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'Photosystem II' in keywords Facet   Publication Year 1993  [X]
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1993[X]
1Author    Ichiro Honda, Makoto Sibagaki, Koichi Yoneyama, Yoshihiro Nakajima, Makoto Konnai, Nobutaka Takahashi, Shigeo YoshidaRequires cookie*
 Title    Photosystem II Inhibition by Phloroglucinol Derivatives Having Both Phenol and Urea Functionalities  
 Abstract    Esters o f 3-nitrophloroglucinecarboxylic acid were found to be active photosystem II (PS II) inhibitors, as were the amides, indicating that, in their structures, the substituted phlorogluci­ nol nuclei themselves plays a major roles in PS II inhibition. A m ong the phenylureidoalkyl esters tested, 3,4-dichlorophenylurea com pound having two amino hydrogen atom s showed high activities. Optimal activity was associated with compounds in which the oxygen atom and the urea structure in the ester side chain were connected via an ethylene group. 
  Reference    Z. Naturforsch. 48c, 159 (1993); received November 3 1992 
  Published    1993 
  Keywords    Photosystem II, Electron Transport Inhibition, Phloroglucinol Derivatives 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0159.pdf 
 Identifier    ZNC-1993-48c-0159 
 Volume    48 
2Author    Koichi Yoneyama, Yoshihiro Nakajima, Masaru Ogasawara, Hitoshi Kuramochi, Makoto Konnai, Hajime Iwamura, Fumihiko Sato, Katsunori Ichinose, Tadao Asami, Nobutaka Takahashi, Shigeo YoshidaRequires cookie*
 Title    Photosystem II Inhibition by Pyran-enamine Derivatives  
 Abstract    Through the studies on structure-activity relationships o f 5-acyl-3-(l-am inoalkylidene)-4-hydroxy-2 H-pyran-2,6(3 H)-dione derivatives in photosystem II (PS II) inhibition, overall lipophilicity o f the m olecule was found to be a major determinant for the activity. In the sub­ stituted N -benzyl derivatives, not only the lipophilicity but also the electronic and steric char­ acters o f the substituents greatly affected the activity. Their mode o f PS II inhibition seemed to be similar to that o f D C M U , whereas pyran-enamine derivatives needed to be highly lipophilic to block the electron transport in thylakoid membranes, which in turn diminished the permea­ bility through biomembranes. 
  Reference    Z. Naturforsch. 48c, 163 (1993); received November 3 1992 
  Published    1993 
  Keywords    Photosystem II, Electron Transport Inhibition, Pyran-enamine Derivatives 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0163.pdf 
 Identifier    ZNC-1993-48c-0163 
 Volume    48 
3Author    H. Adar Kless3, Michal Oren-Shamirb, ItzhakO. Hadc, M. Arvin Edelm, Wim VermaasaRequires cookie*
 Title    Protein Modifications in the D 2 Protein of Photosystem II Affect Properties of the Q B/Herbicide-Binding Environment  
 Abstract    The D 2 protein contains an extended loop (the D-de loop) between helices D and de at the reducing side o f photosystem II (PS II). Characterization o f D 2 mutants o f the cyanobacte­ rium Synechocystis sp. PCC 6803 has indicated that the length and amino acid com position o f the D-de loop are not critical for basic PS II functions, although most o f the residues in that region are conserved phylogenetically. Here we show using herbicide binding and electron-flow inhibition measurements that drastic modifications in the D-de loop o f the D 2 protein modify the interaction o f some PS II-directed herbicides with their binding niche. The stability o f (semi-)reduced Q B in its binding pocket is altered in at least two o f the mutants, as indicated by a shifted peak temperature o f the thermoluminescence signal originating from charge recombi­ nation involving QB. These results suggest a close functional association between the D-de loop o f the D 2 protein and the Q B/herbicide-binding environment, which is viewed as being coordinated mostly by re­ sidues o f the D 1 protein. This represents one o f the first examples o f m odification o f the Q B/ herbicide-binding domain by mutations in the D 2 protein. 
