Cotyledonary leaves of Cucumis sativus cv. Poinsette exhibited senescence-induced losses in chlorophyll (Chl) and protein contents within three weeks since germination. Chl and protein concentrations in cotyledonary leaves approached maximum on 6th d after germination and they declined to 50 and 41 %, respectively, by the 20th day of growth. Activities of both photosystem (PS) 2 and PS1 decreased by 33 and 31 %, respectively, on the 20th day, compared to the control 6th day. Changes in sensitivity of PS2 to inhibitors like atrazine and dibromothymoquinone and sensitivity of PS1 to KCN accompanied the changes in PS2 and PS1 activities. Hence both the acceptor side of PS2 and the donor side of PS1 are affected by senescence-induced changes in cucumber cotyledonary leaves. and J. S. S. Prakash, M. A. Baig, Prasanna Mohanty.
The photosynthetic election transport activities in beet spinách thylakoids were studied using ruthenium chloride as an electron acceptor, Like potassium ferricyanide, RUCI3 supported the non-cyclic electron flow with net evolution of oxygen. The rate of oxygen evolution was at its maximum with 0.5 mM RUCI3 at pH of 8.0 and the election flow coupled to translocation of protons into the thylakoid vesicles. Ruthenium chloride-supported oxygen evolution was inhibited by specific photosynthetic electron tiansport inhibitors like diuron, dibromothymoquinone, potassium cyanide, and mercuric chloride Unlike ferricyanide, the RuCl3-supported oxygen evolution was totally inliibited by potassium cyanide and mercuric chloride at both pH 8.0 and 6.5. Since potassium cyanide and mercuric chloride mostly interrupt the electron flow at plastocyanin level, RUCI3 probably accepts electrons mostly from photosystem 1 or its near vicinity. Besides electron acceptance, RUCI3 suppresses the photophosphoiylation activity in a manner similar to energy transfer inhibitors.
The effects of phenylmercuric acetate (PMA) and apoferredoxin (apoFd) on the diaphorase activity of spinach ferredoxin:NADP+ oxidoreductase (FNR) in the presence of dibromothymoquinone (DBMIB) or cytochrome c (Cyt c) were studied. PMA inhibited effectively (I50 = < 5 μM) ferredoxin-dependent Cyt c reduction but did not affect evidently the enzyme activity in the presence of DBMIB as an electron acceptor. ApoFd caused also inhibition of Cyt c reduction but slightly stimulated, like ferredoxin, DBMIB reduction. We confirm a hypothesis according to which three binding sites for substrates [NADP(H), Fd-Cyt c, quinone/dichlorophenol indophenol] occur within the molecule of isolated FNR. and M. Bojko, S. Więckowski.