scholarly journals STUDY ON THE STRUCTURAL BASIS OF PERIPHERAL LIGHT HARVESTING COMPLEXES (LH2) IN PURPLE NON-SULPHUR PHOTOSYNTHETIC BACTERIA

2010 ◽  
Vol 10 (3) ◽  
pp. 401-408 ◽  
Author(s):  
Tatas H.P. Brotosudarmo ◽  
Richard J. Cogdell
Keyword(s):  
Solar Energy ◽  
Photosynthetic Bacteria ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Purple Bacteria ◽  
Structural Basis ◽  
Carotenoid Pigments ◽  
Light Harvesting Complexes ◽  
Energy Funnel ◽  
Pigment Protein Complexes

Photosynthesis provides an example of a natural process that has been optimized during evolution to harness solar energy efficiently and safely, and finally to use it to produce a carbon-based fuel. Initially, solar energy is captured by the light harvesting pigment-protein complexes. In purple bacteria these antenna complexes are constructed on a rather simple modular basis. Light absorbed by these antenna complexes is funnelled downhill to reaction centres, where light drives a trans-membrane redox reaction. The light harvesting proteins not only provide the scaffolding that correctly positions the bacteriochlorophyll a and carotenoid pigments for optimal energy transfer but also creates an environment that can modulate the wavelength at which different bacteriochlorophyll molecules absorb light thereby creating the energy funnel. How these proteins can modulate the absorption spectra of the bacteriochlorophylls will be discussed in this review.

scholarly journals Structure of the stress-related LHCSR1 complex determined by an integrated computational strategy

2021 ◽  
Author(s):  
Ingrid Guarnetti Prandi ◽  
Vladislav Sláma ◽  
Cristina Pecorilla ◽  
Lorenzo Cupellini ◽  
Benedetta Mennucci
Keyword(s):  
Structural Model ◽  
Light Harvesting ◽  
Structural Information ◽  
Protein Complexes ◽  
Complex Stress ◽  
Main Function ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Pigment Protein Complexes ◽  
Computational Strategy

Light-harvesting complexes (LHCs) are pigment-protein complexes whose main function is to capture sunlight and transfer the energy to reaction centers of photosystems. In response to varying light conditions, LH complexes also play photoregulation and photoprotection roles. In algae and mosses, a sub-family of LHCs, Light-Harvesting complex stress related (LHCSR), is responsible for photoprotective quenching. Despite their functional and evolutionary importance, no direct structural information on LHCSRs is available that can explain their unique properties. In this work we propose a structural model of LHCSR1 from the moss P. Patens, obtained through an integrated computational strategy that combines homology modeling, molecular dynamics, and multiscale quantum chemical calculations. The model is validated by reproducing the spectral properties of LHCSR1. Our model reveals the structural specificity of LHCSR1, as compared with the CP29 LH complex, and poses the basis for understanding photoprotective quenching in mosses.

scholarly journals Contribution of low-temperature single-molecule techniques to structural issues of pigment–protein complexes from photosynthetic purple bacteria

2018 ◽  
Vol 15 (138) ◽  
pp. 20170680 ◽  
Author(s):  
Alexander Löhner ◽  
Richard Cogdell ◽  
Jürgen Köhler
Keyword(s):  
Low Temperature ◽  
Single Molecule ◽  
Degrees Of Freedom ◽  
Protein Complexes ◽  
Purple Bacteria ◽  
Structural Models ◽  
Spectral Features ◽  
Light Harvesting Complexes ◽  
Pigment Protein Complexes ◽  
Photosynthetic Purple Bacteria

As the electronic energies of the chromophores in a pigment–protein complex are imposed by the geometrical structure of the protein, this allows the spectral information obtained to be compared with predictions derived from structural models. Thereby, the single-molecule approach is particularly suited for the elucidation of specific, distinctive spectral features that are key for a particular model structure, and that would not be observable in ensemble-averaged spectra due to the heterogeneity of the biological objects. In this concise review, we illustrate with the example of the light-harvesting complexes from photosynthetic purple bacteria how results from low-temperature single-molecule spectroscopy can be used to discriminate between different structural models. Thereby the low-temperature approach provides two advantages: (i) owing to the negligible photobleaching, very long observation times become possible, and more importantly, (ii) at cryogenic temperatures, vibrational degrees of freedom are frozen out, leading to sharper spectral features and in turn to better resolved spectra.

scholarly journals A photosynthetic antenna complex foregoes unity carotenoid-to-bacteriochlorophyll energy transfer efficiency to ensure photoprotection

2020 ◽  
Vol 117 (12) ◽  
pp. 6502-6508 ◽  
Author(s):  
Dariusz M. Niedzwiedzki ◽  
David J. K. Swainsbury ◽  
Daniel P. Canniffe ◽  
C. Neil Hunter ◽  
Andrew Hitchcock
Keyword(s):  
Energy Transfer ◽  
Transient Absorption ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Fluorescence Emission ◽  
Energy Transfer Efficiency ◽  
Transfer Efficiency ◽  
Light Harvesting Complexes ◽  
Antenna Complex ◽  
Pigment Protein Complexes

