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203 162 162 1 2 Christina Wallrabenstein Bernhard Schink +49-7531-882140 +49-7531-882966 ernhardschink@uni-konstanz.de Fakultät für Biologie Universität Konstanz Postfach 5560 D-78434 Konstanz Germany Abstract Syntrophomonas wolfei and Syntrophus buswellii were grown with butyrate or benzoate in a defined binary coculture with Methanospirillum hungatei . Both strains also grew independent of the partner bacteria with crotonate as substrate. Localization of enzymes involved in butyrate oxidation by S. wolfei revealed that ATP synthase, hydrogenase, and butyryl-CoA dehydrogenase were at least partially membrane-associated whereas 3-hydroxybutyryl-CoA dehydrogenase and crotonase were entirely cytoplasmic. Inhibition experiments with copper chloride indicated that hydrogenase faced the outer surface of the cytoplasmic membrane. Suspensions of butyrate-or benzoate-grown cells of either strain accumulated hydrogen during oxidation of butyrate or benzoate to a low concentration that was thermodynamically in equilibrium with calculated reaction energetics. The protonophore carbonylcyanide m -chlorophenyl-hydrazone (CCCP) and the proton-translocating ATPase inhibitor N,N′ dicyclohexylcarbodiimide (DCCD) both specifically inhibited hydrogen formation from butyrate or benzoate at low concentrations, whereas hydrogen formation from crotonate was not affected. A menaquinone was extracted from cells of S. wolfei and S. buswellii grown syntrophically in a binary methanogenic culture. The results indicate that a proton-potential-driven process is involved in hydrogen release from butyrate or benzoate oxidation.
Archives of Microbiology – Springer Journals
Published: Jul 1, 1994
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