In this section
@article{Vermaas:1984:10.1016/0014-5793(84)80744-9,
author = {Vermaas, WFJ and Rutherford, AW},
doi = {10.1016/0014-5793(84)80744-9},
journal = {FEBS Letters},
pages = {243--248},
title = {EPR measurements on the effects of bicarbonate and triazine resistance on the acceptor side of Photosystem II},
url = {http://dx.doi.org/10.1016/0014-5793(84)80744-9},
volume = {175},
year = {1984}
}
TY - JOUR
AB - CO<inf>2</inf> depletion leads to an approximately 10-fold increase in the light-induced EPR signal at g = 1.82, attributed to the Q<inf>A</inf><sup>-</sup> · Fe<sup>2+</sup> complex, in Photosystem II-enriched thylakoid membrane fragments. Upon reconstitution with HCO<inf>3</inf><sup>-</sup>the signal decreases to the size in control samples. The split pheophytin<sup>-</sup> signal is broader in control or reconstituted than in CO<inf>2</inf>-depleted samples. It is concluded that HCO<inf>2</inf><sup>-</sup> strongly influences the localization and conformation of the Q<inf>A</inf><sup>-</sup> · Fe<sup>+</sup> complex. The Q<inf>A</inf><sup>-</sup> · Fe<sup>2+</sup> and split pheophytirr<sup>-</sup> EPR signals from triazine-resistant Brassica napus were virtually identical to those from triazine-susceptible samples, indicating that the change in the 32-kDa azidoatrazine-binding protein does not lead to a confonnational change of the Q<inf>a</inf><sup>-</sup> · Fe<sup>2+</sup> complex. © 1984.
AU - Vermaas,WFJ
AU - Rutherford,AW
DO - 10.1016/0014-5793(84)80744-9
EP - 248
PY - 1984///
SN - 0014-5793
SP - 243
TI - EPR measurements on the effects of bicarbonate and triazine resistance on the acceptor side of Photosystem II
T2 - FEBS Letters
UR - http://dx.doi.org/10.1016/0014-5793(84)80744-9
VL - 175
ER -
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