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Applied and Environmental Microbiology, December 2006, p. 7821-7828, Vol. 72, No. 12
0099-2240/06/$08.00+0     doi:10.1128/AEM.01274-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Study of Biochemical Pathways and Enzymes Involved in Pyrene Degradation by Mycobacterium sp. Strain KMS

Yanna Liang,¹ Dale R. Gardner,² Charles D. Miller,³ Dong Chen,⁴ Anne J. Anderson,³ Bart C. Weimer,⁴ and Ronald C. Sims^5*

Department of Civil and Environmental Engineering, Utah State University, Logan, Utah 84322,¹ Poisonous Plant Research Laboratory, USDA, Logan, Utah 84341,² Department of Biology, Utah State University, Logan, Utah 84322,³ Center for Integrated Biosystems, Utah State University, Logan, Utah 84322,⁴ Department of Biological and Irrigation Engineering, Utah State University, Logan, Utah 84322⁵

Received 2 June 2006/ Accepted 5 October 2006

Pyrene degradation is known in bacteria. In this study, Mycobacterium sp. strain KMS was used to study the metabolites produced during, and enzymes involved in, pyrene degradation. Several key metabolites, including pyrene-4,5-dione, cis-4,5-pyrene-dihydrodiol, phenanthrene-4,5-dicarboxylic acid, and 4-phenanthroic acid, were identified during pyrene degradation. Pyrene-4,5-dione, which accumulates as an end product in some gram-negative bacterial cultures, was further utilized and degraded by Mycobacterium sp. strain KMS. Enzymes involved in pyrene degradation by Mycobacterium sp. strain KMS were studied, using 2-D gel electrophoresis. The first protein in the catabolic pathway, aromatic-ring-hydroxylating dioxygenase, which oxidizes pyrene to cis-4,5-pyrene-dihydrodiol, was induced with the addition of pyrene and pyrene-4,5-dione to the cultures. The subcomponents of dioxygenase, including the alpha and beta subunits, 4Fe-4S ferredoxin, and the Rieske (2Fe-2S) region, were all induced. Other proteins responsible for further pyrene degradation, such as dihydrodiol dehydrogenase, oxidoreductase, and epoxide hydrolase, were also found to be significantly induced by the presence of pyrene and pyrene-4,5-dione. Several nonpathway-related proteins, including sterol-binding protein and cytochrome P450, were induced. A pyrene degradation pathway for Mycobacterium sp. strain KMS was proposed and confirmed by proteomic study by identifying almost all the enzymes required during the initial steps of pyrene degradation.

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* Corresponding author. Mailing address: Department of Biological & Irrigation Engineering, 4105 Old Main Hill, Utah State University, Logan, UT 84322-4105. Phone: (435) 797-3156. Fax: (435) 797-1248. E-mail: rcsims{at}cc.usu.edu.

Published ahead of print on 13 October 2006.

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Applied and Environmental Microbiology, December 2006, p. 7821-7828, Vol. 72, No. 12
0099-2240/06/$08.00+0     doi:10.1128/AEM.01274-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Child, R., Miller, C. D., Liang, Y., Sims, R. C., Anderson, A. J. (2007). Pyrene Mineralization by Mycobacterium sp. Strain KMS in a Barley Rhizosphere. J. Environ. Qual. 36: 1260-1265 [Abstract] [Full Text]