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Anaerobic degradation of 3-aminobenzoate by a newly isolated sulfate reducer and a methanogenic enrichment culture
Author(s) -
Sylvia Schnell,
Bernhard Schink
Publication year - 1992
Publication title -
archives of microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.648
H-Index - 102
eISSN - 1432-072X
pISSN - 0302-8933
DOI - 10.1007/bf00245361
Subject(s) - thiosulfate , sulfite , chemistry , sulfide , electron acceptor , sulfate , hydrogenase , enrichment culture , methanogenesis , nuclear chemistry , biochemistry , sulfur , stereochemistry , bacteria , organic chemistry , enzyme , biology , methane , genetics
A new rod-shaped, gram-negative, non-sporing sulfate reducer, strain mAB1, was enriched and isolated from marine sediment samples with 3-aminobenzoate as sole electron and carbon source. Strain mAB1 degraded 3-aminobenzoate completely to CO2 and NH3 with stoichiometric reduction of sulfate to sulfide. Cells contained carbon monoxide dehydrogenase, cytochromes, and sulfite reductase P582. Strain mAB1 degraded also benzoate, 4-aminobenzoate, hydroxybenzoates, and some aliphatic compounds. Besides sulfates, also sulfite was reduced with 3-aminobenzoate as electron donor, but not thiosulfate, sulfur, nitrate, or fumarate. The strain grew in sulfide-reduced mineral medium supplemented with 7 vitamins. Strain mAB1 was tentatively affiliated with the genus Desulfobacterium. Experiments with dense cell supsensions showed benzoate accumulation during 3-aminobenzoate degradation under conditions of sulfate limitation or cyanide inhibition. 3-Aminobenzoate was activated to 3-aminobenzoyl-CoA by cell extracts in the presence of ATP, coenzyme A, and Mg2+. Acitivity of 3-aminobenzoyl-CoA synthetase was 16 nmol per min and mg protein, with a KM for 3-aminobenzoate lower than 50 µM. Cell extract of 3-aminobenzoate-grown cells activated also 3-hydroxybenzoate (31.7 nmol per min and mg protein) and benzoate (2.3 nmol per min and mg protein), but not 2-aminobenzoate or 4-aminobenzoate. In the presence of NADH of NADPH, 3-aminobenzoyl-CoA was further metabolized to a not yet identified reduced product.

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