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Wildner GF, Henkel J. The effect of divalent metal ions on the activity of Mg(++) depleted ribulose-1,5-bisphosphate oxygenase. Planta. 1979;146(2):223-8doi: 10.1007/BF00388236.
Wildner, G. F., & Henkel, J. (1979). The effect of divalent metal ions on the activity of Mg(++) depleted ribulose-1,5-bisphosphate oxygenase. Planta, 146(2), 223-8. https://doi.org/10.1007/BF00388236
Wildner, G F, and Henkel, J. "The effect of divalent metal ions on the activity of Mg(++) depleted ribulose-1,5-bisphosphate oxygenase." Planta vol. 146,2 (1979): 223-8. doi: https://doi.org/10.1007/BF00388236
Wildner GF, Henkel J. The effect of divalent metal ions on the activity of Mg(++) depleted ribulose-1,5-bisphosphate oxygenase. Planta. 1979 Jan;146(2):223-8. doi: 10.1007/BF00388236. PMID: 24318063.
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Planta. 1979 Jan;146(2):223-8. doi: 10.1007/BF00388236.

The effect of divalent metal ions on the activity of Mg(++) depleted ribulose-1,5-bisphosphate oxygenase.

Planta

G F Wildner, J Henkel

Affiliations

  1. Lehrstuhl für Biochemie der Pflanzen, Ruhr-Universität Bochum, Postfach 102148, D-4630, Bochum 1, Federal Republic of Germany.

PMID: 24318063 DOI: 10.1007/BF00388236

Abstract

Ribulose-1,5-bisphosphate carboxylase-oxygenase is deactivated by removal of Mg(++). The enzyme activities can be restored to a different extent by the addition of various divalent ions in the presence of CO2. Incubation with Mg(++) and CO2 restores both enzyme activities, whereas, the treatment of the enzyme with the transition metal ions (Mn(++), Co(++), and Ni(++)) and CO2 fully reactivates the oxygenase: however, the carboxylase activity remains low. In experiments where CO2-free conditions were conscientiously maintained, no reactivation of RuBP oxygenase was observed, although Mn(++) ions were present. Other divalent cations such as Ca(++) and Zn(++), restore neither the carboxylase nor the oxygenase reaction. Furthermore, the addition of Mn(++) to the Mg(++) and CO2 preactivated enzyme significantly inhibited carboxylase reactions, but increased the oxygenase reaction.

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