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- W1976452404 abstract "Two mutants, D1-H198Q and D1-H198A, have been previously constructed in Thermosynechococcus elongatus with the aim at modifying the redox potential of the P680•+/P680 couple by changing the axial ligand of PD1, one the two chlorophylls of the Photosystem II primary electron donor [Sugiura et al., Biochim. Biophys. Acta 1777 (2008) 331–342]. However, after the publication of this work it was pointed out to us by Dr. Eberhard Schlodder (Technische Universität Berlin) that in both mutants the pheophytin band shift which is observed upon the reduction of QA was centered at 544 nm instead of 547 nm, clearly showing that the D1 protein corresponded to PsbA1 whereas the mutants were supposedly constructed in the psbA3 gene so that the conclusions in our previous paper were wrong. O2 evolving mutants have been therefore reconstructed and their analyze shows that they are now correct mutants which are suitable for further studies. Indeed, the D1-H198Q mutation downshifted by ≈ 3 nm the P680•+/P680 difference absorption spectrum in the Soret region and increased the redox potential of the P680•+/P680 couple and the D1-H198A mutation decreased the redox potential of the P680•+/P680 couple all these effects being comparable to those which were observed in Synechocystis sp. PCC 6803 [Diner et al., Biochemistry 40 (2001) 9265–9281 and Merry et al. Biochemistry 37 (1998) 17,439–17,447]. We apologize for having presented wrong data and wrong conclusions in our earlier publication." @default.
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- W1976452404 date "2016-12-01" @default.
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- W1976452404 title "Corrigendum to Influence of Histidine-198 of the D1 subunit on the properties of the primary electron donor, P 680 , of photosystem II in Thermosynechococcus elongatus" @default.
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- W1976452404 doi "https://doi.org/10.1016/j.bbabio.2016.09.012" @default.
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