Iron-Blocking the High-Affinity Mn-Binding Site in Photosystem II Facilitates Identification of the Type of Hydrogen Bond Participating in Proton-Coupled Electron Transport via YZ•†

Biochemistry ◽  
2005 ◽  
Vol 44 (28) ◽  
pp. 9746-9757 ◽  
Author(s):  
Boris K. Semin ◽  
Elena R. Lovyagina ◽  
Kirill N. Timofeev ◽  
Ilya I. Ivanov ◽  
Andrei B. Rubin ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Electron Transport ◽  
Photosystem Ii ◽  
Binding Site ◽  
High Affinity

X-Ray Structure Analysis of a Cyanoacrylate Inhibitor of Photosystem II Electron Transport

1991 ◽  
Vol 46 (1-2) ◽  
pp. 93-98 ◽  
Author(s):  
Helen G. McFadden ◽  
Donald C. Craig ◽  
John L. Huppatz ◽  
John N. Phillips
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Chlorophyll Concentration ◽  
Photosynthetic Electron Transport ◽  
Hill Reaction ◽  
Ps Ii ◽  
X Ray ◽  
High Affinity ◽  
Modelling Studies ◽  
Intramolecular Hydrogen

Abstract X-ray crystallographic data for the highly potent cyanoacrylate photosynthetic electron transport inhibitor, (Z)-ethoxyethyl 3-(4-chlorobenzylamino)-2-cyano-4-methylpent-2-enoate, are presented. This compound has a particularly high affinity for the photosystem II (PS II) herbicide receptor with a p I50 value of 9.5 (in the Hill reaction under uncoupled condi­tions with a chlorophyll concentration of 0.1 μg/ml). Data regarding the structure of small li­gands, such as this potent cyanoacrylate, which bind to the site with high affinity may be used to provide the basis for modelling studies of PS II/herbicide complexes. The X-ray data presented confirm the Z-stereochemistry of active cyanoacrylates and demonstrate the pres­ence of a planar core stabilized by an intramolecular hydrogen bond between the ester car­bonyl oxygen and a benzylamino hydrogen atom. In order to assess the importance of the benzylamino -NH -group in this type of cyanoacrylate, analogues containing a methylene group in its place were synthesized and found to be 100-and 1000-fold less active as Hill inhibitors.

Molecular Modelling of the Interaction between DCMU and the QB-Binding Site of Photosystem II

1993 ◽  
Vol 48 (3-4) ◽  
pp. 191-198 ◽  
Author(s):  
Simon P. Mackay ◽  
Patrick J. O ’Malley
Keyword(s):  
Hydrogen Bond ◽  
Photosystem Ii ◽  
Binding Site ◽  
Binding Sites ◽  
The Other ◽  
Reaction Centre ◽  
Protein Model ◽  
Intermolecular Energy ◽  
Herbicide Binding ◽  
Binding Orientations

Abstract The prefered binding orientations for the herbicide DCMU within the QB-binding site of the D 1 protein model from a photosystem II reaction centre have been determined. Calculation of the intermolecular energy between the herbicide and the binding site has been instrumental in obtaining optimum positions reinforced by experimental results from mutation studies and herbicide binding to analogous bacterial reaction centres. We have shown that two binding sites are possible, one involving a hydrogen bond to and the other to the Ser 264 residue. In both cases, which are more important for the stabilization of the interactions.

High-and Low-Affinity Binding of Photosystem II Herbicides to Isolated Thylakoid Membranes and Intact Algal Cells

1982 ◽  
Vol 37 (7-8) ◽  
pp. 620-631 ◽  
Author(s):  
Henrik Laasch ◽  
Klaus Pfister ◽  
Wolfgang Urbach
Keyword(s):  
Photosystem Ii ◽  
Binding Site ◽  
Spinacia Oleracea ◽  
Specific Binding ◽  
Affinity Binding ◽  
Concentration Effects ◽  
Intact Cells ◽  
High Affinity Binding ◽  
High Affinity ◽  
Receptor Sites

Abstract High- and low-affinity binding of photosystem II herbicides to isolated thylakoids of Spinacia oleracea and to intact cells of the unicellular green alga Ankistrodesmus braunii were investigated. Complete mutual displacement of bound diuron-type herbicides (e.g. diuron, atrazine, terbutryn) by either diuron- or phenol-type herbicides (e.g. ioxynil, dinoseb) in thylakoids as well as in intact algal cells was found for herbicide concentrations (< 4 nmol bound herbicide/mg Chl) which gave almost saturated high-affinity binding. This demonstrates a high degree of specific binding of these herbicides towards their receptor sites even in intact algal cells. In contrast, phenol-type herbicides are largely unspecifically bound in algal cells. The mechanism of binding of all photosystem II herbicides at the high-affinity (specific) binding site was found to be competitive. Within the group of diuron-type and of phenol-type herbicides as well as between these two groups, graphical and quantitative analysis of the Lineweaver- Burk plot and of the Dixon plot indicated competitive binding. From this a common binding site for both types of herbicides was concluded. The involvement of two different herbicide binding- proteins is discussed. Low-affinity (unspecific) binding was found to be irreversible in contrast to the easily reversible high-affinity binding. Irreversibility was indicated by a lack of displacement. It is proposed that low-affinity binding represents either a partitioning of the herbicides into the lipophilic parts of the membranes or an attachment to distinct receptor sites. Unspecifically bound herbicides might be responsible for several high concentration effects of the photosystem II herbicides, which are described in the literature. Evidences for the possible existence of a second binding site of these herbicides are presented.

Photoassembly of the Manganese Cluster in Mutants Perturbed in the High Affinity Mn-Binding Site of the H2O-Oxidation Complex of Photosystem II†

Biochemistry ◽  
2007 ◽  
Vol 46 (47) ◽  
pp. 13648-13657 ◽  
Author(s):  
Hong Jin Hwang ◽  
Aaron McLain ◽  
Richard J. Debus ◽  
Robert L. Burnap
Keyword(s):  
Photosystem Ii ◽  
Binding Site ◽  
Manganese Cluster ◽  
High Affinity

Q a Binding to D2 Contributes to the Functional and Structural Integrity of Photosystem II

1990 ◽  
Vol 45 (5) ◽  
pp. 359-365 ◽  
Author(s):  
Wim Vermaas ◽  
Jeroen Charité ◽  
Gaozhong Shen
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Binding Site ◽  
Structural Integrity ◽  
Reaction Centers ◽  
Ps Ii ◽  
Directed Mutation ◽  
Rapid Inactivation ◽  
Reaction Center Complex ◽  
A Site

Two D2 mutants were created with a site-directed mutation near the presumable binding site of QA. In one of the mutants, in which Trp-253, the aromatic residue potentially involved in facilitating electron transport from pheophytin to QA and/or in binding of Q A, had been replaced by Leu, PS II was undetectable in thylakoids. This mutant is an obligate photoheterotroph. In another mutant the Gly-215 residue, located next to the His residue that is proposed to bind QA and Fe2+, was mutated to Trp. This mutation leads to a rapid inactivation of oxygen evolution capacity in the light, and to a virtual elimination of the potential to grow photoautotrophically, but does not greatly affect the number of photosystem II reaction centers on a chlorophyll basis. We propose that proper binding of QA to the photosystem II reaction center complex is a prerequisite for stability of the photosystem II complex. Impairment of Q a binding leads to rapid inactivation of photosystem II, which may be followed by a structural disintegration of the complex.

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