PH-DEPENDENT EXTRACTION OF CA2-II MEMBRANES AND THYLAKOID MEMBRANES -INDICATION OF A CA2+-SENSITIVE SITE ON THE ACCEPTOR SIDE OF PHOTOSYSTEM-II( FROM PHOTOSYSTEM)
Bk. Semin et al., PH-DEPENDENT EXTRACTION OF CA2-II MEMBRANES AND THYLAKOID MEMBRANES -INDICATION OF A CA2+-SENSITIVE SITE ON THE ACCEPTOR SIDE OF PHOTOSYSTEM-II( FROM PHOTOSYSTEM), Photochemistry and photobiology, 68(4), 1998, pp. 538-544
The action of low pH treatment (pH 3.6) known to release Ca2+ from the
oxygen-evolving complex in photosystem II (PSII) membranes and to ind
uce Ca2+-reversible inhibition of electron transport at the acceptor s
ide of PSII in thylakoid membranes (TM) was compared in PSII membranes
and TM. The rate of the inactivation of electron transport by low pH
was four times higher in TM than in PSII membranes. Ferricyanide accel
erated the inactivation of PSII membranes but decreased it in the case
of TM, Low pH treatment also greatly modified the fluorescence induct
ion kinetics in both preparations, but significant differences have be
en found in the fluorescence induction kinetics of treated TM and PSII
membranes. Calcium restored the electron transport activity and fluor
escence induction kinetics in PSII membranes and TM, whereas diphenylc
arbazide restored these functions only in PSII membranes. The reactiva
tion of Ca-depleted PSII membranes was more effective in the dark, whe
reas the reactivation of TM required weak light. In the case of PSII m
embranes subjected to low pH citrate buffer, maximal reactivation was
observed at 60 mM Ca2+ but for TM about 10 mM Ca2+ was required and 60
mM fully inhibited electron transport in TM during reactivation. Thes
e results indicate that the Ca-dependent inactivation of the acceptor
side of PSII in TM after low pH treatment cannot be explained by the e
xtraction of Ca2+ from the oxygen-evolving complex. It is rather sugge
sted that the Ca2+ involved in this inhibition is bound to the accepto
r side of the photosystem near to the Q(A)-non-heme iron binding site
and may participate in the binding of a polypeptide of the PSII light
antenna complex to the PSII reaction center.