Enzyme Regulation in C4 Photosynthesis
Authors:
- Bob B. BuchananBBBob B. Buchanan
- F. MartinFMF. Martin
- J. VidalJVJ. Vidal
Open Access
- 1 August 1981
- journal article
- Published by Oxford University Press (OUP) in Plant Physiology
- Vol. 68 (2) , 300-304
Abstract
NADP-malate dehydrogenase, a light-modulated enzyme of C4 photosynthesis, was purified to homogeneity from leaves of corn. The pure enzyme was activated by thioredoxin m that was reduced either photochemically (with ferredoxin and ferredoxin-thioredoxin reductase) or chemically (with dithiothreitol). Unactivated corn leaf NADP-malate dehydrogenase had a molecular weight of 50,000 to 60,000 and was chromophorefree. The enzyme appeared to have a high content of serine and glycine and to contain both S—S and SH groups. Consequently, NADP-malate dehydrogenase seems to be capable of undergoing reversible oxidation/reduction during its photoregulation.Keywords
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