Abstract
Glucose-6-phosphate dehydrogenase from intact pea chloroplasts is partially membrane bound and inactivated upon illumination. The inhibitory effect of light can be abolished by addition of methylviologen. Kinetic experiments with glucose-6-phosphate dehydrogenase reveal that, in the dark, the enzyme activity is strongly inhibited by the accumulation of NADPH. The inhibition of NADPH can be reversed by the addition of excess NADP+. The non-Michaelis-Menten-type kinetics suggest that the enzyme is stringently regulated by the ratio of NADPH to NADP+ plus NADPH, i.e., the "reduction charge". These observations seem to indicate that in the light the inhibition of glucose-6-phosphate dehydrogenase is due to a high reduction charge, whereas in the dark the enzyme is controlled by the metabolic demand for reducing equivalents.
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Schedule a callMore From: Zeitschrift fur Naturforschung. Section C, Biosciences
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