Redox properties and regulatory mechanism of the iron-quinone electron acceptor in photosystem II as revealed by FTIR spectroelectrochemistry

2022 ◽  
Author(s):  
Yuki Kato ◽  
Takumi Noguchi
Keyword(s):  
Photosystem Ii ◽  
Electron Acceptor ◽  
Regulatory Mechanism ◽  
Redox Properties

scholarly journals Structural Changes in the Acceptor Site of Photosystem II upon Ca2+/Sr2+ Exchange in the Mn4CaO5 Cluster Site and the Possible Long-Range Interactions

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 371
Author(s):  
Koua
Keyword(s):  
Crystal Structure ◽  
Photosystem Ii ◽  
Long Range ◽  
Electron Acceptor ◽  
Structural Changes ◽  
Acceptor Site ◽  
Oxygen Evolving Complex ◽  
Long Range Interactions ◽  
Structural Perturbations ◽  
Oxygen Evolving

The Mn4CaO5 cluster site in the oxygen-evolving complex (OEC) of photosystem II (PSII) undergoes structural perturbations, such as those induced by Ca2+/Sr2+ exchanges or Ca/Mn removal. These changes have been known to induce long-range positive shifts (between +30 and +150 mV) in the redox potential of the primary quinone electron acceptor plastoquinone A (QA), which is located 40 Å from the OEC. To further investigate these effects, we reanalyzed the crystal structure of Sr-PSII resolved at 2.1 Å and compared it with the native Ca-PSII resolved at 1.9 Å. Here, we focus on the acceptor site and report the possible long-range interactions between the donor, Mn4Ca(Sr)O5 cluster, and acceptor sites.

Characterization of bonding interactions of the intermediary electron acceptor in the reaction center of Photosystem II by FTIR spectroscopy

1990 ◽  
Vol 1016 (1) ◽  
pp. 49-54 ◽  
Author(s):  
E. Nabedryk ◽  
S. Andrianambinintsoa ◽  
G. Berger ◽  
M. Leonhard ◽  
W. Mäntele ◽  
...  
Keyword(s):  
Photosystem Ii ◽  
Ftir Spectroscopy ◽  
Reaction Center ◽  
Electron Acceptor

Studies about the Mechanism of Herbicidal Interaction with Photosystem II in Isolated Chloroplasts

1979 ◽  
Vol 34 (11) ◽  
pp. 1010-1014 ◽  
Author(s):  
Gernot Renger
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Excitation Energy ◽  
Electron Acceptor ◽  
Functional Organization ◽  
Regulatory Element ◽  
Release Kinetics ◽  
Acceptor Side ◽  
Receptor Sites ◽  
Isolated Chloroplasts

Abstract Based on the functional organization scheme of system-II-electron transport and its modification by different procedures a proteinaceous component enwrapping the redox components (plastoquinone molecules) of the acceptor side (thereby acting as regulatory element) is inferred to be the unique target for herbicidal interaction with system II. This proteinaceous component, which is attacked by trypsin, provides the receptor sites for the herbicides. Studies of the release kinetics in trypsinated chloroplasts of the inhibition of oxygen evolution with K3 [Fe (CN)6] as electron acceptor indicates, that there exists a binding area with different specific subreceptor sites rather than a unique binding site for the various types of inhibitors. Furthermore, trypsination of the proteinaceous component enhances the efficiency of the plastoquinone pool to act as a non-photochemical quencher for excitation energy.

Low-temperature modulation of the redox properties of the acceptor side of photosystem II: photoprotection through reaction centre quenching of excess energy

2003 ◽  
Vol 119 (3) ◽  
pp. 376-383 ◽  
Author(s):  
Alexander G. Ivanov ◽  
Prafullachandra Sane ◽  
Vaughan Hurry ◽  
Marianna Król ◽  
Dimitry Sveshnikov ◽  
...  
Keyword(s):  
Low Temperature ◽  
Photosystem Ii ◽  
Excess Energy ◽  
Redox Properties ◽  
Temperature Modulation ◽  
Reaction Centre ◽  
Acceptor Side
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