Kinetic properties of soybean net photosynthetic CO2 fixation and of the carboxylase and oxygenase activities of purified soybean (Glycine max [L.] Merr.) ribulose 1 ,5-diphosphate carboxylase (EC 4.1.1.39) were examined as functions of temperature, CO2 concentration, and 02 concentration. With leaves, 02 inhibition of net photosynthetic C02 fixation increased when the ambient leaf temperature was increased. The increased inhibition of C02 fixation at higher temperatures was caused by a reduced affinity of the leaf for CO2 and an increased affinity of the leaf for O2. With purified ribulose 1,5-diphosphate carboxylase, 02 inhibition of C02 incorporation and the ratio of oxygenase activity to carboxylase activity increased with increased temperature. The increased 02 sensitivity of the enzyme at higher temperature was caused by a reduced affinity of the enzyme for C02 and a slightly increased affinity of the enzyme for 02. (10-12, 19, 20). This reversible inhibition is associated with the photosynthetic carbon reduction cycle (11), and the inhibition can be reduced by increasing the CO2 concentration, decreasing the 02 concentration, or by reducing the temperature (15,16 (9,21,23,27