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- W4254409128 abstract "Oxidation of the reduced primary electron acceptor, QA−, of Photosystem II (PS II) in formate-treated spinach thylakoids, was inhibited more after the second than after the first actinic flash. This indicates a slowing of electron flow on the acceptor side of PS II from QA− to QB−, the semiquinone form of the secondary plastoquinone acceptor, formed by electron transfer after the first flash. A hypothesis of electron transfer on the acceptor side of PS II is proposed to accommodate the bicarbonate-reversible formate/formic acid inhibition of electron transfer after single turnover flashes. We suggest that the large inhibition in QA− oxidation after the second flash reflects a blockage of the proton uptake that stabilizes QB−. Kinetics of onset of inhibition following formate addition were followed by measuring the chlorophyll a fluorescence yield, reflecting the concentration of QA−, 1 ms after the second actinic flash as a function of time after the addition of formate. The apparent rate constants for binding and unbinding, and the dissociation constant of formate were determined in the pH range from 5.5 to 7.5. The rate of onset of inhibition following formate addition, reflecting formate or formic acid binding, was highly dependent on the medium pH. Measurements on the initial binding rate, when one of the two (HCO2−/HCOOH) equilibrium species was kept constant and the other varied, suggested that formic acid is the binding species. This conclusion was consistent with the observed pH dependence of formate binding." @default.
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- W4254409128 date "1991-12-03" @default.
- W4254409128 modified "2023-09-27" @default.
- W4254409128 title "Kinetic characteristics of formate/formic acid binding at the plastoquinone reductase site in spinach thylakoids" @default.
- W4254409128 doi "https://doi.org/10.1016/0167-4838(91)90582-k" @default.
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