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Journal of Bacteriology, March 2001, p. 1727-1733, Vol. 183, No. 5
Fachbereich Biologie, Universität
Konstanz, D-78457 Konstanz,1 and
Max-Planck-Institut für Terrestrische Mikrobiologie,
D-35043 Marburg,2 Germany
Received 16 June 2000/Accepted 6 December 2000
A dissimilatory sulfite reductase (DSR) was purified from
the anaerobic, taurine-degrading bacterium Bilophila
wadsworthia RZATAU to apparent homogeneity. The enzyme is
involved in energy conservation by reducing sulfite, which is
formed during the degradation of taurine as an electron acceptor, to
sulfide. According to its UV-visible absorption spectrum with
maxima at 392, 410, 583, and 630 nm, the enzyme belongs to the
desulfoviridin type of DSRs. The sulfite reductase was isolated as an
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.5.1727-1733.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Dissimilatory Sulfite Reductase (Desulfoviridin) of the
Taurine-Degrading, Non-Sulfate-Reducing Bacterium Bilophila
wadsworthia RZATAU Contains a Fused DsrB-DsrD
Subunit
2
2
n
(n
2) multimer with a native size of 285 kDa as
determined by gel filtration. We have sequenced the genes encoding the
and
subunits (dsrA and dsrB,
respectively), which probably constitute one operon. dsrA
and dsrB encode polypeptides of 49 (
) and 54 kDa (
)
which show significant similarities to the homologous subunits of other DSRs. The dsrB gene product of B. wadsworthia
is apparently a fusion protein of dsrB and
dsrD. This indicates a possible functional role of DsrD in
DSR function because of its presence as a fusion protein as an integral
part of the DSR holoenzyme in B. wadsworthia. A
phylogenetic analysis using the available Dsr sequences revealed that
B. wadsworthia grouped with its closest 16S rDNA
relative Desulfovibrio desulfuricans Essex 6.
*
Corresponding author. Mailing address: Fachbereich
Biologie, Universität Konstanz, Universitätsstr.
10, D-78457 Konstanz, Germany. Phone: 7531 88 4385. Fax: 7531 88 29 66. E-mail: heike_laue{at}hotmail.com.
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