  Reference    Z. Naturforsch. 48c, 185—190 (1993); received November 23 1992 
  Published    1993 
  Keywords    Herbicides, Plastoquinone, Photosystem II, Thermoluminescence, Cyanobacteria 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0185.pdf 
 Identifier    ZNC-1993-48c-0185 
 Volume    48 
4Author    V. Ictor, B. Curw, G. Ert, S. Chan Sk Er, O. Scar, J. De, V. Os, J. S. Van RensenRequires cookie*
 Title    Comparison of Photosynthetic Activities in Triazine-Resistant and Susceptible Biotypes of Chenopodium album  
 Abstract    Triazine-resistant and susceptible Chenopodium album plants were grown at low and at high light irradiances. A t the lower light irradiance the dry m atter production of the resistant and the susceptible plants were almost similar. At the higher irradiance the resistant biotype had a significantly lower production. Fluorescence studies showed that the photochemical yield and the photosystem II electron transport rate were lower in the resistant biotype. It could be demonstrated in intact leaves that the lower productivity of the resistant biotype is caused by a higher sensitivity to photoinhibition. However, when studying effects of photoinhibition on electron flow and photophosphorylation in isolated thylakoids o f the two biotypes, no signifi­ cant differences between resistant and susceptible plant materials were observed. It is suggest­ ed that the difference between resistant and susceptible biotypes connected with processes pro­ tective against photoinhibition in intact leaves, are lost during the isolation of thylakoids. 
  Reference    Z. Naturforsch. 48c, 278 (1993); received November 26 1992 
  Published    1993 
  Keywords    Chloroplasts, Triazine-Resistance, Photosystem II, Photoinhibition, Fluorescence 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0278.pdf 
 Identifier    ZNC-1993-48c-0278 
 Volume    48 
5Author    U. Hegde, S. Padhye, L. Kovács, A. Vozár, S. DemeterRequires cookie*
 Title    Modification of Histidine Residues of Photosystem II by Diethyl Pyrocarbonate Inhibits the Electron Transfer between the Primary (QA) and Secondary (QB) Quinone Acceptors  
 Abstract    The effect o f diethyl pyrocarbonate (D EPC) on the photosynthetic electron transport was investigated in isolated spinach thylakoids by partial electron transport rate and thermolumi­ nescence measurements. Incubation o f thylakoids at pH 6.5 with 5 mM DEPC for 15 min re­ sulted in a considerable inhibition o f electron transport from water to dichlorophenolindo-phenol. The inhibition was only partially releaved by addition o f the donor, diphenylcarbazide indicating the effect o f DEPC both on the donor and acceptor sides o f PS II. In the thermolu­ minescence glow curve DEPC-treatm ent abolished the B band (S2Q B~ radiative charge recom ­ bination) at 30 °C with a concom itant appearance o f the Q band (S2QA~ charge recombina­ tion) at 10 °C. This suggests that in isolated thylakoids possessing an active water-splitting sys­ tem DEPC affects the electron transfer from QA to QB but does not inhibit the electron transport from manganese to QA during the S t—>S2 transition o f the water-splitting system. At the acceptor side o f PS II the targets o f DEPC are probably the histidines which are coordinat­ ed to the non-hem e iron. Illumination o f thylakoids at -8 0 °C following DEPC addition after two preflashes at 5 °C resulted in the replacement o f the A (A T) thermoluminescence band at -3 0 °C with a band appearing at -1 5 °C. This observation can be explained by the effect o f DEPC on a donor side histidine com ponent participating in the generation o f the A (A T) band. Consequently, in the interpretation o f results obtained by DEPC treatment o f PS II, both the donor and acceptor side effects o f DEPC should be considered. 
