Spectroscopic Study of the CP43′ Complex and the PSI–CP43′ Supercomplex of the Cyanobacterium Synechocystis PCC 6803 [PDF]
The PSI-CP43' supercomplex of the cyanobacterium Synechocystis PCC 6803, grown under iron-starvation conditions, consists of a trimeric core Photosystem I (PSI) complex and an outer ring of 18 CP43' light-harvesting complexes. We have investigated the electronic structure and excitation energy transfer (EET) pathways within the CP43' (also known as the
Feng, Ximao +6 more
openaire +4 more sources
Spectroscopic study of the light-induced changes of the core antenna complex CP43 in photosystem II
In this study, spectroscopic approaches were used to evaluate light-induced changes in chlorophyll protein 43 (CP43). Upon illumination, we observed chlorophyll (Chl) a bleaching with the complete opening of the tetrapyrrole ring.
Y.G. QU, F. ZHOU, T.Y. KUANG
doaj +2 more sources
Excitation landscape of the CP43 photosynthetic antenna complex from multiscale simulations. [PDF]
QM/MM simulations and the perturbed matrix method are used to investigate a crucial photosynthetic antenna complex, mapping its global excitonic structure and revealing the presence of a low-lying charge transfer state.
Bhattacharjee S +3 more
europepmc +8 more sources
Posttranslational modifications in the CP43 subunit of photosystem II [PDF]
Photosystem II (PSII) catalyzes the light-driven oxidation of water and the reduction of plastoquinone; the oxidation of water occurs at a cluster of four manganese. The PSII CP43 subunit functions in light harvesting, and mutations in the fifth luminal loop (E) of CP43 have established its importance in PSII structure and/or ...
Anderson, Lorraine B. +9 more
core +4 more sources
Spectroscopic Properties of the CP43 Core Antenna Protein of Photosystem II [PDF]
CP43 is a chlorophyll-protein complex that funnels excitation energy from the main light-harvesting system of photosystem II to the photochemical reaction center. We purified CP43 from spinach photosystem II membranes in the presence of the nonionic detergent n-dodecyl-beta,D-maltoside and recorded its spectroscopic properties at various temperatures ...
Groot, ML +8 more
core +5 more sources
Characterization by electron microscopy of dimeric Photosystem II core complexes from spinach with and without CP43 [PDF]
AbstractDimeric associations of the D1-D2-CP47 and D1-D2-CP47-CP43 complexes of Photosystem II from spinach were isolated and purified with sucrose density gradient centrifugation and gel filtration chromatography and analyzed by electron microscopy and image analysis. Images of both preparations show characteristic details in protein density.
Eijckelhoff, Camiel +2 more
openaire +4 more sources
Participation of Glutamate-354 of the CP43 Polypeptide in the Ligation of Manganese and the Binding of Substrate Water in Photosystem II [PDF]
In the current X-ray crystallographic structural models of photosystem II, Glu354 of the CP43 polypeptide is the only amino acid ligand of the oxygen-evolving Mn(4)Ca cluster that is not provided by the D1 polypeptide. To further explore the influence of this structurally unique residue on the properties of the Mn(4)Ca cluster, the CP43-E354Q mutant of
Service, Rachel J +9 more
openaire +5 more sources
ODMR of carotenoid and chlorophyll triplets in CP43 and CP47 complexes of spinach
Abstract Optically detected magnetic resonance (ODMR) of the light-harvesting complexes CP43 and CP47 of the spinach photosynthetic machinery revealed triplet states both from carotenoids and chlorophylls. The triplet state of the only carotenoid present in the complexes (β-carotene) is observed by ODMR using fluorescence detection (FDMR) in the main
CARBONERA, DONATELLA +4 more
openaire +2 more sources
Isolation of CP43 and CP47 Photosystem II Proximal Antenna Complexes From Plants
A single-column method to purify the CP43 and CP47 pigment-protein complexes of photo-system (PS)II from higher plants is presented. To validate the isolation procedure, three different species were used (Spinacea oleracea, Beta vulgaris, and Glycine max), and the procedure worked similarly with all three.
Picorel Castaño, Rafael +2 more
openaire +4 more sources
The structure of intact and active Photosystem II from Arabidopsis thaliana at 2.44 Å resolution. [PDF]
Summary Photosystem II (PS II) is a large membrane‐bound protein complex that catalyses light‐driven water oxidation in plants and cyanobacteria. The structure of PS II is well studied in cyanobacteria; however, there are very few PS II structures from plants.
Forsman J +6 more
europepmc +2 more sources

