Enzymes of Naphthalene Metabolism by Pseudomonas fluorescens 26K Strain

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N. A. Leneva¹, M. P. Kolomytseva², B. P. Baskunov², and L. A. Golovleva^2*

¹Pushchino State University, pr. Nauki 3, 142292 Pushchino, Moscow Region, Russia

²G. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, pr. Nauki 5, 142292 Pushchino, Moscow Region, Russia; E-mail: golovleva@ibpm.pushchino.ru

^* To whom correspondence should be addressed.

Received November 3, 2009; Revision received December 17, 2009

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The ability of Pseudomonas fluorescens 26K strain to utilize naphthalene at concentrations up to 600 mg/liter as the sole source of carbon and energy in mineral liquid media was shown. Using HPLC, TLC, and mass-spectrometry, the intermediates of naphthalene transformation by this strain were identified as naphthalene cis-1,2-dihydrodiol, salicylaldehyde, salicylate, catechol, 2-hydroxymuconic semialdehyde, and 1-naphthol. Catechol 2,3-dioxygenase (a homotetramer with native molecular mass 125 kDa) and NAD⁺-dependent homohexameric naphthalene cis-1,2-dihydrodiol dehydrogenase with native molecular mass 160 kDa were purified from crude extract of the strain and characterized. NAD⁺-dependent homodimeric salicylaldehyde dehydrogenase with molecular mass 110 kDa was purified and characterized for the first time. Based on the data, a pathway of naphthalene degradation by P. fluorescens 26K is suggested.

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KEY WORDS: polyaromatic hydrocarbons, naphthalene, biodegradation, catechol 2,3-dioxygense, naphthalene cis-1,2-dihydrodiol dehydrogenase, salicylaldehyde dehydrogenase

DOI: 10.1134/S0006297910050044

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