A theoretical study on effect of the initial redox state of cytochrome b559 on maximal chlorophyll fluorescence level (F(M)): implications for photoinhibition of photosystem II.
In this work, we extended the reversible radical pair model which describes energy utilization and electron transfer up to the first quinone electron acceptor (Q(A)) in photosystem II (PSII), by redox reactions involving cytochrome (cyt) b559. In the model, cyt b559 accepts electrons from the reduced primary electron acceptor in PSII, pheophytin, and donates electrons to the oxidized primary electron donor in PSII (P680+). Theoretical simulations of chlorophyll fluorescence rise based on the model show that the maximal fluorescence, F(M), increases with an increasing amount of initially reduced cyt b559. In this work we applied, the first to our knowledge, metabolic control analysis (MCA) to a model of reactions in PSII. The MCA was used to determine to what extent the reactions occurring in the model control the F(M) level and how this control depends on the initial redox state of cyt b559. The simulations also revealed that increasing the amount of initially reduced cyt b559 could protect PSII against photoinhibition. Also experimental data, which might be used to validate our theory, are presented and discussed.
Lazár
Dusan
D
Laboratory of Biophysics, Department of Experimental Physics, Faculty of Science, Palacký University, tr. Svobody 26, 771 46 Olomouc, Czech Republic. lazard@seznam.cz
Ilík
Petr
P
Kruk
Jerzy
J
Strzałka
Kazimierz
K
Naus
Jan
J
D002734:Chlorophyll / Q000737:chemistry*; D003573:Cytochrome b Group / Q000378:metabolism*; D004579:Electron Transport; D005453:Fluorescence; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins / Q000378:metabolism*; D045332:Photosystem II Protein Complex / Q000378:metabolism*
D003573:Cytochrome b Group; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D002734:Chlorophyll; C019313:cytochrome b559