The Collapse of the Tyrosine Z•−Mn Spin−Spin Interaction above ∼100 K Reveals the Spectrum of Tyrosine Z•. An Application of Rapid-Scan EPR to the Study of Intermediates of the Water Splitting Mechanism of Photosystem II†

Biochemistry ◽  
2007 ◽  
Vol 46 (50) ◽  
pp. 14335-14341 ◽  
Author(s):  
Georgia Zahariou ◽  
Nikolaos Ioannidis ◽  
George Sioros ◽  
Vasili Petrouleas
Keyword(s):  
Photosystem Ii ◽  
Water Splitting ◽  
Spin Interaction ◽  
Rapid Scan ◽  
Tyrosine Z

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 Biogenesis of water splitting by photosystem II during de-etiolation of barley (Hordeum vulgareL.)

2016 ◽  
Vol 39 (7) ◽  
pp. 1524-1536 ◽  
Author(s):  
Dmitriy Shevela ◽  
Janine Arnold ◽  
Veronika Reisinger ◽  
Hans-Martin Berends ◽  
Karol Kmiec ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Water Splitting

scholarly journals How to build a water-splitting machine: structural insights into photosystem II assembly

2020 ◽  
Author(s):  
Jure Zabret ◽  
Stefan Bohn ◽  
Sandra Schuller ◽  
Oliver Arnolds ◽  
Madeline Möller ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Water Splitting ◽  
Conformational Changes ◽  
Binding Pocket ◽  
Heme Iron ◽  
Structural Motif ◽  
Acceptor Side ◽  
Non Heme Iron ◽  
Assembly Intermediate ◽  
Stepwise Assembly

Abstract Biogenesis of photosystem II (PSII), nature’s water splitting catalyst, is assisted by auxiliary proteins that form transient complexes with PSII components to facilitate stepwise assembly events. Using cryo-electron microscopy, we solved the structure of such a PSII assembly intermediate with 2.94 Å resolution. It contains three assembly factors (Psb27, Psb28, Psb34) and provides detailed insights into their molecular function. Binding of Psb28 induces large conformational changes at the PSII acceptor side, which distort the binding pocket of the mobile quinone (QB) and replace bicarbonate with glutamate as a ligand of the non-heme iron, a structural motif found in reaction centers of non-oxygenic photosynthetic bacteria. These results reveal novel mechanisms that protect PSII from damage during biogenesis until water splitting is activated. Our structure further demonstrates how the PSII active site is prepared for the incorporation of the Mn4CaO5 cluster, which performs the unique water splitting reaction.

The EPR Spectrum of Tyrosine Z•and Its Decay Kinetics in O2-Evolving Photosystem II Preparations†

Biochemistry ◽  
2008 ◽  
Vol 47 (24) ◽  
pp. 6292-6300 ◽  
Author(s):  
Nikolaos Ioannidis ◽  
Georgia Zahariou ◽  
Vasili Petrouleas
Keyword(s):  
Photosystem Ii ◽  
Decay Kinetics ◽  
Epr Spectrum ◽  
Tyrosine Z

scholarly journals Mechanism of Water Splitting by Photosystem II

2014 ◽  
Vol 106 (2) ◽  
pp. 27a
Author(s):  
Yulia Pushkar ◽  
Katherine Davis ◽  
Lifen Yan
Keyword(s):  
Photosystem Ii ◽  
Water Splitting

Structure, Electron Transfer Chain of Photosystem II and the Mechanism of Water Splitting

2021 ◽  
pp. 3-38
Author(s):  
Jian-Ren Shen ◽  
Yoshiki Nakajima ◽  
Fusamichi Akita ◽  
Michihiro Suga
Keyword(s):  
Electron Transfer ◽  
Photosystem Ii ◽  
Water Splitting ◽  
Electron Transfer Chain ◽  
Transfer Chain

245 GHz High-Field EPR Study of Tyrosine-D° and Tyrosine-Z° in Mutants of Photosystem II†

Biochemistry ◽  
1996 ◽  
Vol 35 (3) ◽  
pp. 679-684 ◽  
Author(s):  
Sun Un ◽  
Xiao-Song Tang ◽  
Bruce A. Diner
Keyword(s):  
Photosystem Ii ◽  
High Field ◽  
Tyrosine Z ◽  
Tyrosine D

scholarly journals Mediator-assisted water oxidation by the ruthenium “blue dimer” cis,cis-[(bpy)2(H2O)RuORu(OH2)(bpy)2]4+

2008 ◽  
Vol 105 (46) ◽  
pp. 17632-17635 ◽  
Author(s):  
Javier J. Concepcion ◽  
Jonah W. Jurss ◽  
Joseph L. Templeton ◽  
Thomas J. Meyer
Keyword(s):  
Carbon Dioxide ◽  
Electron Transfer ◽  
Renewable Energy ◽  
Photosystem Ii ◽  
Water Splitting ◽  
Water Oxidation ◽  
Oxygenic Photosynthesis ◽  
Reduced Water ◽  
Insight Into ◽  
Recent Insight

Light-driven water oxidation occurs in oxygenic photosynthesis in photosystem II and provides redox equivalents directed to photosystem I, in which carbon dioxide is reduced. Water oxidation is also essential in artificial photosynthesis and solar fuel-forming reactions, such as water splitting into hydrogen and oxygen (2 H2O + 4 hν → O2 + 2 H2) or water reduction of CO2 to methanol (2 H2O + CO2 + 6 hν → CH3OH + 3/2 O2), or hydrocarbons, which could provide clean, renewable energy. The “blue ruthenium dimer,” cis,cis-[(bpy)2(H2O)RuIIIORuIII(OH2)(bpy)2]4+, was the first well characterized molecule to catalyze water oxidation. On the basis of recent insight into the mechanism, we have devised a strategy for enhancing catalytic rates by using kinetically facile electron-transfer mediators. Rate enhancements by factors of up to ≈30 have been obtained, and preliminary electrochemical experiments have demonstrated that mediator-assisted electrocatalytic water oxidation is also attainable.

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