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Journal of Bacteriology, August 2002, p. 4343-4350, Vol. 184, No. 16
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.16.4343-4350.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Roles for the Two 1-Butanol Dehydrogenases of Pseudomonas butanovora in Butane and 1-Butanol Metabolism

Department of Biochemistry and Biophysics,¹ Department of Botany and Plant Pathology, Oregon State University, Corvallis, Oregon 97331-2902²

Received 18 March 2002/ Accepted 12 May 2002

Pseudomonas butanovora grown on butane or 1-butanol expresses two 1-butanol dehydrogenases, a quinoprotein (BOH) and a quinohemoprotein (BDH). BOH exhibited high affinity towards 1-butanol (K_m = 1.7 ± 0.2 µM). BOH also oxidized butyraldehyde and 2-butanol (K_m = 369 ± 85 µM and K_m = 662 ± 98 µM, respectively). The mRNA induction profiles of BOH and BDH at three different levels of 1-butanol, a nontoxic level (0.1 mM), a growth-supporting level (2 mM), and a toxic level (40 mM), were similar. When cells were grown in citrate-containing medium in the presence of different levels of 1-butanol, wild-type P. butanovora could tolerate higher levels of 1-butanol than the P. butanovora boh::tet strain and the P. butanovora bdh::kan strain. A model is proposed in which the electrons from 1-butanol oxidation follow a branched electron transport chain. BOH may be coupled to ubiquinone, with the electrons being transported to a cyanide-sensitive terminal oxidase. In contrast, electrons from BDH may be transferred to a terminal oxidase that is less sensitive to cyanide. The former pathway may function primarily in energy generation, while the latter may be more important in the detoxification of 1-butanol.

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