Properties of a Wolinella succinogenes mutant lacking periplasmic sulfide dehydrogenase (Sud).
A delta 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 delta 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.
Kotzian
S
S
Institut für Mikrobiologie der J. W. Goethe-Universität, Frankfurt am Main, Germany.
Kreis-Kleinschmidt
V
V
Krafft
T
T
Klimmek
O
O
Macy
J M
JM
Kröger
A
A
D003574:Cytochrome c Group / Q000032:analysis*; D004579:Electron Transport; D009154:Mutation; D010088:Oxidoreductases / Q000032:analysis*; D013440:Sulfides / Q000378:metabolism; D016968:Wolinella / Q000201:enzymology* / Q000254:growth & development
D003574:Cytochrome c Group; D013440:Sulfides; C032915:polysulfide; D010088:Oxidoreductases; C064500:flavocytochrome c sulfide dehydrogenase