Abstract
HIGHLY purified ‘malic’ enzyme from pigeon's liver1 mediates a fixation of carbon dioxide through catalysis of reaction (1). When, by coupling with a suitable dehydrogenase system, triphosphopyridine nucleotide is continuously reconverted to its reduced form, malate is readily synthesized from pyruvate and carbon dioxide2. Should illuminated chloroplast preparations be able to effect a reduction of pyridine nucleotides, then the photochemical reaction could be coupled to reductive carbon dioxide fixation by a well-defined enzyme system2,3. Such a mechanism might operate in photosynthesis. A ‘malic’ enzyme specific for triphosphopyridine nucleotide is present in the tissues of higher plants4. 
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References
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Tolmach, L. J. (University of Chicago), has recently observed that a photochemical oxygen evolution occurring in spinach juice is stimulated by triphosphopyridine nucleotide (personal communication by Dr. H. Gaffron). This is in agreement with the findings reported here.
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VISHNIAC, W., OCHOA, S. Photochemical Reduction of Pyridine Nucleotides by Spinach Grana and Coupled Carbon Dioxide Fixation. Nature 167, 768–769 (1951). https://doi.org/10.1038/167768a0
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DOI: https://doi.org/10.1038/167768a0
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