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residue potentially involved in facilitating electron transport from pheophytin to QA and/or in binding of Q A, had been replaced by Leu, PS II was undetectable in thylakoids.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.

The Inhibition of Photosynthetic Light Reactions by Halogenated Naphthoquinones

1981 ◽  
Vol 36 (7-8) ◽  
pp. 645-655 ◽  
Author(s):  
Klaus Pfister ◽  
Hartmut K. Lichtenthaler ◽  
Günther Burger ◽  
Hans Musso ◽  
Manuel Zahn
Keyword(s):  
Chlorophyll Fluorescence ◽  
Electron Transport ◽  
Binding Site ◽  
Chlorophyll A ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Ps Ii ◽  
Photosynthetic Electron Flow ◽  
A Site ◽  
Fluorescence Transients

Abstract Halogenated naphthoquinones act as inhibitors of photosynthetic electron flow. I50 concentra­ tion for inhibition of methylviologen reduction were found to range between 2 × 10-5 m to 2 × 10-6 M. Comparing their effects on several partial reactions of electron flow, the inhibition site of the naphthoquinones was found to be at the reducing site of PS II. Studies of fluorescence transients in presence of halogenated naphthoquinones give further evidence for a site action similar to that of diuron and different to that of DBMIB. All naphthoquinones act as quenchers of chlorophyll fluorescence with pure chlorophyll a, and with much higher efficiency in green algae and chloroplasts. It is concluded, that the halogenated naphthoquinones act similar to PS II-inhibitors like diuron, but do not share a common binding site at the PS II-complex. Implications of a possible involvement of phylloquinone K 1 in photosynthetic electron transport are discussed. The synthesis of 2-chloro-as well as 2-bromo-3-isopropyl-1,4-naphthoquinone is described.

Photosystem II Inhibition by Pyran-enamine Derivatives

1993 ◽  
Vol 48 (3-4) ◽  
pp. 163-167
Author(s):  
Koichi Yoneyama ◽  
Yoshihiro Nakajima ◽  
Masaru Ogasawara ◽  
Hitoshi Kuramochi ◽  
Makoto Konnai ◽  
...  
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Thylakoid Membranes ◽  
Major Determinant ◽  
Ps Ii ◽  
Structure Activity Relationships ◽  
Structure Activity

Abstract Through the studies on structure-activity relationships of 5-acyl-3-(1-aminoalkylidene)-4-hydroxy-2 H-pyran-2,6(3 H)-dione derivatives in photosystem II (PS II) inhibition, overall lipophilicity of the molecule was found to be a major determinant for the activity. In the substituted N -benzyl derivatives, not only the lipophilicity but also the electronic and steric characters of the substituents greatly affected the activity. Their mode of PS II inhibition seemed to be similar to that of DCMU , whereas pyran-enamine derivatives needed to be highly lipophilic to block the electron transport in thylakoid membranes, which in turn diminished the permeability through biomembranes.

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.

Mechanism of Action of the Herbicide 4,6-Dinitro-o-cresol in Photosynthesis

1979 ◽  
Vol 34 (11) ◽  
pp. 1021-1023 ◽  
Author(s):  
J. J. S. van Rensen ◽  
J. H. Hobé
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Mechanism Of Action ◽  
Chemical Structure ◽  
Methyl Viologen ◽  
Primary Electron ◽  
Reaction Centers ◽  
Mehler Reaction ◽  
Cyclic Photophosphorylation ◽  
Primary Electron Acceptor

Abstract The herbicide 4,6-dinitro-o-cresol inhibits electron transport to ferricyanide and non-cyclic photophosphorylation for 50% at about 15 μm. At higher concentrations the photosystem I depen­dent Mehler reaction ascorbate/dichlorophenolindophenol to methyl viologen is stimulated, while cyclic photophosphorylation is inhibited. The herbicide thus is an inhibitory uncoupler. Although the chemical structure of 4,6-dinitro-o-cresol is different from that of the diuron-type herbicides, its site and mechanism of action is similar. Both 4,6-dinitro-o-cresol and diuron inhibit electron transport between the primary electron acceptor of Photosystem II and the plastoquinone pool. This causes a closing of the reaction centers of Photosystem II. The interaction with the inhibited molecule however is different for the two herbicides.