  Reference    Z. Naturforsch. 48c, 896—9 (1993); received May 4/September 6 1993 
  Published    1993 
  Keywords    Diethyl Pyrocarbonate, Histidine, Photosynthesis, Photosystem II, Thermoluminescence 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0896.pdf 
 Identifier    ZNC-1993-48c-0896 
 Volume    48 
6Author    Hiroyuki Koike, Yasuhiro Kashino, Kazuhiko SatohRequires cookie*
 Title    Interactions of Halogenated Benzoquinones with the Non-Heme Iron (Q40o) in Photosystem II  
 Abstract    Interactions o f halogenated benzoquinones with the acceptor side o f Photosystem (PS) II were studied by measuring fluorescence induction curves and flash-induced absorbance changes in PS II particles isolated from Synechococcus vulcanus. Following results were ob­ tained: 1) Addition o f some halogenated benzoquinones prior to 3-(3,4-dichlorophenyl)-l,l-dimethylurea (D C M U) in the dark increased the area above the fluorescence induction curve (work integral) by a factor o f two. 2) Based on the ability to increase the fluorescence work integral, halogenated benzoquinones could be divided into two groups. 3) 2,6-D ichlorobenzo-quinone (2,6-D C BQ), trichlorobenzoquinone (TCBQ) and tetrahalogenated benzoquinones except tetrafluorobenzoquinone (fluoranil) (group A) increased the work integral, but 2,5-D CBQ and fluoranil (group B) did not. 4) Rapid reoxidation o f QA was observed in the presence o f quinones which belong to group A. These results were interpreted in terms o f dark oxidation o f by quinones belonging to group A. Possible mechanisms o f oxidation o f Q400 by these quinones in the dark are discussed. 
  Reference    Z. Naturforsch. 48c, 168 (1993); received Novem ber 9 1992 
  Published    1993 
  Keywords    Photosystem II, Q400, Halogenated Benzoquinone, Q B-Site, Fluorescence Induction 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0168.pdf 
 Identifier    ZNC-1993-48c-0168 
 Volume    48 
7Author    Kazuhiko Satoh, Yasuhiro Kashino, Hiroyuki KoikeRequires cookie*
 Title    Electron Transport from QA to Thymoquinone in a Synechococcus Oxygen-Evolving Photosystem II Preparation: Role of QB and Binding Affinity of Thymoquinone to the QB Site  
 Abstract    We have recently shown that binding affinities o f benzoquinones can be estimated by two methods in photosystem (PS) II particles (K. Satoh et al., Biochim. Biophys. Acta 1 1 0 2 ,4 5 -5 2 (1992)). U sing these methods we calculated the binding affinity o f thym oquinone (2-methyl-5-isopropyl-/?-benzoquinone) to the Q B site and studied how the quinone accepts electrons in oxygen-evolving PS II particles isolated from the thermophilic cyanobacteria, Synechococcus elongatus and S. vulcanus. The results are as follows: (1) The binding constant o f thym oqui­ none to the Q B site determined by several methods was around 0.33 m M . (2) At low thym oqui­ none concentrations the quinone was supposed to accept electrons via QB-plastoquinone, whereas at high concentrations the quinone seemed to bind to the QB site and accept an elec­ tron directly from Q~A. Lower rates o f photoreduction o f the quinone at high concentrations were attributed to a slower turnover rate o f the quinone at the QB site than that o f endogenous plastoquinone. (3) A model for the function o f plastoquinone at the Q B site, which can explain all the results, was presented. According to this model, the plastoquinone molecule at the Q B site is not replaced by another plastoquinone molecule. Instead, it transfers electrons to pool plastoquinone molecules by turning over its head group but remaining its long side chain bound to the PS II complexes. 
