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Articles

Enzyme Regulation in C₄ Photosynthesis ^1,2

PURIFICATION AND PROPERTIES OF THIOREDOXIN-LINKED NADP-MALATE DEHYDROGENASE FROM CORN LEAVES

F. Martin and J. Vidal

Section of Cell Physiology, Department of Plant and Soil Biology, University of California, Berkeley, California 94720, Laboratoire de Biologie Vegetale, Universite de Nancy I, 54037 Nancy-Cedex, France

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.

⁴ To whom correspondence regarding this paper should be addressed.

¹ This work was aided by grants from the Competitive Research Grants Office of the United States Department of Agriculture and the French Foreign Ministry.

² Second paper of a series, first paper is identified in Ref. 17.

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