Corrigendum to “Structure and dynamics of the N-terminal loop of PsbQ from photosystem II of Spinacia oleracea” [Biochem. Biophys. Res. Commun. 345 (2006) 287–291]

2006 ◽  
Vol 348 (3) ◽  
pp. 1205
Author(s):  
Jaroslava Ristvejová ◽  
Vladimír Kopecký ◽  
Žofie Sovová ◽  
Mónica Balsera ◽  
Juan B. Arellano ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Spinacia Oleracea ◽  
Structure And Dynamics ◽  
Terminal Loop

Structure and dynamics of the N-terminal loop of PsbQ from photosystem II of Spinacia oleracea

2006 ◽  
Vol 345 (1) ◽  
pp. 287-291 ◽  
Author(s):  
Jaroslava Ristvejová ◽  
Vladimír Kopecký ◽  
Žofie Sovová ◽  
Mónica Balsera ◽  
Juan B. Arellano ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Spinacia Oleracea ◽  
Structure And Dynamics ◽  
Terminal Loop

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.

scholarly journals Investigating the Structure and Dynamics of Apo‐Photosystem II

ChemCatChem ◽  
2019 ◽  
Vol 11 (16) ◽  
pp. 4072-4080 ◽  
Author(s):  
Ruocheng Han ◽  
Katharina Rempfer ◽  
Miao Zhang ◽  
Holger Dobbek ◽  
Athina Zouni ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Structure And Dynamics

scholarly journals The effects of high concentrations of salts on photosynthetic electron transport in spinach (Spinacia oleracea) chloroplasts

1982 ◽  
Vol 204 (3) ◽  
pp. 705-712 ◽  
Author(s):  
A C Stewart
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Photosystem I ◽  
Spinacia Oleracea ◽  
Photosynthetic Electron Transport ◽  
Potassium Citrate ◽  
O2 Evolution ◽  
Hofmeister Series ◽  
Reaction Centre ◽  
High Concentrations

1. Photosynthetic electron transport from water to lipophilic Photosystem II acceptors was stimulated 3-5-fold by high concentrations (greater than or equal to 1 M) of salts containing anions such as citrate, succinate and phosphate that are high in the Hofmeister series. 2. In trypsin-treated chloroplasts, K3Fe(CN)6 reduction insensitive to 3-(3,4-dichlorophenyl)-1,1-dimethylurea was strongly stimulated by high concentrations of potassium citrate, but there was much less stimulation of 2,6-dichloroindophenol reduction in Tris-treated chloroplasts supplied with 1,5-diphenylcarbazide as artificial donor. The results suggest that the main site of action of citrate was the O2-evolving complex of Photosystem II. 3. Photosystem I partial reactions were also stimulated by intermediate concentrations of citrate (up to 2-fold stimulation by 0.6-0.8 M-citrate), but were inhibited at the highest concentrations. The observed stimulation may have been caused by stabilizaton of plastocyanin that was complexed with the Photosystem I reaction centre, 4. At 1 M, potassium citrate protected O2 evolution against denaturation by heat or by the chaotropic agent NaNO3. 5. It is suggested that anions high in the Hofmeister series stimulated and stabilized electron transport by enhancing water structure around the protein complexes in the thylakoid membrane.

scholarly journals Preparation and Photosynthesis-Inhibiting Activity of Novel Dihalogenated 3-Hydroxynaphthalene-2-carboxanilides

Proceedings ◽  
2019 ◽  
Vol 41 (1) ◽  
pp. 30
Author(s):  
Jiri Kos ◽  
Tomas Gonec ◽  
Tomas Strharsky ◽  
Michal Oravec ◽  
Josef Jampilek
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Spinacia Oleracea ◽  
Photosynthetic Electron Transport ◽  
Microwave Assisted Synthesis ◽  
Inhibiting Activity ◽  
Microwave Assisted ◽  
Spinacia Oleracea L ◽  
Wide Range

In this study, a series of nine 3-hydroxynaphthalene-2-carboxanilides, disubstituted on the anilide ring by fluorine, chlorine and bromine in various positions, was prepared by microwave-assisted synthesis and characterized. The compounds were tested for their activity related to the inhibition of photosynthetic electron transport (PET) in spinach (Spinacia oleracea L.) chloroplasts. The PET-inhibiting activity of the compounds was within a wide range, but rather moderate; the highest activity within the series of the compounds was observed for N-(3,5-difluorophenyl)-3-hydroxynaphthalene-2-carboxamide (IC50 = 9.8 µM). The compounds were found to inhibit PET in photosystem II.