  Reference    Z. Naturforsch. 48c, 174 (1993); received November 9 1992 
  Published    1993 
  Keywords    Q b Site, Photosystem II, Thym oquinone, Plastoquinone, Synechococcus 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0174.pdf 
 Identifier    ZNC-1993-48c-0174 
 Volume    48 
8Author    Sophie Creuzet, TeresaM. Iranda, Jean-M Arc DucruetRequires cookie*
 Title    Comparison of Experimental and Calculated Hydrogen Bonding Properties of Some Urea and Triazine Inhibitors of Photosystem II  
 Abstract    Previous studies o f structure/activity relationships o f photosystem II inhibitors, including com parisons o f their inhibitory power in herbicide-resistant and susceptible chloroplasts, have led to predict the role o f hydrogen bonding, associated to hydrophobicity, in the binding onto the Qb site. The crystallographic structures o f bacterial reaction centers now allow these bonds to be identified. In order to be able to understand the binding o f various herbicides and the effects o f resistance mutations within the Q B site, a reliable estimation o f hydrogen bonding strengths is needed. We show here, by calculating interactions with model com pounds, con ­ trolled by physicochemical measurements, that the hydrogen bonding properties o f the C = X nucleophilic moiety present in most PS II inhibitors are different for triazines as compared to urea or amide derivatives. Semiempirical methods (AM 1) fail to reproduce the energies o f hy­ drogen bonds between a triazine ring nitrogen and a phenolic proton. An empirical method (SI BFA), designed to reproduce interaction energies, has been adapted with the aim o f calculat­ ing the binding energies o f various herbicides with models o f the Q B site. 
  Reference    Z. Naturforsch. 48c, 179 (1993); received November 12 1992 
  Published    1993 
  Keywords    Herbicide, Herbicide Resistance, Hydrogen Bonding, M olecular Calculation, Photosystem II 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0179.pdf 
 Identifier    ZNC-1993-48c-0179 
 Volume    48 
9Author    V. A. Boichenko, V. V. Klimovb, S. R. Mayes3, J. Barber1, T. Echnology, M. Edicine, London Sw, A. Y., U. K.Requires cookie*
 Title    Characterization of the Light-Induced Oxygen Gas Exchange from the IC 2 Deletion Mutant of Synechocystis PCC 6803 Lacking the Photosystem II 33 kDa Extrinsic Protein  
 Abstract    The absence o f the extrinsic M n-stabilizing 33 kD a protein in the IC 2 mutant o f Synecho­ cystis PCC 6803 disturbs the redox cycling o f the water splitting system and retards the formation o f its higher S-states (I. Vass, K.. We have performed analyses o f the flash-induced oxygen exchange in the mutated cyanobacterium to clarify further the role o f the 33 kD a protein. Under aerobic conditions, both the wild type and IC2 mutant show a relative­ ly slow signal o f oxygen rise on the first flash which is increased about twice by the addition o f 10 (aM D C M U and significantly diminished by lowering the oxygen concentration in the medi­ um. According to action spectra measurements, this m ode o f apparent oxygen release is me­ diated by PS I and can be attributed to a light induced inhibition o f respiratory activity. In contrast to the wild type, having the usual oxygen evolution flash pattern with a periodicity o f four, the IC2 mutant shows a binary oscillation pattern o f flash-induced respiratory oxygen exchange at a flash frequency 10 Hz, being dampened with D C M U or by a lower flash fre­ quency (< 1 Hz). Oxygen evolution due to water splitting is clearly seen in the IC2 mutant when background far-red illumination is applied to saturate the signal due to respiratory inhi­ bition, but a quadruple oscillatory com ponent o f flash-induced oxygen evolution appears only in the presence o f artificial electron acceptors under partial aerobic conditions. The mutant possesses a higher PS I/PS II ratio compared to the wild type, as judged from both the flash-induced yields and quantum efficiencies o f the steady-state rates o f the oxygen exchange reac­ tions. Estimates o f antenna sizes indicate about a 20% decrease o f optical cross-section at 675 nm o f the PS II unit in IC 2 mutants in comparison with the wild type. It is suggested that the absence o f the 33 kDa protein leads to a m odification o f the PS II assembly and because o f the slowing down o f the S-state cycle, the rate o f cyclic electron flow around PS II is enhanced. It seems that the absence o f the 33 kD a protein in Synechocystis 6803 also disturbs energy transfer between adjacent PS II core complexes and may also alter their association with the phycobilisomes. 
