Photoactivation and Regulation of Spinach Leaf Fructose 1,6-bisphosphatase

Abstract

Fructose 1,6-bisphosphatase, in isolated intact chloroplast from spinach leaves, is photoactivated by ferredoxin/thioredoxin system. The mechanism involved is conversion of enzyme disulfide to sulfhydryl groups as the photoactivation is inhibited by sulfhydryl group modifying agents which are able to penetrate the chloroplast envelope. Reduction of ferredoxin on the reducing side of photosystem I is found to be a key event and active electron flow to ferredoxin must be maintained for keeping the enzyme in activated state. DCMU - a classical electron transport chain inhibitor and other exogenously added electron acceptors, which intercept electrons on or before ferredoxin cause deactivation of fructose 1,6-bisphosphatase in light. The rate of deactivation, in dark, is also enhanced by exogenously added electron acceptors and sulfhydryl group modifying agents. The mechanism of regulation of fructose 1,6-bisphosphatase is discussed.