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Plant Physiology 90:788-791 (1989)
© 1989 American Society of Plant Biologists

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Metabolism and Enzymology

Localization of the Enzymes Involved in the Photoevolution of H2 from Acetate in Chlamydomonas reinhardtii1

Kenneth O. Willeford and Martin Gibbs

Institute for Photobiology of Cells and Organelles, Brandeis University, Waltham, Massachusetts 02254

The localization of a series of enzymes involved in the anaerobic photodissimilation of acetate in Chlamydomonas reinhardtii F-60 adapted to a hydrogen metabolism was determined through the enzymic analyses of the chloroplastic, cytoplasmic, and mitochondrial fractions obtained with a cellular fractionation procedure that incorporated cell wall removal by treatment with autolysine, digestion of the plasmalemma with the detergent digitonin, and fractionation by differential centrifugation on a Percoll step gradient. The sequence of events leading to the photoevolution of H2 from acetate includes the conversion of acetate into succinate via the extraplastidic glyoxylate cycle, the oxidation of succinate to fumarate by chloroplastic succinate dehydrogenase, and the oxidation of malate to oxaloacetate in the chloroplast by NAD dependent malate dehydrogenase. The level of potential activity for the enzymes assayed were sufficient to accommodate the observed rate of the photoanaerobic dissimilation of acetate and the photoevolution of H2.

1 Supported by the U.S. Department of Energy DE-ACO2-76-ERO 3231.




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M. Berkemeyer, R. Scheibe, and O. Ocheretina
A Novel, Non-redox-regulated NAD-dependent Malate Dehydrogenase from Chloroplasts of Arabidopsis thaliana L.
J. Biol. Chem., October 23, 1998; 273(43): 27927 - 27933.
[Abstract] [Full Text] [PDF]


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Copyright © 1989 by the American Society of Plant Biologists