Properties of a Wolinella succinogenes mutant lacking periplasmic sulfide dehydrogenase (Sud) |
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Authors: | S Kotzian V Kreis-Kleinschmidt T Krafft O Klimmek J M Macy A Kröger |
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Institution: | Institut für Mikrobiologie der J.W. Goethe-Universit?t, Marie-Curie-Strasse 9, D-60439 Frankfurt am Main, Germany Tel. +49-69-798-29507; Fax +49-69-798-29527, DE
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Abstract: | A Δsud 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 Δpsr 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.
Received: 31 August 1995 / Accepted: 25 October 1995 |
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Keywords: | Sulfide dehydrogenase (Sud) Polysulfide reduction Fumarate respiration with sulfide Wolinella succinogenes |
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