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Orthophosphite-Nicotinamide Adenine Dinucleotide Oxidoreductase from Pseudomonas fluorescens

^a Department of Bacteriology, Indiana University, Bloomington, Indiana 47405

ABSTRACT

Information was obtained on the general properties and specificity of orthophosphite-nicotinamide adenine dinucleotide oxidoreductase. The enzyme was extracted from Pseudomonas fluorescens 195 grown in medium containing orthophosphite as the sole source of phosphorus. An enzyme preparation suitable for characterization was obtained from crude extracts by use of high-speed centrifugation, protamine sulfate precipitation, ammonium sulfate fractionation, and Sephadex gel filtration. The enzyme exhibited maximal activity at pH 7.0, and was inactivated within 6 min at 37 C. Arsenite, hypophosphite, nitrite, selenite, and tellurite were not oxidized by the enzyme. Sulfite inhibited the enzymatic oxidation of orthophosphite in an apparent competitive manner.

¹ Present address: Department of Biochemistry, University of Washington, Seattle 98105.

² Present address: Division of Biological Sciences, University of Maryland Baltimore County. Baltimore 21228.

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