PMID:9683642
| Citation |
Dimroth, P and Schink, B (1998) Energy conservation in the decarboxylation of dicarboxylic acids by fermenting bacteria. Arch. Microbiol. 170:69-77 |
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| 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 malonate, succinate, and glutarate fermentation) by membrane-bound primary decarboxylase sodium ion pumps into an electrochemical gradient of sodium ions across the membrane; or, alternatively, an electrochemical proton gradient can be established by the combined action of a soluble decarboxylase with a dicarboxylate/monocarboxylate antiporter (in oxalate and malate fermentation). The thus generated electrochemical Na+ or H+ gradients are then exploited for ATP synthesis by Na+- or H+-coupled F1F0 ATP synthases. This new type of energy conservation has been termed decarboxylation phosphorylation and is responsible entirely for ATP synthesis in several anaerobic bacteria. |
| Links | |
| Keywords |
Adenosine Triphosphate/metabolism; Bacteria, Anaerobic/physiology; Carboxy-Lyases/metabolism; Decarboxylation; Dicarboxylic Acids/metabolism; Electron Transport/physiology; Electrophysiology; Energy Metabolism/physiology; Fermentation/physiology; Propionibacterium/metabolism; Sodium-Potassium-Exchanging ATPase/physiology |
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