herbicide binding niche of photosystem II--a model

The Q(B) binding niche of photosystem II is also the binding site for many different herbicides. In order to understand the mode of binding of the herbicides, a 3-dimensional model of the binding niche was constructed. The model was based upon a comparison of the known structure of the Q(B) binding...

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Veröffentlicht in:Pesticide Science 1991, Vol.31 (1), p.65-72
Hauptverfasser: Tietjen, K.G, Kluth, J.F, Andree, R, Haug, M, Lindig, M, Muller, K.H, Wroblowsky, H.J, Trebst, A
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container_end_page 72
container_issue 1
container_start_page 65
container_title Pesticide Science
container_volume 31
creator Tietjen, K.G
Kluth, J.F
Andree, R
Haug, M
Lindig, M
Muller, K.H
Wroblowsky, H.J
Trebst, A
description The Q(B) binding niche of photosystem II is also the binding site for many different herbicides. In order to understand the mode of binding of the herbicides, a 3-dimensional model of the binding niche was constructed. The model was based upon a comparison of the known structure of the Q(B) binding niche in purple bacteria with sequence and mutant data of the D-1 protein of photosystem II. Plastoquinone builds up hydrogen bonds to phenylalanine 265 backbone amide nitrogen, to serine 264 hydroxyl, and to histidine 215 delta-1 nitrogen. In addition to these hydrogen bond donors and acceptors, herbicides call build up hydrogen bonds to backbone carbonyl of alanine 263 and to serine 268 hydroxyl. This is supported by binding data of inhibitors in Chlamydomonas reinhardtii chloroplasts of wild type and of five D-I protein mutants (Ser264Ala, Ala251 Val, Phe255Tyr, Val2l9Ile, Leu275Phe).
doi_str_mv 10.1002/ps.2780310108
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Sci</addtitle><description>The Q(B) binding niche of photosystem II is also the binding site for many different herbicides. In order to understand the mode of binding of the herbicides, a 3-dimensional model of the binding niche was constructed. The model was based upon a comparison of the known structure of the Q(B) binding niche in purple bacteria with sequence and mutant data of the D-1 protein of photosystem II. Plastoquinone builds up hydrogen bonds to phenylalanine 265 backbone amide nitrogen, to serine 264 hydroxyl, and to histidine 215 delta-1 nitrogen. In addition to these hydrogen bond donors and acceptors, herbicides call build up hydrogen bonds to backbone carbonyl of alanine 263 and to serine 268 hydroxyl. This is supported by binding data of inhibitors in Chlamydomonas reinhardtii chloroplasts of wild type and of five D-I protein mutants (Ser264Ala, Ala251 Val, Phe255Tyr, Val2l9Ile, Leu275Phe).</description><subject>Agronomy. 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Sci</addtitle><date>1991</date><risdate>1991</risdate><volume>31</volume><issue>1</issue><spage>65</spage><epage>72</epage><pages>65-72</pages><issn>0031-613X</issn><issn>1526-498X</issn><eissn>1096-9063</eissn><coden>PSSCBG</coden><abstract>The Q(B) binding niche of photosystem II is also the binding site for many different herbicides. In order to understand the mode of binding of the herbicides, a 3-dimensional model of the binding niche was constructed. The model was based upon a comparison of the known structure of the Q(B) binding niche in purple bacteria with sequence and mutant data of the D-1 protein of photosystem II. Plastoquinone builds up hydrogen bonds to phenylalanine 265 backbone amide nitrogen, to serine 264 hydroxyl, and to histidine 215 delta-1 nitrogen. In addition to these hydrogen bond donors and acceptors, herbicides call build up hydrogen bonds to backbone carbonyl of alanine 263 and to serine 268 hydroxyl. This is supported by binding data of inhibitors in Chlamydomonas reinhardtii chloroplasts of wild type and of five D-I protein mutants (Ser264Ala, Ala251 Val, Phe255Tyr, Val2l9Ile, Leu275Phe).</abstract><cop>London</cop><pub>John Wiley &amp; Sons, Ltd</pub><doi>10.1002/ps.2780310108</doi><tpages>8</tpages></addata></record>
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identifier ISSN: 0031-613X
ispartof Pesticide Science, 1991, Vol.31 (1), p.65-72
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source Wiley Online Library Journals Frontfile Complete; Periodicals Index Online
subjects Agronomy. Soil science and plant productions
amino acids
atrazine
binding sites
Biological and medical sciences
Chemical control
Chlamydomonas reinhardtii
chloroplasts
cyanoacrylate
Fundamental and applied biological sciences. Psychology
herbicides
inhibitors
interactions
lenacil
metribuzin
molecular conformation
Parasitic plants. Weeds
photosystem II
Phytopathology. Animal pests. Plant and forest protection
proteins
simulation models
thiazoles
triazine herbicides
Weeds
title herbicide binding niche of photosystem II--a model
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