EPR-ENDOR of the electronic structure from two nitrogenously ligated bis(.mu.-oxo)-manganese(III)-manganese(IV) model complexes spectroscopically relevant to the multi-manganese center of photosystem II

1991 ◽  
Vol 113 (21) ◽  
pp. 7853-7858 ◽  
Author(s):  
Xiao Ling Tan ◽  
Yilma Gultneh ◽  
Joseph E. Sarneski ◽  
Charles P. Scholes
Keyword(s):  
Electronic Structure ◽  
Photosystem Ii ◽  
Model Complexes ◽  
Iv Model

scholarly journals Rapid Evolution of the Photosystem II Electronic Structure during Water Splitting

2018 ◽  
Vol 8 (4) ◽  
Author(s):  
Katherine M. Davis ◽  
Brendan T. Sullivan ◽  
Mark C. Palenik ◽  
Lifen Yan ◽  
Vatsal Purohit ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Photosystem Ii ◽  
Water Splitting ◽  
Rapid Evolution

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.

Probing the Electronic Structure of the Di-Iron Subsite of [Fe]-Hydrogenase:  A Photoelectron Spectroscopic Study of Fe(I)−Fe(I) Model Complexes

2003 ◽  
Vol 107 (23) ◽  
pp. 4612-4618 ◽  
Author(s):  
Xin Yang ◽  
Mathieu Razavet ◽  
Xue-Bin Wang ◽  
Christopher J. Pickett ◽  
Lai-Sheng Wang
Keyword(s):  
Electronic Structure ◽  
Spectroscopic Study ◽  
Model Complexes

scholarly journals The Basic Properties of the Electronic Structure of the Oxygen-evolving Complex of Photosystem II Are Not Perturbed by Ca2+Removal

2012 ◽  
Vol 287 (29) ◽  
pp. 24721-24733 ◽  
Author(s):  
Thomas Lohmiller ◽  
Nicholas Cox ◽  
Ji-Hu Su ◽  
Johannes Messinger ◽  
Wolfgang Lubitz
Keyword(s):  
Electronic Structure ◽  
Photosystem Ii ◽  
Oxygen Evolving Complex ◽  
Basic Properties ◽  
Oxygen Evolving

Pulsed1H and55Mn ENDOR studies of dinuclear Mn(III)Mn(IV) model complexes

1998 ◽  
Vol 95 (6) ◽  
pp. 1283-1294 ◽  
Author(s):  
DAVID W. RANDALL ◽  
MICHAEL K. CHAN ◽  
WILLIAM H. ARMSTRONG ◽  
R. DAVID BRITT
Keyword(s):  
Model Complexes ◽  
Iv Model
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