Abstract
The generation of transmembrane electric potential difference (ΔΨ) in quinone acceptor complex of proteoliposomes containing core complexes of photosystem II from spinach was studied using for the measurements a direct electrometric technique. Besides the fast increase in the membrane potential associated with the electron transfer between the redox-active tyrosine 161 residue (YZ) in D1 polypeptide and the primary quinone acceptor QA, an additional electrogenic phase with τ ∼ 0.85 msec at pH 7.3 and the maximal relative amplitude of ∼ 11% of the Y oxZ Q −A phase was observed after the second light flash. The sensitivity of this phase to diuron (an inhibitor of electron transfer between QA and the secondary quinone acceptor QB), the dependence of its amplitude on the light flash parity, and also a decrease in its rate constant with increase in pH indicated that it was due to dismutation of Q −A and Q −B with the subsequent protonation of a doubly reduced plastoquinone molecule: Q −A Q −B + 2H+ → QAQBH2.
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Abbreviations
- PSII:
-
pigment-protein complex of photosystem II
- RC:
-
reaction center
- QA and QB :
-
primary and secondary quinone acceptor, respectively
- P680:
-
primary electron donor of PSII RC
- YZ :
-
redox-active tyrosine 161 residue of PSII D1 subunit
- ΔΨ:
-
transmembrane electric potential difference
- τ:
-
time of response amplitude changing e-fold
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Translated from Biokhimiya, Vol. 70, No. 12, 2005, pp. 1639–1645.
Original Russian Text Copyright © 2005 by Mamedov, Tyunyatkina, Semenov.
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Mamedov, M.D., Tyunyatkina, A.A. & Semenov, A.Y. Electrogenic Protonation of the Secondary Quinone Acceptor QB in Spinach Photosystem II Complexes Incorporated into Lipid Vesicles. Biochemistry (Moscow) 70, 1348–1353 (2005). https://doi.org/10.1007/s10541-005-0268-z
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DOI: https://doi.org/10.1007/s10541-005-0268-z