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Articles

Regulation of Soybean Net Photosynthetic CO₂ Fixation by the Interaction of CO₂, O₂, and Ribulose 1,5-Diphosphate Carboxylase ^1,2

William L. Ogren^b

Richard H. Hageman^c

^a Department of Agronomy, University of Illinois, Urbana, Illinois 61801, ^b United States Regional Soybean Laboratory, North Central Region, Agricultural Research Service, United States Department of Agriculture, Urbana, Illinois 61801, Department of Agronomy, University of Illinois, Urbana, Illinois 61801

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 O₂ concentration. With leaves, O₂ inhibition of net photosynthetic CO₂ fixation increased when the ambient leaf temperature was increased. The increased inhibition of CO₂ 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, O₂ inhibition of CO₂ incorporation and the ratio of oxygenase activity to carboxylase activity increased with increased temperature. The increased O₂ sensitivity of the enzyme at higher temperature was caused by a reduced affinity of the enzyme for CO₂ and a slightly increased affinity of the enzyme for O₂. The similarity of the effect of temperature on the affinity of intact leaves and of ribulose 1,5-diphosphate carboxylase for CO₂ and O₂ provides further evidence that the carboxylase regulates the O₂ response of photosynthetic CO₂ fixation in soybean leaves. Based on results reported here and in the literature, a scheme outlining the stoichiometry between CO₂ and O₂ fixation in vivo is proposed.

Oxygen competitively inhibited carboxylase activity with respect to CO₂, and CO₂ competitively inhibited oxygenase activity with respect to O₂. Within the limits of experimental error, the Michaelis constant (CO₂) in the carboxylase reaction was identical with the inhibition constant (CO₂) in the oxygenase reaction, and the Michaelis constant (O₂) in the oxygenase reaction was identical with the inhibition constant (O₂) in the carboxylase reaction. The Michaelis constant, (ribulose 1,5-diphosphate) was the same in both the carboxylase and oxygenase reactions. This equality of kinetic constants is consistent with the notion that the same enzyme catalyzes both reactions.

¹ This investigation was supported in part by Agricultural Research Service, United States Department of Agriculture Cooperative Agreements 016-15-18 and 716-15-10. and by the Department of Scientific and Industrial Research, New Zealand.

² Dedicated to the memory of Milton Zucker.

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