Initial steps in the fermentation of 3-hydroxybenzoate by Sporotomaculum hydroxybenzoicum.

The anaerobic bacterium Sporotomaculum hydroxybenzoicum ferments 3-hydroxybenzoate to acetate, butyrate, and CO2. 3-Hydroxybenzoate was activated to 3-hydroxybenzoyl-CoA in a CoA-transferase reaction with acetyl-CoA or butyryl-CoA as CoA donors. 3-Hydroxybenzoyl-CoA was reductively dehydroxylated, forming benzoyl-CoA. This reaction was measured in cell-free extracts with cob(I)alamin as low-potential electron donor. No evidence was obtained that cob(I)alamin is the physiological electron donor; however, inhibitor studies indicated involvement of a strong nucleophile in the reaction. Benzoate was degraded by dense cell suspensions without a lag phase until an in situ deltaG' value <-25 kJ mol(-1) was reached. Benzoyl-CoA reductase was not detected. Enzyme activities for all reaction steps from glutaryl-CoA to butyryl-CoA, and ATP formation via acetate kinase were detected in cell-free extracts. Glutaconyl-CoA decarboxylase is likely to act as a primary sodium ion pump.