Open AccessEnergy conservation in fermentative glutarate degradation by the bacterial strain WoGl3
Author(s) -
Matthies Carola,
Schink Bernhard
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb14044.x
Subject(s) - fermentation , enzyme , chemistry , strain (injury) , sodium , substrate (aquarium) , biochemistry , bacteria , energy source , biology , organic chemistry , coal , ecology , genetics , anatomy
Dicarboxylic acids with 2–5 carbon atoms can be degraded fermentatively by pure cultures of various strictly anaerobic bacteria. The small amount of free energy released in these decarboxylations (about 20–25 kJ mol −1 ) is conserved as sole source of growth energy either through sodium‐pumping decarboxylases or through electrogenic substrate/product transport devices. In the glutarate‐fermenting bacterial strain WoGl3 a glutaconyl‐CoA‐decarboxylating enzyme activity was detected. This enzyme was inhibited by avidin and was stimulated by sodium ions. The enzyme activity was partially associated with the cytoplasmic membrane, indicating that energy conservation is accomplished through a sodium‐ion‐pumping glutaconyl‐CoA decarboxylase enzyme.