Beyond ‘seeing is believing’: the antenna size of the photosystems <i>in vivo</i>

Croce, Roberta

doi:10.1111/nph.16758

Cited by 28 publications

(21 citation statements)

References 49 publications

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“…On the other hand, LHCI is generally stable and its size has not been observed to change under illumination with different light intensity (Bailey et al, 2001). However, the distances between the core and the antennas may be regulated to modulate the energy transfer reactions under fluctuating light conditions (Liu and Blankenship, 2019; Croce, 2020). Furthermore, the LHCI is likely to separate from the core under other stressful environments such as under an anaerobic environment (Nellaepalli et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

Structure of plant photosystem I−light harvesting complex I supercomplex at 2.4 Å resolution

Wang

et al. 2021

JIPB

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Photosystem I (PSI) is one of the two photosystems in photosynthesis, and performs a series of electron transfer reactions leading to the reduction of ferredoxin. In higher plants, PSI is surrounded by four light‐harvesting complex I (LHCI) subunits, which harvest and transfer energy efficiently to the PSI core. The crystal structure of PSI‐LHCI supercomplex has been analyzed up to 2.6 Å resolution, providing much information on the arrangement of proteins and cofactors in this complicated supercomplex. Here we have optimized crystallization conditions, and analyzed the crystal structure of PSI‐LHCI at 2.4 Å resolution. Our structure showed some shift of the LHCI, especially the Lhca4 subunit, away from the PSI core, suggesting the indirect connection and inefficiency of energy transfer from this Lhca subunit to the PSI core. We identified five new lipids in the structure, most of them are located in the gap region between the Lhca subunits and the PSI core. These lipid molecules may play important roles in binding of the Lhca subunits to the core, as well as in the assembly of the supercomplex. The present results thus provide novel information for the elucidation of the mechanisms for the light‐energy harvesting, transfer and assembly of this supercomplex.

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Section: Introductionmentioning

confidence: 99%

Structure of plant photosystem I−light harvesting complex I supercomplex at 2.4 Å resolution

Wang

et al. 2021

JIPB

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“…1A) [3][4][5][6]. The four symmetry-related chlorophyll (Chl) binding sites are identical, and therefore, the four bound chromophores experience identical protein surroundings and are spectroscopically equivalent, contrarily to chlorophyll (Chl)-binding complexes involved in photosynthesis, in which tens to hundreds of chromophores are bound in finely tuned individual binding sites [12], resulting in highly complex spectra. It follows that WSCP is an ideal model system for detailed spectroscopic investigation focused on understanding Chl-protein and Chl-Chl interactions [5,[13][14][15][16][17][18][19][20].…”

Section: Introductionmentioning

confidence: 99%

Electron Nuclear Double Resonance of the Chlorophyll Triplet State in the Water-Soluble Chlorophyll Protein from Brassica oleracea: Investigation of the Effect of the Binding Site on the Hyperfine Couplings

et al. 2020

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An investigation of the photoexcited triplet state of chlorophyll (Chl) a in the water-soluble chlorophyll protein (WSCP) of Brassica oleracea has been carried out by means of electron-nuclear double resonance (ENDOR), achieving a complete assignment of the observed hyperfine couplings corresponding to methine protons and methyl groups of Chl a triplet state. The triplet-state properties, and in particular the hyperfine couplings, were found to be similar to those previously reported for Chl a in the WSCP of Lepidium virginicum. Therefore, the porphyrin ring deformation observed in Brassica oleracea WSCP seems to only slightly affect the spin density of 3Chl a. This may be relevant when considering the robustness of triplet–triplet energy transfer mechanisms, relying on wavefunction overlap, in systems, such as the photosynthetic light-harvesting complexes, in which Chl triplet states with distorted geometries are involved.

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“…The light-harvesting apparatus in photosynthetic organisms are diverse in order to adapt to different living environments, including temperature variations ( Cogdell et al, 2006 ; Solov’ev and Erokhin, 2008 ; Ivanov et al, 2017 ; Madireddi et al, 2019 ; Croce, 2020 ). Exploring the mechanisms of temperature adaptation has a profound impact on understanding the energy transfer process of photosynthesis.…”

Section: Introductionmentioning

confidence: 99%

Bridging Carotenoid-to-Bacteriochlorophyll Energy Transfer of Purple Bacteria LH2 With Temperature Variations: Insights From Conformational Changes

2021

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Photosynthesis is a key process for converting light energy into chemical energy and providing food for lives on Earth. Understanding the mechanism for the energy transfers could provide insights into regulating energy transfers in photosynthesis and designing artificial photosynthesis systems. Many efforts have been devoted to exploring the mechanism of temperature variations affecting the excitonic properties of LH2. In this study, we performed all-atom molecular dynamics (MD) simulations and quantum mechanics calculations for LH2 complex from purple bacteria along with its membrane environment under three typical temperatures: 270, 300, and 330 K. The structural analysis from validated MD simulations showed that the higher temperature impaired interactions at N-terminus of both α and β polypeptide helices and led to the dissociation of this hetero polypeptide dimer. Rhodopin-β-D-glucosides (RG1) moved centripetally with α polypeptide helices when temperature increased and enlarged their distances with bacteriochlorophylls molecules that have the absorption peak at 850 nm (B850), which resulted in reducing the coupling strengths between RG1 and B850 molecules. The present study reported a cascading mechanism for temperature regulating the energy transfers in LH2 of purple bacteria.

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Beyond ‘seeing is believing’: the antenna size of the photosystems in vivo

Cited by 28 publications

References 49 publications

Structure of plant photosystem I−light harvesting complex I supercomplex at 2.4 Å resolution

Structure of plant photosystem I−light harvesting complex I supercomplex at 2.4 Å resolution

Electron Nuclear Double Resonance of the Chlorophyll Triplet State in the Water-Soluble Chlorophyll Protein from Brassica oleracea: Investigation of the Effect of the Binding Site on the Hyperfine Couplings

Bridging Carotenoid-to-Bacteriochlorophyll Energy Transfer of Purple Bacteria LH2 With Temperature Variations: Insights From Conformational Changes

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