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Applied and Environmental Microbiology, June 1999, p. 2691-2696, Vol. 65, No. 6
School of Biological Sciences, The University
of Birmingham, Edgbaston, Birmingham B15 2TT, United
Kingdom,1 and Institute of Microbiology,
Russian Academy of Sciences, Moscow 117811, Russia2
Received 12 November 1998/Accepted 24 March 1999
Resting cells of Desulfovibrio desulfuricans coupled
the oxidation of a range of electron donors to Tc(VII) reduction. The reduced technetium was precipitated as an insoluble low-valence oxide.
The optimum electron donor for the biotransformation was hydrogen,
although rapid rates of reduction were also supported when formate or
pyruvate was supplied to the cells. Technetium reduction was less
efficient when the growth substrates lactate and ethanol were
supplied as electron donors, while glycerol, succinate, acetate, and
methanol supported negligible reduction. Enzyme activity was stable for
several weeks and was insensitive to oxygen. Transmission electron
microscopy showed that the radionuclide was precipitated at the
periphery of the cell. Cells poisoned with Cu(II), which is selective
for periplasmic but not cytoplasmic hydrogenases, were unable to reduce
Tc(VII), a result consistent with the involvement of a periplasmic
hydrogenase in Tc(VII) reduction. Resting cells, immobilized in a
flowthrough membrane bioreactor and supplied with Tc(VII)-supplemented
solution, accumulated substantial quantities of the radionuclide when
formate was supplied as the electron donor, indicating the potential of
this organism as a biocatalyst to treat Tc-contaminated wastewaters.
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Reduction of Technetium by Desulfovibrio
desulfuricans: Biocatalyst Characterization and Use in a
Flowthrough Bioreactor
*
Corresponding author. Present address: Department of
Microbiology, 203 Morrill Science Center IVN, University of
Massachusetts, Amherst, MA 01003. Phone: (413) 545-9651. Fax: (413)
545-1578. E-mail: jrlloyd{at}microbio.umass.edu.
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