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Plant Physiology 77:571-577 (1985)
© 1985 American Society of Plant Biologists

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Articles

Purification and Characterization of the Pea Chloroplast Pyruvate Dehydrogenase Complex 1

A Source of Acetyl-CoA and NADH for Fatty Acid Biosynthesis

Pamela J. Camp2 and Douglas D. Randall

Department of Biochemistry, University of Missouri, Columbia, Missouri 65211

The pyruvate dehydrogenase complex has been purified 76-fold, to a specific activity of 0.6 µmoles per minute per milligram protein, beginning with isolated pea (Pisum sativum L. var Little Marvel) chloroplasts. Purification was accomplished by rate zonal sedimentation, polyethyleneglycol precipitation, and ethyl-agarose affinity chromatography. Characterization of the substrates as pyruvate, NAD+, and coenzyme-A and the products as NADH, CO2, and acetyl-CoA, in a 1:1:1 stoichiometry unequivocally established that activity was the result of the pyruvate dehydrogenase complex. Immunochemical analysis demonstrated significant differences in structure and organization between the chloroplast pyruvate dehydrogenase complex and the more thoroughly characterized mitochondrial complex. Chloroplast complex has a higher magnesium requirement and a more alkaline pH optimum than mitochondrial complex, and these properties are consistent with light-mediated regulation in vivo. The chloroplast pyruvate dehydrogenase complex is not, however, regulated by ATP-dependent inactivation. The properties and subcellular localization of the chloroplast pyruvate dehydrogenase complex are consistent with its role of providing acetyl-CoA and NADH for fatty acid synthesis.

2 Present address: Biology Department, University of Dayton, 300 College Park, Dayton, OH 45469.

1 Supported by National Science Foundation Grant PCM-8104659. This is journal report No. 9690 from the Missouri Stae Agricultural Experiment Station.




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