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. 1968 Nov;96(5):1640–1648. doi: 10.1128/jb.96.5.1640-1648.1968

Autotrophy in Nitrosocystis oceanus1

Peter J leb Williams a,2, Stanley W Watson a
PMCID: PMC315222  PMID: 5726306

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.

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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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