A strictly anaerobic, benzoate-degrading bacterium, Syntrophus buswellii strain GA, was able to degrade benzoate or 3-phenylpropionate to acetate, CO2 and H-2, if the hydrogen partial pressure was sufficiently low. The hydrogen was removed in syntrophic coculture by Methanospirillum hungatei or by Desulfovibrio sp. through interspecies hydrogen transfer or in pure culture by the use of crotonate as reducible cosubstrate. Alternatively, S. buswellii strain GA could grow in pure culture with crotonate. Activities of seven catabolic enzymes were measured in crude cell extracts of S. buswellii strain GA grows with various substrates and of crotonate-grown S. buswellii strain DSM 2612A. Benzoate, 3-phenylpropionate and crotonate were activated by CoA ligases. Glutaryl-CoA dehydrogenase was found to be involved in the degradation of aromatic compounds and enzymes catalysing beta-oxidation were involved in the reaction sequence from crotonyl-CoA to acetate. A c-type cytochrome was present in the cytoplasm, whereas b-type cytochromes were associated with the membranes of both S. buswellii strains grown on crotonate. These indicated the presence of an electron-transport system. A high growth yield of crotonate-grown S. buswellii strain GA might be explained by electron-transport phosphorylation in addition to substrate-level phosphorylation.