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MECHANISM OF PHOTOINACTIVATION OF PLANT PLASMA MEMBRANE ATPASE
Author(s) -
Imbrie C. W.,
Murphy T. M.
Publication year - 1984
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1984.tb04582.x
Subject(s) - chemistry , photochemistry , atpase , membrane , rosa × damascena , tryptophan , singlet oxygen , biophysics , absorbance , fluorescence , oxygen , octane , azide , solvent , chromatography , biochemistry , organic chemistry , biology , essential oil , enzyme , physics , amino acid , quantum mechanics
UV radiation at 290 and 365 nm inactivates two forms of the K + ‐stimulated ATPase associated with the plasma membrane of suspension‐cultured cells of Rosa damascena . One form is 15 and 36 times more sensitive than the other to 290 and 365 nm, respectively. For both forms, the inactivation requires oxygen, is inhibited by azide and diazobicyclo(2.2.2.2)octane, but not glycerol, and is enhanced up to 7.5 times in deuterium oxide solvent. Inactivation occurs concomitantly with loss of absorbance at 290 nm. Cs + and NO − 3 , quenchers of tryptophan fluorescence, inhibit inactivation. The results suggest that inactivation involves singlet‐oxygen mediated destruction of tryptophans in the ATPases.