scholarly journals Nucleotide sequence of the gene from the cyanobacterium Anacystis nidulans R2 encoding the Mn-stabilizing protein involved in photosystem II water oxidation.

1987 ◽  
Vol 84 (23) ◽  
pp. 8230-8234 ◽  
Author(s):  
T. Kuwabara ◽  
K. J. Reddy ◽  
L. A. Sherman
Keyword(s):  
Nucleotide Sequence ◽  
Photosystem Ii ◽  
Water Oxidation ◽  
Anacystis Nidulans

Inactivation of Photosynthetic O2 Evolution in the Cyanobacterium Anacystis nidulans PCC 6301: Influence of Nitrogen Metabolites and Divalent Cation Concentration

1991 ◽  
Vol 46 (11-12) ◽  
pp. 1024-1032 ◽  
Author(s):  
Gudrun Wälzlein ◽  
Elfriede K. Pistorius
Keyword(s):  
Photosystem Ii ◽  
Nitrogen Source ◽  
Divalent Cation ◽  
Water Oxidation ◽  
Divalent Cations ◽  
Nitrogen Deficiency ◽  
Anacystis Nidulans ◽  
O2 Evolution ◽  
Cation Deficiency

Abstract An investigation about the in vivo inactivation of photosynthetic water oxidation has been carried out in the cyanobacterium Anacystis nidulans (Synechococcus PCC 6301). Photosystem II and photosystem I activity as well as the relative amount of the D1 and manganese stabilizing peptide of photosystem II were determined after growing the cells in nutrient media with variations in the nitrogen source and the concentration of the major divalent cations (Mg2+ and Ca2+). The results show a rapid inactivation of water oxidation in A. nidulans in response to nitrogen deficiency and in response to reduced Mg2+ and Ca2+ concentrations. The inactivation of water oxidation observed under divalent cation deficiency could be greatly accelerated when L-amino acids instead of ammonia or nitrate were used as nitrogen source. Under these conditions inactivation of water oxidation correlated with a rapid loss of D1 and with a slower loss of the manganese stabilizing peptide from photosystem II. A possible regulation of the photosystem II activity in A. nidulans by nitrogen metabolites is suggested.

Effect of Magnesium and Calcium Ions on the Photoelectron Transport Activity of Low-Salt Suspended Hydrilla verticillata Thylakoids: Possible Sites of Cation Interaction

1998 ◽  
Vol 53 (9-10) ◽  
pp. 849-856
Author(s):  
Sujata R. Mishra ◽  
Surendra Chandra Sabat
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Electron Donor ◽  
Water Oxidation ◽  
Electron Flow ◽  
Hydrilla Verticillata ◽  
Transport Activity ◽  
Low Salt ◽  
Electron Transport Activity ◽  
Stimulation Of

Stimulatory effect of divalent cations like calcium (Ca2+) and magnesium (Mg2+) was investigated on electron transport activity of divalent cation deficient low-salt suspended (LS) thylakoid preparation from a submerged aquatic angiosperm, Hydrilla verticillata. Both the cations stimulated electron transport activity of LS-suspended thylakoids having an intact water oxidation complex. But in hydroxylamine (NH2OH) - or alkaline Tris - washed thylakoid preparations (with the water oxidation enzyme impaired), only Ca2+ dependent stimulation of electron transport activity was found. The apparent Km of Ca2+ dependent stimulation of electron flow from H2O (endogenous) or from artificial electron donor (exogenous) to dichlorophenol indophenol (acceptor) was found to be identical. Calcium supported stimulation of electron transport activity in NH2OH - or Tris - washed thylakoids was electron donor selective, i.e., Ca2+ ion was only effective in electron flow with diphenylcarbazide but not with NH2OH as electron donor to photosystem II. A magnesium effect was observed in thylakoids having an intact water oxidation complex and the ion became unacceptable in NH2OH - or Tris - washed thylakoids. Indirect experimental evidences have been presented to suggest that Mg2+ interacts with the water oxidation complex, while the Ca2+ interaction is localized betw een Yz and reaction center of photosystem II.

The S2 to S3 transition for water oxidation in PSII (photosystem II), revisited

2018 ◽  
Vol 20 (35) ◽  
pp. 22926-22931 ◽  
Author(s):  
Per E. M. Siegbahn
Keyword(s):  
Photosystem Ii ◽  
Water Oxidation ◽  
Light Flash

The formation of O2 from water requires four transitions, each one after the absorption of one light flash.

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 Simulation of the isotropic EXAFS spectra for the S2 and S3 structures of the oxygen evolving complex in photosystem II

2015 ◽  
Vol 112 (13) ◽  
pp. 3979-3984 ◽  
Author(s):  
Xichen Li ◽  
Per E. M. Siegbahn ◽  
Ulf Ryde
Keyword(s):  
Photosystem Ii ◽  
Water Oxidation ◽  
Density Functional ◽  
Structural Changes ◽  
Complete Agreement ◽  
Oxygen Evolving Complex ◽  
Chemical Modeling ◽  
Oxygen Evolving ◽  
High Degree ◽  
Exafs Spectra

Most of the main features of water oxidation in photosystem II are now well understood, including the mechanism for O–O bond formation. For the intermediate S2 and S3 structures there is also nearly complete agreement between quantum chemical modeling and experiments. Given the present high degree of consensus for these structures, it is of high interest to go back to previous suggestions concerning what happens in the S2–S3 transition. Analyses of extended X-ray adsorption fine structure (EXAFS) experiments have indicated relatively large structural changes in this transition, with changes of distances sometimes larger than 0.3 Å and a change of topology. In contrast, our previous density functional theory (DFT)(B3LYP) calculations on a cluster model showed very small changes, less than 0.1 Å. It is here found that the DFT structures are also consistent with the EXAFS spectra for the S2 and S3 states within normal errors of DFT. The analysis suggests that there are severe problems in interpreting EXAFS spectra for these complicated systems.

Chapter 9. Energy from Photosystem II: Manganese Water Oxidation Catalysts

2011 ◽  
pp. 249-272
Author(s):  
Robin Brimblecombe ◽  
G. Charles Dismukes ◽  
Gerhard F. Swiegers ◽  
Leone Spiccia
Keyword(s):  
Photosystem Ii ◽  
Water Oxidation ◽  
Oxidation Catalysts
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