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Enzymes of Naphthalene Metabolism by Pseudomonas fluorescens 26K Strain

N. A. Leneva1, M. P. Kolomytseva2, B. P. Baskunov2, and L. A. Golovleva2*

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

DOI: 10.1134/S0006297910050044