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Recombinant Light Harvesting Complexes: Views and Perspectives

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Book cover Photosynthesis: Structures, Mechanisms, and Applications

Summary

This review introduces to the method of in vitro reconstitution of pigment-protein complexes of higher plants, a technique which allows for the assembly of functional antenna proteins starting from free pigments and bacterially-expressed apoprotein. After discussing the reconstitution method itself, the key elements required for it (xanthophylls and chlorophyll b) and the timescales of the process, a few examples of the achievements made by using recombinant proteins are presented. Site-directed mutagenesis of chlorophyll-binding residues of recombinant complexes provided an important contribution to the field of photosynthesis by allowing the identification of the transition energy levels of individual chromophores. Progress has also been made employing recombinant antenna complexes in photovoltaic applications (quantum dots and Ti2O catalyst), a recent and still largely unexplored field of research. Finally, the recent use of luminal loop mutants of LHCII for the study of the non-photochemical quenching (NPQ) mechanism, one of the most studied phenomena in photosynthesis, revealed insights into how NPQ is triggered by low pH. It is proposed that reconstituting the NPQ locus in vitro in liposomes with a natural thylakoid membrane lipid composition, containing purified/recombinant LHCII, minor antennae and PsbS in various combinations and concentrations may clarify how the NPQ mechanism works at a molecular level

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Abbreviations

CP:

chlorophyll binding protein

D:

aspartate

DCCD:

dicyclohexylcarbodiimide

DM:

dodecylmaltoside

E:

glutamate

FFEM:

freeze-fracture electron microscopy

G:

glycine

H:

histidine

HOMO:

highest occupied molecular orbital

HPLC:

high pressure liquid chromatography

IPTG:

Isopropil-β-D-1-tiogalattopiranoside

LHCII:

light harvesting complex II

LUMO:

lowest unoccupied molecular orbital

Ni-NTA:

Nickel- Nitrilotriacetic acid

NMR:

Nuclear magnetic resonance

NPQ:

non-photochemical quenching

OGP:

Octyl β-D-glucopyranoside

PSII:

photosystem II

Q:

glutamine

QD:

quantum dot

R:

arginine

RT:

room temperature

SDS:

sodium-dodecyl sulphate

V:

valine

W:

tryptophan

WT:

wild type

Y:

tyrosine

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Acknowledgements

This work was supported by The Leverhulme Trust Research Grant RPG-2012-478 awarded to AVR.

Conflict of Interest

None Declared.

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Authors and Affiliations

  1. School of Biological and Chemical Sciences, Queen Mary University of London, London, UK

    Erica Belgio & Alexander V. Ruban

  2. Department of Autotrophic Microorganisms – ALGATECH, Institute of Microbiology ASCR, Třeboň, Czech Republic

    Erica Belgio

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  1. Erica Belgio
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  2. Alexander V. Ruban
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Correspondence to Erica Belgio .

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Editors and Affiliations

  1. Department of Physical Sciences, Alabama State University, Montgomery, Alabama, USA

    Harvey J.M. Hou

  2. Center for Research in Climate Change and Global Warming, Institute for Advanced Studies in Basic Sciences, Zanjan, Iran

    Mohammad Mahdi Najafpour

  3. School of Molecular Sciences, Center for Applied Structural Discovery at the Biodesign Institute, Arizona State University, Tempe, Arizona, USA

    Gary F. Moore

  4. Institute of Plant Physiology, Russian Academy of Sciences, Moscow, Russia

    Suleyman I. Allakhverdiev

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Belgio, E., Ruban, A.V. (2017). Recombinant Light Harvesting Complexes: Views and Perspectives. In: Hou, H., Najafpour, M., Moore, G., Allakhverdiev, S. (eds) Photosynthesis: Structures, Mechanisms, and Applications. Springer, Cham. https://doi.org/10.1007/978-3-319-48873-8_3

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