scholarly journals The CP43 Proximal Antenna Complex of Higher Plant Photosystem II Revisited: Modeling and Hole Burning Study. I

2008 ◽  
Vol 112 (32) ◽  
pp. 9921-9933 ◽  
Author(s):  
Nhan C. Dang ◽  
Valter Zazubovich ◽  
Mike Reppert ◽  
Bhanu Neupane ◽  
Rafael Picorel ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Hole Burning ◽  
Higher Plant ◽  
Antenna Complex

scholarly journals On the Conflicting Estimations of Pigment Site Energies in Photosynthetic Complexes: A Case Study of the CP47 Complex

2016 ◽  
Vol 11 ◽  
pp. ACI.S32151 ◽  
Author(s):  
Tonu Reinot ◽  
Jinhai Chen ◽  
Adam Kell ◽  
Mahboobe Jassas ◽  
Kevin C. Robben ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Population Dynamics ◽  
Photosystem Ii ◽  
Hole Burning ◽  
Protein Subunit ◽  
Structure Population ◽  
Chl A ◽  
Antenna Complex ◽  
Photosynthetic Complexes

We focus on problems with elucidation of site energies ( E n0) for photosynthetic complexes (PSCs) in order to raise some genuine concern regarding the conflicting estimations propagating in the literature. As an example, we provide a stern assessment of the site energies extracted from fits to optical spectra of the widely studied CP47 antenna complex of photosystem II from spinach, though many general comments apply to other PSCs as well. Correct values of E n0 for chlorophyll (Chl) a in CP47 are essential for understanding its excitonic structure, population dynamics, and excitation energy pathway(s). To demonstrate this, we present a case study where simultaneous fits of multiple spectra (absorption, emission, circular dichroism, and nonresonant hole-burned spectra) show that several sets of parameters can fit the spectra very well. Importantly, we show that variable emission maxima (690-695 nm) and sample-dependent bleaching in nonresonant hole-burning spectra reported in literature could be explained, assuming that many previously studied CP47 samples were a mixture of intact and destabilized proteins. It appears that the destabilized subpopulation of CP47 complexes could feature a weakened hydrogen bond between the 13 1 -keto group of Chl29 and the PsbH protein subunit, though other possibilities cannot be entirely excluded, as discussed in this work. Possible implications of our findings are briefly discussed.

scholarly journals Use of protein cross-linking and radiolytic footprinting to elucidate PsbP and PsbQ interactions within higher plant Photosystem II

2014 ◽  
Vol 111 (45) ◽  
pp. 16178-16183 ◽  
Author(s):  
Manjula P. Mummadisetti ◽  
Laurie K. Frankel ◽  
Henry D. Bellamy ◽  
Larry Sallans ◽  
Jost S. Goettert ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Cross Linking ◽  
Higher Plant ◽  
Protein Cross Linking

scholarly journals Energy Transfer Pathways in the Minor Antenna Complex CP29 of Photosystem II: A Femtosecond Study of Carotenoid to Chlorophyll Transfer on Mutant and WT Complexes

2003 ◽  
Vol 84 (4) ◽  
pp. 2517-2532 ◽  
Author(s):  
Roberta Croce ◽  
Marc G. Müller ◽  
Stefano Caffarri ◽  
Roberto Bassi ◽  
Alfred R. Holzwarth
Keyword(s):  
Energy Transfer ◽  
Photosystem Ii ◽  
Antenna Complex

scholarly journals Electronic Structure of Tyrosyl D Radical of Photosystem II, as Revealed by 2D-Hyperfine Sublevel Correlation Spectroscopy

2021 ◽  
Vol 7 (9) ◽  
pp. 131
Author(s):  
Maria Chrysina ◽  
Georgia Zahariou ◽  
Nikolaos Ioannidis ◽  
Yiannis Sanakis ◽  
George Mitrikas
Keyword(s):  
Electronic Structure ◽  
Photosystem Ii ◽  
Water Oxidation ◽  
Spinacia Oleracea ◽  
Higher Plants ◽  
Correlation Spectroscopy ◽  
Oxygen Evolving Complex ◽  
Higher Plant ◽  
Proton Coupled Electron Transfer ◽  
S Oxidation

The biological water oxidation takes place in Photosystem II (PSII), a multi-subunit protein located in thylakoid membranes of higher plant chloroplasts and cyanobacteria. The catalytic site of PSII is a Mn4Ca cluster and is known as the oxygen evolving complex (OEC) of PSII. Two tyrosine residues D1-Tyr161 (YZ) and D2-Tyr160 (YD) are symmetrically placed in the two core subunits D1 and D2 and participate in proton coupled electron transfer reactions. YZ of PSII is near the OEC and mediates electron coupled proton transfer from Mn4Ca to the photooxidizable chlorophyll species P680+. YD does not directly interact with OEC, but is crucial for modulating the various S oxidation states of the OEC. In PSII from higher plants the environment of YD• radical has been extensively characterized only in spinach (Spinacia oleracea) Mn- depleted non functional PSII membranes. Here, we present a 2D-HYSCORE investigation in functional PSII of spinach to determine the electronic structure of YD• radical. The hyperfine couplings of the protons that interact with the YD• radical are determined and the relevant assignment is provided. A discussion on the similarities and differences between the present results and the results from studies performed in non functional PSII membranes from higher plants and PSII preparations from other organisms is given.

Persistent spectral hole-burning study on photosystem II reaction center reconstructed with dibromothymoquinone

2002 ◽  
Vol 98 (1-4) ◽  
pp. 131-139
Author(s):  
Y Kawamata ◽  
S Machida ◽  
K Horie ◽  
S Itoh ◽  
M Iwaki ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Reaction Center ◽  
Hole Burning ◽  
Spectral Hole Burning ◽  
Spectral Hole
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