[Light activation of the enzyme ribulose diphosphate carboxylase].
Some activation mechanisms of RuDP-carboxylase under illumination are considered. It is assumed on the grounds of experimental data that under illumination thylacoid membranes pass from one phase (I) to another (II). Kinetics of this transition is taken as similar to that of surface phase transition of the first kind. It is assumed that the number of enzyme molecules passing from the inactive to active state is proportional to the area of thylacoid membranes in the II phase (as the time function). A change in the stroma determined by the kinetics of transition of thylocoid membranes in the transition process leads to a change of the mean time between two successive catalytic acts of the enzyme activated molecules. The obtained kinetic curve of RuDP-carboxylating reaction in the transition process under illumination coincides with the curve obtained in [1] by expanding the experimental curves of the values of labels 14C, 32P of 3PGA to constituents.
D002262:Carboxy-Lyases / Q000528:radiation effects*; D002736:Chloroplasts / Q000201:enzymology* / Q000528:radiation effects; D004789:Enzyme Activation / Q000528:radiation effects; D006859:Hydrogen / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007425:Intracellular Membranes / Q000528:radiation effects; D007700:Kinetics; D008027:Light; D008274:Magnesium / Q000494:pharmacology; D010539:Permeability; D012273:Ribulose-Bisphosphate Carboxylase / Q000528:radiation effects*
D006859:Hydrogen; D002262:Carboxy-Lyases; D012273:Ribulose-Bisphosphate Carboxylase; D008274:Magnesium
Aktivirovanie svetom fermenta ribulozodifosfatkarboksilazy.