Carotenoids play a number of important roles in photosynthesis, primarily providing light-harvesting and photoprotective energy dissipation functions within pigment–protein complexes. The carbon–carbon double bond (C=C) conjugation length of carotenoids (N), generally between 9 and 15, determines the carotenoid-to-(bacterio)chlorophyll [(B)Chl] energy transfer efficiency. Here we purified and spectroscopically characterized light-harvesting complex 2 (LH2) fromRhodobacter sphaeroidescontaining theN= 7 carotenoid zeta (ζ)-carotene, not previously incorporated within a natural antenna complex. Transient absorption and time-resolved fluorescence show that, relative to the lifetime of the S1state of ζ-carotene in solvent, the lifetime decreases ∼250-fold when ζ-carotene is incorporated within LH2, due to transfer of excitation energy to the B800 and B850 BChlsa. These measurements show that energy transfer proceeds with an efficiency of ∼100%, primarily via the S1→ Qxroute because the S1→ S0fluorescence emission of ζ-carotene overlaps almost perfectly with the Qxabsorption band of the BChls. However, transient absorption measurements performed on microsecond timescales reveal that, unlike the nativeN≥ 9 carotenoids normally utilized in light-harvesting complexes, ζ-carotene does not quench excited triplet states of BChla, likely due to elevation of the ζ-carotene triplet energy state above that of BChla. These findings provide insights into the coevolution of photosynthetic pigments and pigment–protein complexes. We propose that theN≥ 9 carotenoids found in light-harvesting antenna complexes represent a vital compromise that retains an acceptable level of energy transfer from carotenoids to (B)Chls while allowing acquisition of a new, essential function, namely, photoprotective quenching of harmful (B)Chl triplets.

scholarly journals Macrocycle ring deformation as the secondary design principle for light-harvesting complexes

2018 ◽  
Vol 115 (39) ◽  
pp. E9051-E9057 ◽  
Author(s):  
Luca De Vico ◽  
André Anda ◽  
Vladimir Al. Osipov ◽  
Anders Ø. Madsen ◽  
Thorsten Hansen
Keyword(s):  
Protein Interactions ◽  
Design Principle ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Critical Factor ◽  
Structural Factors ◽  
Modeling Tools ◽  
Light Harvesting Complexes ◽  
Pigment Protein Complexes ◽  
Rhodoblastus Acidophilus

Natural light-harvesting is performed by pigment–protein complexes, which collect and funnel the solar energy at the start of photosynthesis. The identity and arrangement of pigments largely define the absorption spectrum of the antenna complex, which is further regulated by a palette of structural factors. Small alterations are induced by pigment–protein interactions. In light-harvesting systems 2 and 3 from Rhodoblastus acidophilus, the pigments are arranged identically, yet the former has an absorption peak at 850 nm that is blue-shifted to 820 nm in the latter. While the shift has previously been attributed to the removal of hydrogen bonds, which brings changes in the acetyl moiety of the bacteriochlorophyll, recent work has shown that other mechanisms are also present. Using computational and modeling tools on the corresponding crystal structures, we reach a different conclusion: The most critical factor for the shift is the curvature of the macrocycle ring. The bending of the planar part of the pigment is identified as the second-most important design principle for the function of pigment–protein complexes—a finding that can inspire the design of novel artificial systems.

scholarly journals Silver Island Film for Enhancing Light Harvesting in Natural Photosynthetic Proteins

2020 ◽  
Vol 21 (7) ◽  
pp. 2451 ◽  
Author(s):  
Dorota Kowalska ◽  
Marcin Szalkowski ◽  
Karolina Sulowska ◽  
Dorota Buczynska ◽  
Joanna Niedziolka-Jonsson ◽  
...  
Keyword(s):  
Light Harvesting ◽  
Protein Complexes ◽  
Photosynthetic Pigment ◽  
Functional Materials ◽  
Photosynthetic Reaction Centers ◽  
Light Harvesting Complexes ◽  
Pigment Protein Complexes ◽  
Chlorophyll Protein ◽  
Silver Island ◽  
Photosynthetic Complexes

The effects of combining naturally evolved photosynthetic pigment–protein complexes with inorganic functional materials, especially plasmonically active metallic nanostructures, have been a widely studied topic in the last few decades. Besides other applications, it seems to be reasonable using such hybrid systems for designing future biomimetic solar cells. In this paper, we describe selected results that point out to various aspects of the interactions between photosynthetic complexes and plasmonic excitations in Silver Island Films (SIFs). In addition to simple light-harvesting complexes, like peridinin-chlorophyll-protein (PCP) or the Fenna–Matthews–Olson (FMO) complex, we also discuss the properties of large, photosynthetic reaction centers (RCs) and Photosystem I (PSI)—both prokaryotic PSI core complexes and eukaryotic PSI supercomplexes with attached antenna clusters (PSI-LHCI)—deposited on SIF substrates.

Structural Role of Carotenoids in Photosynthetic Membranes

1996 ◽  
Vol 51 (11-12) ◽  
pp. 763-771 ◽  
Author(s):  
Andrey A Moskalenko ◽  
Navassard V Karapetyan
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Purple Bacteria ◽  
Reaction Centers ◽  
Structural Components ◽  
Light Harvesting Complexes ◽  
Photosynthetic Membranes

Besides the light-harvesting and protecting role, carotenoids are also instrumental as structural components for the assembly of light-harvesting complexes in purple bacteria and green plants, as well as for the formation of photosystem II complex. Carotenoids stabilize those pigm ent-protein complexes, but have no effect on the form ation of the reaction centers of purple bacteria and photosystem I of plants.

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