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• W1976804570 abstract "An electron paramagnetic resonance (EPR) signal near g=6 in Photosystem II (PSII) membranes has been assigned to a high spin form of cytochrome (Cyt) b(559) (R. Fiege, U. Schreiber, G. Renger, W. Lubitz, V.A. Shuvalov, FEBS Lett. 377 (1995) 325-329). Here we have further investigated the origin of this signal. A slow formation of the signal during storage in the dark is observed in oxygen-evolving PSII membranes, which correlate with the oxidation of Fe(2+) by plastosemiquinone or oxygen. Removal of oxygen inhibits formation of the high spin iron signal. The g=6 EPR signal is photoreduced at cryogenic temperatures and is restored slowly by subsequent dark storage at 77 K. The amplitude of the photoreduced signal increases as the pH is lowered, which shows that the origin is not the hydroxyl ligated Cyt b(559) species proposed previously. Different cryoprotectants also influence the amplitude and lineshape of the high spin iron signal in a manner suggesting that smaller cryoprotectants can penetrate the iron environment. A correlation between the high spin iron and g=1.6 EPR signal assigned to an interaction involving the semiquinones of Qa and Qb is shown. It is concluded that the appearance of the high spin iron signal in oxygen-evolving PSII membranes involves reduced PSII electron acceptors and oxygen and suggests that the signal is from the non-haem iron of PSII." @default.
• W1976804570 created "2016-06-24" @default.
• W1976804570 creator A5080633635 @default.
• W1976804570 date "2001-04-01" @default.
• W1976804570 modified "2023-10-18" @default.
• W1976804570 title "Photoreducible high spin iron electron paramagnetic resonance signals in dark-adapted Photosystem II: are they oxidised non-haem iron formed from interaction of oxygen with PSII electron acceptors?" @default.
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• W1976804570 doi "https://doi.org/10.1016/s0005-2728(00)00257-7" @default.
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