Anion Effects on the Electron Acceptor Side of Photosystem II in a Transformable Cyanobacterium Synechocystis 6803

1979 ◽

Vol 34 (11) ◽

pp. 1010-1014 ◽

Cited By ~ 32

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.

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Chloroacetates as inhibitors of photosystem II: Effects on electron acceptor side

Journal of Photochemistry and Photobiology B Biology ◽

10.1016/s1011-1344(96)07347-2 ◽

1997 ◽

Vol 37 (1-2) ◽

pp. 107-117 ◽

Cited By ~ 17

Author(s):

Govindjee ◽

Chunhe Xu ◽

Gert Schansker ◽

Jack J.S van Rensen

Keyword(s):

Photosystem Ii ◽

Electron Acceptor ◽

Acceptor Side

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Consequences of structural modifications in cytochrome b559 on the electron acceptor side of Photosystem II

Photosynthesis Research ◽

10.1007/s11120-018-0521-0 ◽

2018 ◽

Vol 139 (1-3) ◽

pp. 475-486

Author(s):

Makoto Nakamura ◽

Alain Boussac ◽

Miwa Sugiura

Keyword(s):

Photosystem Ii ◽

Electron Acceptor ◽

Cytochrome B559 ◽

Structural Modifications ◽

Acceptor Side

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Differential Inhibition and Rephasing of Photosystem II Electron Acceptor Side by Monohalogenated Acetates of Different Hydrophobicity

Zeitschrift für Naturforschung C ◽

10.1515/znc-1992-9-1013 ◽

1992 ◽

Vol 47 (9-10) ◽

pp. 711-716 ◽

Cited By ~ 2

Author(s):

Chunhe Xu ◽

Yong Zhu ◽

Govindjee

Keyword(s):

Photosystem Ii ◽

Partition Coefficient ◽

Reaction Center ◽

Electron Acceptor ◽

Inhibitory Activity ◽

Differential Inhibition ◽

Ps Ii ◽

Acceptor Side ◽

Unusual Effect

We demonstrate here that monohalogenated acetates (MFA , monofluoroacetate; M CA, monochloroacetate; MBA, monobromoacetate) are unique probes of the electron acceptor side of the photosystem II (PS II) reaction center: (1) they differentially inhibit the reoxidation of the reduced primary plastoquinone electron acceptor, QA-, by the secondary plastoquinone electron acceptor QB, and increase the equilibrium [QA-] in the order: MBA ≳ M CA > MFA; and (2) M CA and MBA rephase the PS II electron acceptor side, a rather unusual effect. This results in flash number dependence of [QA-] with maxima at even flashes to change to odd flashes. Furthermore, we demonstrate a correlation between the inhibitory activity of the halogenated acetates with their hydrophobicity (i.e., partition coefficient).

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Cation Effects on the Electron-Acceptor Side of Photosystem II

The Journal of Physical Chemistry B ◽

10.1021/jp513035u ◽

2015 ◽

Vol 119 (24) ◽

pp. 7722-7728 ◽

Cited By ~ 15

Author(s):

Sahr Khan ◽

Jennifer S. Sun ◽

Gary W. Brudvig

Keyword(s):

Photosystem Ii ◽

Electron Acceptor ◽

Cation Effects ◽

Acceptor Side

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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 ◽

10.3390/biom9080371 ◽

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.

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