  Reference    Z. Naturforsch. 48c, 224—201 (1993); received December 10 1992 
  Published    1993 
  Keywords    Photosystem II, Oxygen Evolution, 33 kD a Protein, Synechocystis, Mutants 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0224.pdf 
 Identifier    ZNC-1993-48c-0224 
 Volume    48 
10Author    G. Renger, H. M. Gleiter, E. Haag, F. ReifarthRequires cookie*
 Title    Photosystem II: Thermodynamics and Kinetics of Electron Transport from Qa" to Q b(Q b' ) and Deleterious Effects of Copper(II)  
 Abstract    Studies on thermodynamics and kinetics o f electron transfer from QA~ to QB(QB") were per­ formed by m onitoring laser flash induced changes o f the relative fluorescence emission as a function o f temperature (220 K < T < 310 K) in isolated thylakoids and PS II membrane frag­ ments. In addition, effects o f bivalent metal ions on PS II were investigated by measuring conven­ tional fluorescence induction curves, oxygen evolution, manganese content and atrazine bind­ ing mostly in PS II membrane fragments. It was found: a) the normalized level o f the fluores­ cence remaining 10 s after the actinic flash (FJF0) steeply increases at temperatures below -1 0 to -2 0 °C, b) the fast phase o f the transient fluorescence change becomes markedly retard­ ed with decreasing temperatures, c) am ong different cations (Cu2+, Zn2+, Cd2+, N i2+, Co2+) only Cu2+ exhibits marked effects in the concentration range below 100 jim and d) Cu2+ decreases the normalized variable fluorescence, inhibits oxygen evolution and diminishes the affinity to atrazine binding without affecting the number o f binding sites. The content o f about four manganeses per functionally competent oxygen evolving complex is not changed by [Cu2+] < 70 |iM. Based on these findings it is concluded: i) a temperature dependent equilibrium between an inactive (I) and active (A) state o f QA~ reoxidation by Q b(Qb) is characterized by standard 
  Reference    Z. Naturforsch. 48c, 234 (1993); received November 23 1992 
  Published    1993 
  Keywords    Photosystem II, Q B-Site, Copper(II) Effects, Fluorescence, Oxygen Evolution 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0234.pdf 
 Identifier    ZNC-1993-48c-0234 
 Volume    48 
11Author    J. SymRequires cookie*
 Title    The Role of D 1* in Light-Induced D 1 Protein Turnover in Leaves  
 Abstract    ea, H arald R . B olh à r-N ord en kam pfb, and C hrista C ritch ley3 Light-induced degradation o f the D 1 protein of photosystem II (PS II) was determined by radioactive pulse-chase labelling experiments in intact leaves o f Schefflera polybotrya. PS II photochemical efficiency was monitored by measuring chlorophyll fluorescence. A significant and consistent decline in the F J F m ratio was taken to indicate photoinhibition. The formation and degradation o f a modified form o f the D 1 protein, D 1*, was different under photoinhibi-tory or non-photoinhibitory light conditions. At photoinhibitory irradiance greater amounts o f D 1 * were formed relative to D 1, and the degradation of D 1* was slower when compared with non-photoinhibitory irradiance. The formation and degradation o f D 1* were therefore shown to be at least partly light intensity dependent. Higher light intensities appeared to slow D 1* degradation, which suggests a modification in PS II turnover properties. 
  Reference    Z. Naturforsch. 48c, 246 (1993); received December 12 1992 
  Published    1993 
  Keywords    Photosynthesis, Photosystem II, Photoinhibition, D 1 Degradation, Chlorophyll Fluorescence 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0246.pdf 
 Identifier    ZNC-1993-48c-0246 
 Volume    48 
12Author    SimonP M Ackay, PatrickJ. O 'malleyRequires cookie*
 Title    Molecular Modelling of the Interactions between Optically Active Triazine Herbicides and Photosystem II  
 Abstract    The Q b binding site o f photosystem II in green plants displays stereoselectivity for the (S') stereoisomer o f the a-m ethylbenzyl derivative o f atrazine but not for derivatives with smaller substituents such as sec-butyl. We have shown that interactive models reflect the experimental data by determining the intermolecular energies between the D 1 protein binding region (resi­ dues Leu 210 to Val 280) and the triazine analogs. The intermolecular energy was calculated by van der W aals and electrostatic interactions after energy minimization o f the combined structures to reduce inter and intramolecular strain. On the basis o f these assumptions the role o f stereoselectivity for optically active triazines was site responsible such stereoselectivity was identified. 
