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Thermoluminescence evidence for light‐induced oxidation of tyrosine and histidine residues in manganese‐depleted photosystem II particles
Author(s) -
Allakhverdiev Suleyman I.,
Klimov Vyacheslav V.,
Demeter Sandor
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80325-b
Subject(s) - photosystem ii , p680 , histidine , manganese , chemistry , tyrosine , photosynthetic reaction centre , thermoluminescence , electron paramagnetic resonance , photochemistry , electron transfer , photosystem , electron transport chain , photosystem i , nuclear chemistry , photosynthesis , biochemistry , enzyme , materials science , nuclear magnetic resonance , luminescence , organic chemistry , optoelectronics , physics
In the thermoluminescence (TL) glow curve of photosystem II, particles depleted of manganese, a tyrosine modifier, 7‐chloro‐4‐nitrobenz‐2‐oxa‐1,3‐diazole (NBD) a bolishes the TL band appearing around −55°C (TL −55 ). Addition of a histidine modifier, diethylpyrocarbonate results in the disappearance of the band peaking around −30°C (TL −30 ). NBD treatment also abolishes the EPR signal II fast of oxidized tyrosine donor, Y 21 and inhibits the electron transport from diphenylcarbazide to 2,6‐dichlorophenol‐indophenol. It is concluded that the TL −55 and TL −30 bands can be assigned to oxidized tyrosine (Y 2 + ) and histidine (His + ) residues, respectively, which participate in electron transfer from manganese to the reaction center of chlorophyll, P680 + .