Abstract
We investigated the inhibitory action of cadmium ions on the energy and electron transfer within PSII using fluorescence spectroscopy. We have examined thylakoid membranes isolated from a wild type (WT) and a mutant (M) of tobacco with a point mutation in the β-chain of cytochrome b559. Variable fluorescence measurements were made of PSII samples treated with various concentrations of cadmium salts. From these experiments we were able to determine the impact of the cadmium cations on the efficiency of photochemical processes within PSII and the activity of its acceptor side. We observed that cadmium ions act differently on the WT and M in the presence of chloride anions. Sulfate ions enhanced the inhibitory effect of Cd2+ but at low concentrations, CdSO4 diminished some characteristic transitions monitored for CdCl2. At the lowest applied concentrations, the salts had no influence on the Kautsky effect in the mutant, whereas a strong effect is observed in the WT. This phenomenon is related to the point mutation of cytochrome b559 which is supposed to modify the QB binding site on the acceptor side of PSII (Burda et al., these Proceedings). At higher applied concentrations of Cd salts, one has to consider additional Cd2+ interactions with chlorophylls from the light harvesting antenna.
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References
Ädelroth P, Paddock ML, Tehrani A, Beatty JT, Feher G, Okamura MY (2001) Identification of the proton pathway in bacterial reaction centers: Decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors. Biochem 40:14538-14546.
Berthold DA, Babcock GT, Yocum CE (1981) A highly resolved, oxygen evolving Photosystem II preparation from spinach thylakoid membranes. FEBS Lett 134:231-234.
Bock R, Koessel H, Maliga P (1994) Introduction of a heterologous editing site into the tobacco plastid genome - the lack of RNA editing leads to a mutant phenotype. EMBO J 13:4623-4628.
Ishikita H, Knapp E-W (2005) Induced conformational changes upon Cd2 + binding at photosynthetic reaction centers. PNAS 12(45):16215-16220.
Paddock ML, Sagle L, Tehrani A, Beatty JT, Feher G, Okamura MY (2003) Mechanism of proton transfer inhibition by Cd2+ binding to bacterial reaction centers: Determination of the pKA of functionally important histidine residues. Biochem 42:9626-9632.
Utsching LM, Ohigashi Y, Thurnauer MC, Tiede DM (1998) Centers that modulates QA to QB electron transfer. Biochem 37:8278-8281.
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© 2008 Springer Science + Business Media, B.V.
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de Odrowaąż Piramowicz, M., Bock, R., Orzechowska, A., Strzałka, K., Burda, K. (2008). Binding Sites of Cadmium Ions Within Photosystem II. In: Allen, J.F., Gantt, E., Golbeck, J.H., Osmond, B. (eds) Photosynthesis. Energy from the Sun. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-6709-9_70
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DOI: https://doi.org/10.1007/978-1-4020-6709-9_70
Publisher Name: Springer, Dordrecht
Print ISBN: 978-1-4020-6707-5
Online ISBN: 978-1-4020-6709-9
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