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Applied and Environmental Microbiology, September 2001, p. 3958-3963, Vol. 67, No. 9
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.9.3958-3963.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Energy Yield of Respiration on Chloroaromatic Compounds in Desulfitobacterium dehalogenans

Bram A. van de Pas,1 Stefan Jansen,1 Cor Dijkema,2 Gosse Schraa,1 Willem M. de Vos,1 and Alfons J. M. Stams1,*

Laboratory of Microbiology, Wageningen University, 6703 CT Wageningen,1 and Laboratory of Molecular Physics, Wageningen University, 6703 HA Wageningen,2 The Netherlands

Received 11 December 2000/Accepted 27 June 2001

The amount of energy that can be conserved via halorespiration by Desulfitobacterium dehalogenans JW/IU-DC1 was determined by comparison of the growth yields of cells grown with 3-chloro-4-hydroxyphenyl acetate (Cl-OHPA) and different electron donors. Cultures that were grown with lactate, pyruvate, formate, or hydrogen as an electron donor and Cl-OHPA as an electron acceptor yielded 3.1, 6.6, 1.6, and 1.6 g (dry weight) per mol of reduction equivalents, respectively. Fermentative growth on pyruvate yielded 14 g (dry weight) per mol of pyruvate oxidized. Pyruvate was not fermented stoichiometrically to acetate and lactate, but an excess of acetate was produced. Experiments with 13C-labeled bicarbonate showed that during pyruvate fermentation, approximately 9% of the acetate was formed from the reduction of CO2. Comparison of the growth yields suggests that 1 mol of ATP is produced per mol of acetate produced by substrate-level phosphorylation and that there is no contribution of electron transport phosphorylation when D. dehalogenans grows on lactate plus Cl-OHPA or pyruvate plus Cl-OHPA. Furthermore, the growth yields indicate that approximately 1/3 mol of ATP is conserved per mol of Cl-OHPA reduced in cultures grown in formate plus Cl-OHPA and hydrogen plus Cl-OHPA. Because neither formate nor hydrogen nor Cl-OHPA supports substrate-level phosphorylation, energy must be conserved through the establishment of a proton motive force. Pyruvate ferredoxin oxidoreductase, lactate dehydrogenase, formate dehydrogenase, and hydrogenase were localized by in vitro assays with membrane-impermeable electron acceptors and donors. The orientation of chlorophenol-reductive dehalogenase in the cytoplasmic membrane, however, could not be determined. A model is proposed, which may explain the topology analyses as well as the results obtained in the yield study.

* Corresponding author. Mailing address: Laboratory of Microbiology, Wageningen University, Hesselink van Suchtelenweg 4, NL-6703 CT Wageningen, The Netherlands. Phone: 31-(0)-317483101. Fax: 31-(0)-317483829. E-mail: Fons.stams{at}algemeen.micr.wag-ur.nl.

Applied and Environmental Microbiology, September 2001, p. 3958-3963, Vol. 67, No. 9
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.9.3958-3963.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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