Higher concentration of Q(B)-nonreducing photosystem II centers in triazine-resistant Chenopodium album plants as revealed by analysis of chlorophyll fluorescence kinetics

Plants resistant to triazine-type herbicides are known to be altered in their photosystem II reaction center. Serine at site 264 in D1 protein is replaced by glycine. The measurements of chlorophyll a fluorescence excitations with a variable number of saturating flashes in Chenopodium album plants s...

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Veröffentlicht in:Journal of plant physiology. - 1979. - 166(2009), 15 vom: 15. Okt., Seite 1616-23
1. Verfasser: Van Rensen, Jack J S (VerfasserIn)
Weitere Verfasser: Vredenberg, Wim J
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2009
Zugriff auf das übergeordnete Werk:Journal of plant physiology
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Photosystem II Protein Complex Plant Proteins Triazines Chlorophyll 1406-65-1 Chlorophyll A YF5Q9EJC8Y
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245 1 0 |a Higher concentration of Q(B)-nonreducing photosystem II centers in triazine-resistant Chenopodium album plants as revealed by analysis of chlorophyll fluorescence kinetics 
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520 |a Plants resistant to triazine-type herbicides are known to be altered in their photosystem II reaction center. Serine at site 264 in D1 protein is replaced by glycine. The measurements of chlorophyll a fluorescence excitations with a variable number of saturating flashes in Chenopodium album plants show characteristic differences between the resistant and the wild-type plants. These differences appear in response to the first flash as well as in the rise pattern of subsequent flashes of a 12.5 Hz flash train. The differences indicate a higher concentration of Q(B)-nonreducing reaction centers in the resistant biotype, and confirm earlier results on a slower rate of electron transport between the primary and secondary electron acceptors 
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