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Journal of Bacteriology, April 2004, p. 2156-2163, Vol. 186, No. 7
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.7.2156-2163.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Selenocysteine-Containing Proteins in Anaerobic Benzoate Metabolism of Desulfococcus multivorans

Franziska Peters,¹ Michael Rother,^2, and Matthias Boll^1*

Institut für Biologie II, Albert-Ludwigs-Universität, Freiburg,¹ Mikrobiologie, Department für Biologie I, Ludwig-Maximilians-Universität, Munich, Germany²

Received 29 July 2003/ Accepted 11 December 2003

The sulfate-reducing bacterium Desulfococcus multivorans uses various aromatic compounds as sources of cell carbon and energy. In this work, we studied the initial steps in the aromatic metabolism of this strictly anaerobic model organism. An ATP-dependent benzoate coenzyme A (CoA) ligase (AMP plus PP_i forming) composed of a single 59-kDa subunit was purified from extracts of cells grown on benzoate. Specific activity was highest with benzoate and some benzoate derivatives, whereas aliphatic carboxylic acids were virtually unconverted. The N-terminal amino acid sequence showed high similarities with benzoate CoA ligases from Thauera aromatica and Azoarcus evansii. When cultivated on benzoate, cells strictly required selenium and molybdenum, whereas growth on nonaromatic compounds, such as cyclohexanecarboxylate or lactate, did not depend on the presence of the two trace elements. The growth rate on benzoate was half maximal with 1 nM selenite present in the growth medium. In molybdenum- and/or selenium-depleted cultures, growth on benzoate could be induced by addition of the missing trace elements. In extracts of cells grown on benzoate in the presence of [⁷⁵Se]selenite, three radioactively labeled proteins with molecular masses of 100, 30, and 27 kDa were detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. The 100- and 30-kDa selenoproteins were 5- to 10-fold induced in cells grown on benzoate compared to cells grown on lactate. These results suggest that the dearomatization process in D. multivorans is not catalyzed by the ATP-dependent Fe-S enzyme benzoyl-CoA reductase as in facultative anaerobes but rather involves unknown molybdenum- and selenocysteine-containing proteins.

Present address: Department of Microbiology, University of Illinois, Urbana-Champaign, Ill.

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