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.

On the question of the light-harvesting role of β-carotene in photosystem II and photosystem I core complexes

2014 ◽  
Vol 81 ◽  
pp. 121-127 ◽  
Author(s):  
Kostas Stamatakis ◽  
Merope Tsimilli-Michael ◽  
George C. Papageorgiou
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Light Harvesting ◽  
Β Carotene

Isolation and characterization of three membranebound chlorophyll-protein complexes from four dinoflagellate species

1993 ◽  
Vol 340 (1294) ◽  
pp. 381-392 ◽  
Keyword(s):  
Energy Transfer ◽  
Photosystem I ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Gradient Centrifugation ◽  
Water Soluble ◽  
Molar Ratio ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Isolation And Characterization

Employing discontinuous sucrose density gradient centrifugation of n -dodecyl β-d-maltoside-solubilized thylakoid membranes, three chlorophyll (Chl)-protein complexes containing Chl a , Chl c 2 and peridinin in different proportions, were isolated from the dinoflagellates Symbiodinium microadriaticum, S. kawagutii, S. pilosum and Heterocapsa pygmaea . In S. microadriaticum , the first complex, containing 13% of the total cellular Chl a , and minor quantities of Chl c 2 and peridinin, is associated with polypeptides with apparent molecular mass ( M r ) of 8-9 kDa, and demonstrated inefficient energy transfer from the accessory pigments to Chl a . The second complex contains Chl a , Chl c 2 and peridinin in a molar ratio of 1:1:2, associated with two apoproteins of M r 19-20 kDa, and comprises 45%, 75% and 70%, respectively, of the cellular Chl a , Chl c 2 and peridinin. The efficient energy transfer from Chl c 2 and peridinin to Chl a in this complex is supportive of a light-harvesting function. This Chl a - c 2 - peridin-protein complex represents the major light-harvesting complex in dinoflagellates. The third complex obtained contains 12% of the cellular Chl a , and appears to be the core of photosystem I, associated with a light-harvesting complex. This complex is spectroscopically similar to analogous preparations from different taxonomic groups, but demonstrates a unique apoprotein composition. Antibodies against the water-soluble peridinin-Chl a -protein (sPCP) light-harvesting complexes failed to cross-react with any of the thylakoid-associated complexes, as did antibodies against Chl a - c -fucoxanthin apoprotein (from diatoms). Antibodies against the P 700 apoprotein of plants did not cross-react with the photosystem I complex. Similar results were observed in the other dinoflagellates.

scholarly journals Photosynthetic light harvesting and thylakoid organization in a CRISPR/Cas9 Arabidopsis thaliana LHCB1 knockout mutant.

2021 ◽  
Author(s):  
Hamed Sattari Vayghan ◽  
Wojciech J Nawrocki ◽  
Christo Schiphorst ◽  
Dimitri Tolleter ◽  
Hu Chen ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Cross Section ◽  
Photosystem I ◽  
Absorption Cross Section ◽  
Light Harvesting ◽  
Higher Plants ◽  
Oxygenic Photosynthesis ◽  
Growth Delay ◽  
Absorption Cross ◽  
Light Harvesting Complexes

Light absorbed by chlorophylls of photosystem II and I drives oxygenic photosynthesis. Light-harvesting complexes increase the absorption cross-section of these photosystems. Furthermore, these complexes play a central role in photoprotection by dissipating the excess of absorbed light energy in an inducible and regulated fashion. In higher plants, the main light-harvesting complex is the trimeric LHCII. In this work, we used CRISPR/Cas9 to knockout the five genes encoding LHCB1, which is the major component of the trimeric LHCII. In absence of LHCB1 the accumulation of the other LHCII isoforms was only slightly increased, thereby resulting in chlorophyll loss leading to a pale green phenotype and growth delay. Photosystem II absorption cross-section was smaller while photosystem I absorption cross-section was unaffected. This altered the chlorophyll repartition between the two photosystems, favoring photosystem I excitation. The equilibrium of the photosynthetic electron transport was partially maintained by a lower photosystem I over photosystem II reaction center ratio and by the dephosphorylation of LHCII and photosystem II. Loss of LHCB1 altered the thylakoid structure, with less membrane layers per grana stack and reduced grana width. Stable LHCB1 knock out lines allow characterizing the role of this protein in light harvesting and acclimation and pave the way for future in vivo mutational analyses of LHCII.

scholarly journals Theoretical Assessment of Hinge-Type Models for Electron Donors in Reaction Centers of Photosystems I and II as Well as of Purple Bacteria

2020 ◽  
Author(s):  
Denis Artiukhin ◽  
Patrick Eschenbach ◽  
Jörg Matysik ◽  
Johannes Neugebauer
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Purple Bacteria ◽  
High Sensitivity ◽  
Reaction Centers ◽  
Electron Donors ◽  
Molecular Systems ◽  
Density Distributions ◽  
Theoretical Assessment ◽  
Spin Densities

Hinge-type molecular models for electron donors in reaction centers of Photosystem I, II, and purple bacteria were investigated using a two-state computational approach based on Frozen-Density Embedding. This methodology, dubbed FDE-diab, is known to avoid consequences of the self-interaction error as far as intermolecular phenomena are concerned, which allows to predict qualitatively correct spin densities for large bio-molecular systems. The calculated spin density distributions are in a good agreement with available experimental results and demonstrated a very high sensitivity to changes in relative orientiation of co-factors and amino-acid protonation states. This allows to validate the previously proposed hinge-type models and make predictions on protonation states of axial histidine molecules. Contrary to the reaction centers in Photosystem I and purple bacteria, the axial histidines from Photosystem II were found to be deprotonated. This fact might shed some light on remarkable properties of Photosystem II reaction centers.

scholarly journals Theoretical Assessment of Hinge-Type Models for Electron Donors in Reaction Centers of Photosystems I and II as Well as of Purple Bacteria

2020 ◽  
Author(s):  
Denis Artiukhin ◽  
Patrick Eschenbach ◽  
Jörg Matysik ◽  
Johannes Neugebauer
Keyword(s):  
Photosystem Ii ◽  
Photosystem I ◽  
Purple Bacteria ◽  
High Sensitivity ◽  
Reaction Centers ◽  
Electron Donors ◽  
Molecular Systems ◽  
Density Distributions ◽  
Theoretical Assessment ◽  
Spin Densities

Hinge-type molecular models for electron donors in reaction centers of Photosystem I, II, and purple bacteria were investigated using a two-state computational approach based on Frozen-Density Embedding. This methodology, dubbed FDE-diab, is known to avoid consequences of the self-interaction error as far as intermolecular phenomena are concerned, which allows to predict qualitatively correct spin densities for large bio-molecular systems. The calculated spin density distributions are in a good agreement with available experimental results and demonstrated a very high sensitivity to changes in relative orientiation of co-factors and amino-acid protonation states. This allows to validate the previously proposed hinge-type models and make predictions on protonation states of axial histidine molecules. Contrary to the reaction centers in Photosystem I and purple bacteria, the axial histidines from Photosystem II were found to be deprotonated. This fact might shed some light on remarkable properties of Photosystem II reaction centers.

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.

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