Properties of a Wolinella succinogenes mutant lacking periplasmic sulfide dehydrogenase (Sud)
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© Springer-Verlag 1996
S H O RT C O M M U N I C AT I O N
S. Kotzian · V. Kreis-Kleinschmidt · T. Krafft · O. Klimmek · J. M. Macy · A. Kröger
Properties of a Wolinella succinogenes mutant lacking periplasmic sulfide dehydrogenase (Sud)
Received: 31 August 1995 / Accepted: 25 October 1995
Abstract A ∆sud deletion mutant of Wolinella succinogenes that lacked the periplasmic sulfide dehydrogenase (Sud) was constructed using homologous recombination. The mutant grew with sulfide and fumarate, indicating that Sud was not a component of the electron transport chain that catalyzed fumarate respiration with sulfide as an electron donor. Likewise, growth with formate and either polysulfide or sulfur was not affected by the deletion. Removal of Sud from wild-type W. succinogenes by spheroplast formation did not decrease the activity of electron transport to polysulfide. The ∆psr deletion mutant that lacks polysulfide reductase (Psr) grew by fumarate respiration with sulfide as an electron donor, indicating that Psr is not required for this activity. Key words Sulfide dehydrogenase (Sud) · Polysulfide reduction · Fumarate respiration with sulfide · Wolinella succinogenes Abbreviations Psr Polysulfide reductase · Sud Sulfide dehydrogenase · kan Kanamycin resistance gene
Introduction While certain bacteria catalyze fumarate reduction by sulfide (reaction 1; Eisenmann et al. 1995), Wolinella succinogenes is the only organism known to grow at the expense of reaction 1 (Macy et al. 1986; Widdel 1988). HS– + Fumarate + H+ → S + Succinate
(1)
Dedicated to E. Mutschler, Frankfurt, on the occasion of his 65th birthday S. Kotzian · V. Kreis-Kleinschmidt · T. Krafft · O. Klimmek · J. M. Macy · A. Kröger (Y) Institut für Mikrobiologie der J.W. Goethe-Universität, Marie-Curie-Strasse 9, D-60439 Frankfurt am Main, Germany Tel. +49-69-798-29507; Fax +49-69-798-29527
The enzyme acting as sulfide dehydrogenase in the electron transport chain catalyzing reaction (1) in W. succinogenes has not yet been identified. Two enzymes that catalyze sulfide oxidation with an artificial electron acceptor have been isolated from W. succinogenes. The function of one of these enzymes, periplasmic sulfide dehydrogenase (Sud), is not known (Kreis-Kleinschmidt et al. 1995). To determine the function of Sud, a ∆sud mutant was constructed in this study and tested for growth at the expense of reaction (1) and also with polysulfide or elemental sulfur as the terminal electron acceptor. The membrane-integrated polysulfide reductase (Psr), the second enzyme that catalyzes sulfide oxidation with an artificial electron acceptor, has been identified as the terminal reductase in the electron transport chain catalyzing polysulfide reduction with formate (reaction 2) or H2 (Schröder et al. 1988; Klimmek et al. 1991; Fauque et al. 1994; Krafft et al. 1995). HCO2– + Sn2– → CO2 + HS– + S2– n–1
(2)
To determine whether Psr serves as a sulfide dehydrogenase in the catalysis of reaction (1), the (psr mutant (Krafft et al. 1995) was tested for growth with sulfide and fum
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