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

Hilpert, Wilhelm; Schink, Bernhard; Dimroth, Peter

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

Dateien

Life_by_a_new_decarboxylation_dependent_energy_conservation.pdfGröße: 1.18 MBDownloads: 564

Datum

1984

Autor:innen

Hilpert, Wilhelm

Schink, Bernhard

Dimroth, Peter

URI (zitierfähiger Link)

http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-26848

Link zur Lizenz

Attribution-NonCommercial-NoDerivs 2.0 Generic

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

The EMBO Journal. 1984, 3(8), pp. 1665-1670

Zusammenfassung

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.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

ATP synthesis, Propionigenium modestum, Na + ions, methylmalonyl CoA, decarboxylation

Zitieren

ISO 690

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. 1984, 3(8), pp. 1665-1670

BibTex

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

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    <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>
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Universitätsbibliographie

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