Low-Energy Exciton Level Structure and Dynamics in LightHarvesting Complex II Trimers from the Chl a/b Antenna Complex of Photosystem II

1994 ◽  
Vol 98 (17) ◽  
pp. 4729-4735 ◽  
Author(s):  
N. R. S. Reddy ◽  
H. van Amerongen ◽  
S. L. S. Kwa ◽  
R. van Grondelle ◽  
G. J. Small
Keyword(s):  
Photosystem Ii ◽  
Level Structure ◽  
Low Energy ◽  
Complex Ii ◽  
Chl A ◽  
Structure And Dynamics ◽  
Antenna Complex

High-and Low-Affinity Binding of Photosystem II Herbicides to Isolated Thylakoid Membranes and Intact Algal Cells

1982 ◽  
Vol 37 (7-8) ◽  
pp. 620-631 ◽  
Author(s):  
Henrik Laasch ◽  
Klaus Pfister ◽  
Wolfgang Urbach
Keyword(s):  
Photosystem Ii ◽  
Binding Site ◽  
Spinacia Oleracea ◽  
Specific Binding ◽  
Affinity Binding ◽  
Concentration Effects ◽  
Intact Cells ◽  
High Affinity Binding ◽  
High Affinity ◽  
Receptor Sites

Abstract High- and low-affinity binding of photosystem II herbicides to isolated thylakoids of Spinacia oleracea and to intact cells of the unicellular green alga Ankistrodesmus braunii were investigated. Complete mutual displacement of bound diuron-type herbicides (e.g. diuron, atrazine, terbutryn) by either diuron- or phenol-type herbicides (e.g. ioxynil, dinoseb) in thylakoids as well as in intact algal cells was found for herbicide concentrations (< 4 nmol bound herbicide/mg Chl) which gave almost saturated high-affinity binding. This demonstrates a high degree of specific binding of these herbicides towards their receptor sites even in intact algal cells. In contrast, phenol-type herbicides are largely unspecifically bound in algal cells. The mechanism of binding of all photosystem II herbicides at the high-affinity (specific) binding site was found to be competitive. Within the group of diuron-type and of phenol-type herbicides as well as between these two groups, graphical and quantitative analysis of the Lineweaver- Burk plot and of the Dixon plot indicated competitive binding. From this a common binding site for both types of herbicides was concluded. The involvement of two different herbicide binding- proteins is discussed. Low-affinity (unspecific) binding was found to be irreversible in contrast to the easily reversible high-affinity binding. Irreversibility was indicated by a lack of displacement. It is proposed that low-affinity binding represents either a partitioning of the herbicides into the lipophilic parts of the membranes or an attachment to distinct receptor sites. Unspecifically bound herbicides might be responsible for several high concentration effects of the photosystem II herbicides, which are described in the literature. Evidences for the possible existence of a second binding site of these herbicides are presented.

Functional Heterogeneity of Photosystem II in Domain Specific Regions of the Thylakoid Membrane of Spinach (Spinacia oleracea L.)†

Biochemistry ◽  
2007 ◽  
Vol 46 (11) ◽  
pp. 3443-3453 ◽  
Author(s):  
John Veerman ◽  
Michael D. McConnell ◽  
Sergei Vasil'ev ◽  
Fikret Mamedov ◽  
Stenbjörn Styring ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Thylakoid Membrane ◽  
Spinacia Oleracea ◽  
Functional Heterogeneity ◽  
Domain Specific ◽  
Spinacia Oleracea L
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