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'Atrazine' in keywords Facet   section ZfN Section C  [X]
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1993 (1)
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1981 (1)
1Author    KatherineE. Steinback, Klaus Pfister, CharlesJ. AmtzenRequires cookie*
 Title    Trypsin-Mediated Removal of Herbicide Binding Sites within the Photosystem II Complex  
 Abstract    Trypsin treatment of isolated chloroplast thylakoids resulted in a step-wise modification o f surface exposed membrane polypeptides. Early effects o f the protease action resulted in a decrease in inhibitory activity of atrazine, diuron, pyrazon, and bromacil, but an initial increase in the activity of bromnitrothymol and dinoseb. Direct measurements o f atrazine binding demonstrated that decreased inhibitory activity corresponded to a decreased binding affinity in the treated membranes. Longer term effects o f trypsin caused removal of atrazine binding sites and a concomitant block o f electron transport chains. The data are consistent with a concept that the traizine receptor protein is a component o f the electron transport chain which is successively degraded in two or more steps by protease attack. Polyacrylamide gel electrophoresis of trypsin-treated membranes and sub-membrane fragments derived from these membranes revealed that several polypeptides are membrane surface exposed. The involvement o f a 32000 dalton polypeptide in creating the atrazine binding site is discussed. 
  Reference    Z. Naturforsch. 36c, 98 (1981); received September 221980 
  Published    1981 
  Keywords    Photosynthesis, Atrazine, Diuron, Chloroplast Membranes, Receptor Protein 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0098.pdf 
 Identifier    ZNC-1981-36c-0098 
 Volume    36 
2Author    G. Ewald, C. Wiessner, H. MichelRequires cookie*
 Title    Sequence Analysis of Four Atrazine-Resistant Mutants from Rhodopseudomonas viridis  
 Abstract    Four atrazine-resistant mutants from the purple bacterium Rhodopseudom onas viridis were isolated. Sequence analysis revealed three different mutant strains carrying mutations in the herbicide-binding pocket: i) M AV 2: L 212-G lu —* Lys, ii) M AV 3: L216-Phe —» Ser and iii) M AV 4 = MAV 5: L217-Arg His, L220-Val Leu. Except M AV 3 all Rps. viridis mutants are different from those selected by their resistance towards the closely related triazine terbutryn. 
  Reference    Z. Naturforsch. 45c, 459 (1990); received December 9 1989 
  Published    1990 
  Keywords    Herbicide-Resistant Mutants, Atrazine, Photosynthetic Reaction Center, Sequence Analysis 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0459.pdf 
 Identifier    ZNC-1990-45c-0459 
 Volume    45 
3Author    MarcelA K Jansen, ChristoM. Alan, Yoseph Shaaltiel, Jonathan GresselRequires cookie*
 Title    Mode of Evolved Photooxidant Resistance to Herbicides and Xenobiotics  
 Abstract    A few species have evolved resistance to paraquat after repeated selection. As paraquat still inhibited N A D P reduction, we hypothesized that resistance might be due to (a) detoxification o f the paraquat-generated active oxygen species and (b) that resistant plants would have some cross resistance to other xenobiotic oxidants as well as to photoinhibition, which we subse­ quently demonstrated. The levels o f plastid isozymes o f the oxygen detoxification pathway: (CuZn) superoxide dismutase, ascorbate peroxidase and glutathione reductase were genetical­ ly higher in the resistant than in the sensitive biotype o f C onyza bonariensis through the F2 generation. Resistance was suppressed by chelators o f copper and/or zinc. Intact chloroplasts from resistant plants had less membrane damage with and without paraquat, than those from sensitive plants. Resistant C onyza plants recover from paraquat inhibition o f photosynthesis in 3 -4 h in high light, whereas sensitive plants died. Both resistant and sensitive plants recov­ ered from paraquat in 3 -4 h in low light intensities. Paraquat-resistant Conyza plants were cross-tolerant to S 0 2, atrazine, acifluorfen and to photoinhibition. Drought-tolerant maize inbreds were cross-tolerant to paraquat, SO, and acifluorfen (compared to sensitive lines) and they also possessed higher levels o f (Cu/Zn) superoxide dismutase and glutathione reductase. The tolerance to oxidant stresses in C onyza and maize increases with plant age, suggesting that the shift to resistance is a constitutive, earlier expression o f the genes normally expressed later in development. 
  Reference    Z. Naturforsch. 45c, 463 (1990); received November 9 1989 
  Published    1990 
  Keywords    Paraquat, Acifluorfen, Atrazine, Photoinhibition, Superoxide Dismutase 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0463.pdf 
 Identifier    ZNC-1990-45c-0463 
 Volume    45 
4Author    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