C. Neil. Wed . "Excitation energy transfer between monomolecular layers of light harvesting LH2 and LH1-reaction centre complexes printed on a glass substrate". France. https://doi.org/10.1039/d0lc00156b.
@article{osti_1633684,
title = {Excitation energy transfer between monomolecular layers of light harvesting LH2 and LH1-reaction centre complexes printed on a glass substrate},
author = {Huang, Xia and Vasilev, Cvetelin and Hunter, C. Neil},
abstractNote = {Light-harvesting 2 (LH2) and light-harvesting 1 – reaction centre (RCLH1) complexes purified from the photosynthetic bacterium Rhodobacter (Rba.) sphaeroides were cross-patterned on glass surfaces for energy transfer studies. Atomic force microscopy (AFM) images of the RCLH1 and LH2 patterns show the deposition of monomolecular layers of complexes on the glass substrate. Spectral imaging and fluorescence life-time imaging microscopy (FLIM) revealed that RCLH1 and LH2 complexes, sealed under physiological conditions, retained their native light-harvesting and energy transfer functions. Measurements of the amplitude and lifetime decay of fluorescence emission from LH2 complexes, the energy transfer donors, and gain of fluorescence emission from acceptor RCLH1 complexes, provide evidence for excitation energy transfer from LH2 to RCLH1. Directional energy transfer on the glass substrate was unequivocally established by using LH2-carotenoid complexes and RCLH1 complexes with genetically removed carotenoids. Specific excitation of carotenoids in donor LH2 complexes elicited fluorescence emission from RCLH1 acceptors. To explore the longevity of this novel nanoprinted photosynthetic unit, RCLH1 and LH2 complexes were cross-patterned on a glass surface and sealed under a protective argon atmosphere. The results show that both complexes retained their individual and collective functions and are capable of directional excitation energy transfer for at least 60 days.},
doi = {10.1039/d0lc00156b},
journal = {Lab on a chip (Print)},
number = 14,
volume = 20,
place = {France},
year = {2020},
month = {1}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.1039/d0lc00156b

Figures / Tables:

Fig. 1 Fig. 1: Schematic diagram of the micro-contact printing method used to fabricate the cross-patterned LH2 and RCLH1 protein arrays. A – Si master with rectangular arrays of 5 μm width, 10 μm pitch and 1.35 μm step height. B and C – Casting a PDMS replica of the master. Dmore » and E – Inking the stamp with LH2 (green). F – PLL coated glass reacted with DMS (yellow). G and H – Printing LH2 on glass; I – printing RCLH1 complexes (red) on glass orthogonally to LH2 arrays.« less

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