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. 1981 Aug;68(2):300–304. doi: 10.1104/pp.68.2.300

Enzyme Regulation in C4 Photosynthesis 1,2

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

Jean-Pierre P Jacquot 1,2,3, Bob B Buchanan 1,2,4, F Martin 1,2, J Vidal 1,2
PMCID: PMC427479  PMID: 16661905

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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