1998
DOI: 10.1007/s002030050616
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Energy conservation in the decarboxylation of dicarboxylic acids by fermenting bacteria

Abstract: Decarboxylation of dicarboxylic acids (oxalate, malonate, succinate, glutarate, and malate) can serve as the sole energy source for the growth of fermenting bacteria. Since the free energy change of a decarboxylation reaction is small (around -20 kJ per mol) and equivalent to only approximately one-third of the energy required for ATP synthesis from ADP and phosphate under physiological conditions, the decarboxylation energy cannot be conserved by substrate-level phosphorylation. It is either converted (in mal… Show more

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Cited by 125 publications
(96 citation statements)
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“…It can be hypothesized that the decarboxylase in S. hydroxybenzoicum generates a Na + ion motive force as well. This would be equivalent to 1/3 mol ATP per mol substrate converted (Dimroth and Schink 1998). There is no evidence for any additional means of energy conservation in S. hydroxybenzoicum.…”
Section: Benzoyl-coa Metabolism In S Hydroxybenzoicummentioning
confidence: 96%
“…It can be hypothesized that the decarboxylase in S. hydroxybenzoicum generates a Na + ion motive force as well. This would be equivalent to 1/3 mol ATP per mol substrate converted (Dimroth and Schink 1998). There is no evidence for any additional means of energy conservation in S. hydroxybenzoicum.…”
Section: Benzoyl-coa Metabolism In S Hydroxybenzoicummentioning
confidence: 96%
“…strain CIB (29). In some organisms of limited energetic budget, such as fermenting bacteria, glutaryl-CoA is oxidized by a NAD-dependent glutaryl-CoA dehydrogenase and then decarboxylated by the action of a membrane-bound multicomponent glutaconylCoA decarboxylase, which is sodium dependent and couples decarboxylation with the translocation of a sodium ion across the membrane, leading to ATP synthesis (89). The conversion of glutaryl-CoA to crotonyl-CoA with the formation of ATP can be regarded as an additional means of energy conservation imposed by the strict energy constraints of syntrophic metabolism (107,328).…”
Section: Benzoate Catabolism: the Benzoyl-coa Degradation Pathwaymentioning
confidence: 99%
“…The same cluster harbors two genes (Cf_2063 and Cf_2079) with coding homology to several thiamine pyrophosphate-requiring enzymes, including oxalyl-CoA decarboxylases. In the anaerobic bacterium Oxalobacter formigenes, which belongs to the same family as Collimonas, the net activity of these activities (that is oxalate in, formate out) generates a proton gradient from which the bacterium derives energy (Anantharam et al, 1989;Dimroth and Schink, 1998). Downstream of Cf_2063 are four genes (Cf_2064-2067) that code for the a-, b-, g-and d-subunits of an NAD-dependent formate dehydrogenase (Oh and Bowien, 1998).…”
Section: Carbon and Energy Metabolismmentioning
confidence: 99%