The Effect of Divalent Metal Ions on the Activity of Mg(++) Depleted Ribulose-1,5-bisphosphate Oxygenase

Overview

Journal Planta

Specialty Biology

Date 2013 Dec 10

PMID 24318063

Citations 5

Authors

G F Wildner

J Henkel

Affiliations

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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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