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Life by a new decarboxylation-dependent energy conservation mechanism with Na+ as coupling ion

Life by a new decarboxylation-dependent energy conservation mechanism with Na+ as coupling ion

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HILPERT, Wilhelm, Bernhard SCHINK, Peter DIMROTH, 1984. Life by a new decarboxylation-dependent energy conservation mechanism with Na+ as coupling ion. In: The EMBO Journal. 3(8), pp. 1665-1670

@article{Hilpert1984decar-8154, title={Life by a new decarboxylation-dependent energy conservation mechanism with Na+ as coupling ion}, year={1984}, number={8}, volume={3}, journal={The EMBO Journal}, pages={1665--1670}, author={Hilpert, Wilhelm and Schink, Bernhard and Dimroth, Peter} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/8154"> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:41:01Z</dcterms:available> <dc:creator>Hilpert, Wilhelm</dc:creator> <dcterms:bibliographicCitation>First publ. in: The EMBO Journal 3 (1984), 8, pp. 1665-1670</dcterms:bibliographicCitation> <dcterms:issued>1984</dcterms:issued> <dc:language>eng</dc:language> <dcterms:title>Life by a new decarboxylation-dependent energy conservation mechanism with Na+ as coupling ion</dcterms:title> <dc:contributor>Schink, Bernhard</dc:contributor> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:format>application/pdf</dc:format> <dc:creator>Schink, Bernhard</dc:creator> <dc:creator>Dimroth, Peter</dc:creator> <dcterms:abstract xml:lang="eng">We report here a new mode of ATP synthesis in living cells. The anaerobic bacterium Propionigenium modestum gains its total energy for growth from the conversion of succinate to propionate according to: succinate + H20 → propionate + HCO3 - (AGOI = -20.6 kJ/mol). The small free energy change of this reaction does not allow a substrate-linked phosphorylation mechanism, and no electron transport phosphorylation takes place. Succinate was degraded by cell-free extracts to propionate and CO2 via succinyl-CoA, methylmalonyl- CoA and propionyl-CoA. This pathway involves a membrane-bound methylmalonyl-CoA decarboxylase which couples the exergonic decarboxylation with a Na + ion transport across the membrane. The organism also contained a membrane-bound ATPase which was specifically activated by Na + ions and catalyzed the transport of Na + ions into inverted bacterial vesicles upon ATP hydrolysis. The transport was abolished by monensin but not by the uncoupler carbonylcyanide- p-trifluoromethoxy phenylhydrazone. Isolated membrane vesicles catalyzed the synthesis of ATP from ADP and inorganic phosphate when malonyl-CoA was decarboxylated and malonyl-CoA synthesis from acetyl-CoA when ATP was hydrolyzed. These syntheses were sensitive to monensin which indicates that Na + functions as the coupling ion. We conclude from these results that ATP synthesis in P. modestum is driven by a Na + ion gradient which is generated upon decarboxylation of methylmalonyl-CoA.</dcterms:abstract> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8154"/> <dc:contributor>Hilpert, Wilhelm</dc:contributor> <dc:contributor>Dimroth, Peter</dc:contributor> <dc:rights>deposit-license</dc:rights> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:41:01Z</dc:date> </rdf:Description> </rdf:RDF>

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