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...
| Veröffentlicht in: | Journal of plant physiology. - 1979. - 166(2009), 15 vom: 15. Okt., Seite 1616-23 |
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| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2009
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| 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 |
| Zusammenfassung: | 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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| Beschreibung: | Date Completed 17.11.2009 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1618-1328 |
| DOI: | 10.1016/j.jplph.2009.04.011 |