Inhibition by Tetranitromethane of Photosynthetic Electron Transport from Water to Photosystem II in Chloroplasts

1980 ◽  
Vol 35 (3-4) ◽  
pp. 293-297 ◽  
Author(s):  
P. V. Sane ◽  
Udo Johanningmeier
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Electron Flow ◽  
Ph Dependence ◽  
Photosynthetic Electron Transport ◽  
Donor Side ◽  
Ps Ii ◽  
Diphenyl Carbazide ◽  
Low Concentrations ◽  
Sh Group

Abstract Low concentrations (10 µM) of tetranitromethane inhibit noncyclic electron transport in spinach chloroplasts. A study of different partial electron transport reactions shows that tetranitromethane primarily interferes with the electron flow from water to PS II. At higher concentrations the oxidation of plastohydroquinone is also inhibited. Because diphenyl carbazide but not Mn2+ ions can donate electrons efficiently to PS II in the presence of tetranitromethane it is suggested that it blocks the donor side of PS II prior to donation of electrons by diphenyl carbazide. The pH dependence of the inhibition by this protein modifying reagent may indicate that a functional-SH group is essential for a protein, which mediates electron transport between the water splitting complex and the reaction center of PS II.

Quantum Yields of Photosystem II Electron Transport and Carbon Dioxide Fixation in C4 Plants

1990 ◽  
Vol 17 (5) ◽  
pp. 579 ◽  
Author(s):  
JP Krall ◽  
GE Edwards
Keyword(s):  
Carbon Dioxide ◽  
Electron Transport ◽  
Quantum Yield ◽  
Photosystem Ii ◽  
Malic Enzyme ◽  
Co2 Fixation ◽  
C4 Plants ◽  
Quantum Yields ◽  
Ps Ii ◽  
Co2 Concentrations

The quantum yields of non-cyclic electron transport from photosystem II (determined from chlorophyll a fluorescence) and carbon dioxide assimilation were measured in vivo in representative species of the three subgroups of C4 plants (NADP-malic enzyme, NAD-malic enzyme and PEP-carboxykinase) over a series of intercellular CO2 concentrations (CI) at both 21% and 2% O2. The CO2 assimilation rate was independent of O2 concentration over the entire range of Ci (up to 500 μbar) in all three C4 subgroups. The quantum yield of PS II electron transport was similar, or only slightly greater, in 21% v. 2% O2 at all Ci values. In contrast, in the C3 species wheat there was a large O2 dependent increase in PS II quantum yield at low CO2, which reflects a high level of photorespiration. In the C4 plants, the relationship of the quantum yield of PS II electron transport to the quantum yield of CO2 fixation is linear suggesting that photochemical use of energy absorbed by PS II is tightly linked to CO2 fixation in C4 plants. This relationship is nearly identical in all three subgroups and may allow estimates of photosynthetic rates of C4 plants based on measurements of PS II photochemical efficiency. The results suggest that in C4 plants both the photoreduction of O2 and photorespiration are low, even at very limiting CO2 concentrations.

Kinetic response of photosystem II photochemistry in the cyanobacterium Spirulina platensis to high salinity is characterized by two distinct phases

1999 ◽  
Vol 26 (3) ◽  
pp. 283 ◽  
Author(s):  
Congming Lu ◽  
Giuseppe Torzillo ◽  
Avigad Vonshak
Keyword(s):  
Electron Transport ◽  
Quantum Yield ◽  
Photosystem Ii ◽  
Spirulina Platensis ◽  
High Salinity ◽  
Photochemical Quenching ◽  
Second Phase ◽  
Ps Ii ◽  
Reaction Centres ◽  
Two Phases