  Reference    Z. Naturforsch. 48c, 474 (1993); received January 13/February 16 1993 
  Published    1993 
  Keywords    Atrazine, Electrostatic Interactions, Intermolecular Energy, Molecular M odelling, Photosystem II 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0474.pdf 
 Identifier    ZNC-1993-48c-0474 
 Volume    48 
13Author    KlausG. Tietjen, Wilfried Draber, John Goossens, JohannesR. Jansen, JoachimF. Kluth, Michael Schindler, Heinz-Jürgen, Wroblowsky Bayer, A. G.Requires cookie*
 Title    Binding of Triazines and Triazinones in the QB-Binding Niche of Photosystem II  
 Abstract    A series o f 20 triazines (derivatives o f 2-alkylam ino-4-benzylam ino-6-chloro-l,3,5-triazines) and 37 triazinones (derivatives o f 3-alkyl-4-am ino-6-phenyl-l,2,4-triazin-5-ones) is tested for inhibitory potency in photosynthetic electron flow through photosystem II o f wild type Chla-mydomonas reinhardtii and o f five mutants with aminoacid substitutions in the D 1 protein at valine 219, alanine 251, phenylalanine 255, serine 264, and leucine 275. The data are used for computer modelling o f .the possible location o f the com pounds within a three dimensional model o f the QB-binding niche o f the D 1 protein. 
  Reference    Z. Naturforsch. 48c, 205 (1993); received November 23 1992 
  Published    1993 
  Keywords    D 1 Protein, Herbicides, Molecular M odeling, Photosystem II, Q B-Binding Niche 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0205.pdf 
 Identifier    ZNC-1993-48c-0205 
 Volume    48 
14Author    Z. NaturforschRequires cookie*
 Title    Kinetics of Electron Transfer between Q A and Q B in Wild Type and Herbicide-Resistant Mutants of Chlamydomonas reinhardtii  
 Abstract    A n ton y R . C ro fts*, Irene B aroli, D avid K ra m e r, and Shinichi T a o k a Biophysics Division and *D epartm ent o f M icrobiology, University o f Illinois at U rbana-Cham paign, U rb ana, We have investigated the electron transfer kinetics for reduction o f plastoquinone by photo­ system II in six m utant strains o f Chlamydomonas reinhardtii by following the decay o f the high fluorescence state after flash activation, and com pared the separate reactions of the two-electron gate with those o f a wild type strain. By analysis o f the electron transfer kinetics, and separate measurement o f the equilibrium constant for stabilization o f the bound semiquinone after one flash, we have been able to deconvolute the contributions o f rate constants and equi­ librium constants for plastoquinone binding and electron transfer to the overall process. Two mutations, S 264 A and A 251 V, led to a marked slowing o f kinetics for reduction of plastoqui­ none to the bound semiquinone. In S 2 6 4 A , the second electron transfer was also slower, but was normal in A 2 5 1 V. In m utant G 2 5 6 D , the electron transfer kinetics were normal after the first flash, but slowed after the second. In mutants L 2 5 7 F , V 2 1 9 I, and F 2 5 5 Y , the electron transfer kinetics after both flashes were similar to those in wild type. We discuss the results in terms of a model which provides a description o f the mechanism o f the two-electron gate in terms of measured kinetic and equilibrium constants, and we give values for these parameters in all strains tested. 
  Reference    Z. Naturforsch. 48c, 259 (1993); received December 10 1992 
  Published    1993 
  Keywords    Electron Transfer, Kinetics, Tw o-Electron G ate, Herbicide Resistance, Photosystem II 
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 TEI-XML for    default:Reihe_C/48/ZNC-1993-48c-0259.pdf 
 Identifier    ZNC-1993-48c-0259 
 Volume    48