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Spinach RuBP carboxylase-oxygenase (Rubisco) purified from the commercially available enzyme, underwent kinetic changes when micromolar concentrations of O-p-nitrophenylhy- droxvlamine (NPHA) were applied on fully activated enzyme. Under steady-state conditions, a decrease of K m  CO 2  was observed without changes in V max . Double reciprocal plots showed a competitive stimulation of carboxylase function. The substrate specificity factor k = V c  K o /V o  K c  was increased from approximatively 15-20% upon treatment with NPHA, using both parallel and simultaneous determinations of RuBP-carboxylase and oxygenase activities.

zeitschrift für naturforschung c

Chemical Control of Photorespiration: Steady-State Kinetic and Conformational Changes of Ribulose-1,5-bisphosphate Carboxylase/Oxygenase Obtained with O-p-Nitrophenylhydroxylamine