The kinetic response of photosystem II (PS II) photochemistry in Spirulina platensis(Norstedt M2 ) to high salinity (0.75 M NaCl) was found to consist of two phases. The first phase, which was independent of light, was characterized by a rapid decrease (15–50%) in the maximal efficiency of PS II photochemistry (Fv /Fm), the efficiency of excitation energy capture by open PS II reaction centres (Fv′/Fm′), photochemical quenching (qp) and the quantum yield of PS II electron transport (Φ PS II) in the first 15 min, followed by a recovery up to about 80–92% of their initial levels within the next 2 h. The second phase took place after 4 h, in which further decline in above parameters occurred. Such a decline occurred only when the cells were incubated in the light, reaching levels as low as 45–70% of their initial levels after 12 h. At the same time, non-photochemical quenching (qN) and Q B -non-reducing PS II reaction centres increased significantly in the first 15 min and then recovered to the initial level during the first phase but increased again in the light in the second phase. The changes in the probability of electron transfer beyond QA (ψo) and the yield of electron transport beyond QA (φ Eo), the absorption flux (ABS/RC) and the trapping flux (TRo /RC) per PS II reaction centre also displayed two different phases. The causes responsible for the decreased quantum yield of PS II electron transport during the two phases are discussed.

Photoreduction of NADP+ in Photosystem II of Higher Plants: Requirement for Manganese

1992 ◽  
Vol 47 (1-2) ◽  
pp. 57-62 ◽  
Author(s):  
Suleyman I. Allakhverdiev ◽  
Vyacheslav V. Klimov
Keyword(s):  
Photosystem Ii ◽  
Higher Plants ◽  
Complete Removal ◽  
Reaction Centers ◽  
Higher Plant ◽  
Ps Ii ◽  
Alternate Pathway ◽  
Manganese Extraction ◽  
Quinone Acceptor ◽  
Reduced State

Abstract The effects of reversible manganese extraction on NADP+ photoreduction were studied with higher plant subchloroplast preparations of photosystem II (PS II). Under anaerobic conditions, when the reaction centers (RCs) of PS II are “closed” (i.e. in the state [P680 Pheo] QA), and in the presence of ferredoxin-ferredoxin-NADP+ reductase, NADP+ reduction is observed at a rate of 0.8 -1.1 nmol/mg × chlorophyll × h. After complete removal of manganese from PS II, the rate of NADP+ reduction is reduced 40 - 50-fold. Upon the addition of Mn at a concentration of approx. 4 Mn atoms per reaction center, the NADP+ reduction is restored up to 85 -90% of the initial value. When half of this amount of Mn is combined with about 40 times of the equivalent concentration of other divalent ions (Ca2+, Sr2+, Mg2+ etc.) the reaction is also reactivated. Dinoseb (10-6 m) an inhibitor of electron transfer in PS II prevents NADP+ photoreduction. It is concluded that under conditions when the first quinone acceptor, QA, is in its reduced state (QA-) electrons are transferred from reduced pheophytin (Pheo·̅) to NADP+, indicating that PS II can reduce NADP+ without the participation of PS I. On the basis of these and literature data, an alternate pathway for electron phototransfer in PS II reaction centers of higher plants is suggested. Some problems concerning the Z-scheme are discussed.

Involvement of the Xanthophyll Cycle in Regulation of Cyclic Electron Flow around Photosystem II

1996 ◽  
Vol 51 (1-2) ◽  
pp. 47-52 ◽  
Author(s):  
W. I. Gruszecki ◽  
K. Strzałk ◽  
K.P. Bader ◽  
A. Radunz ◽  
G.H. Schmid
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Oxygen Evolution ◽  
Xanthophyll Cycle ◽  
Electron Flow ◽  
Photosynthetic Apparatus ◽  
Photosynthetic Oxygen Evolution ◽  
Cyclic Electron Transport ◽  
Ps Ii ◽  
Low Levels

Abstract In our previous study (Gruszecki et al., 1995) we have postulated that the mechanism of cyclic electron transport around photosystem II, active under overexcitation of the photosynthetic apparatus by light is under control of the xanthophyll cycle. The combination of dif­ferent light quality and thylakoids having various levels of xanthophyll cycle pigments were applied to support this hypothesis. In the present work photosynthetic oxygen evolution from isolated tobacco chloroplasts was measured by means of mass spectrometry under conditions of high or low levels of violaxanthin, being transformed to zeaxanthin during dark incubation in an ascorbate containing buffer at pH 5.7. Analysis of oxygen evolution and of light-induced oxygen uptake indicate that the de-epoxidation of violaxanthin to zeaxanthin results in an increased cyclic electron transport around PS II, thus dimishing the vectorial electron flow from water. An effect similar to de-epoxidation was observed after incubation of thylakoid membranes with specific antibodies against violaxanthin.

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