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J Bacteriol. 1968 November; 96(5): 1640-1648
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Autotrophy in Nitrosocystis oceanus¹

^a Woods Hole Oceanographic Institution, Woods Hole, Massachusetts 02543

ABSTRACT

Enzymatic assays of cell-free extracts of the ammonia-oxidizing bacterium Nitrosocystis oceanus failed to establish that the biochemical basis of its obligate autotrophy stemmed solely from a metabolic defect. All of the Embden-Meyerhof enzymes except phosphofructokinase, and all of the tricarboxylic acid-cycle enzymes, as well as reduced nicotinamide adenine dinucleotide oxidase, were found in these extracts. A phosphoenolpyruvate-CO²-fixing system was also demonstrated. Resting cells incubated with ¹⁴C-D-glucose and ¹⁴C-L-glutamate and cells grown in the presence of ¹⁴C-labeled glucose, glutamate, pyruvate, and methionine incorporated these compounds into cellular material, but at a level too low to provide the cells' major carbon and energy needs.

² Present address: Department of Oceanography, The University, Southampton, England.

¹ Contribution no. 2150 from the Woods Hole Oceanographic Institution, Woods Hole, Mass. 02543.