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ATP generation during reduced inorganic sulfur compound oxidation by Acidithiobacillus caldus is exclusively due to electron transport phosphorylation.
Umeå University.ORCID iD: 0000-0002-9622-3318
Umeå University.
University of Wales, Bangor, Gwynedd, UK.
2002 (English)In: Extremophiles, ISSN 1431-0651, E-ISSN 1433-4909, Vol. 6, no 2, p. 123-129Article in journal (Refereed) Published
Abstract [en]

The synthesis of adenosine 5-triphosphate (ATP) (increase in phosphorylation potential) during the oxidation of reduced inorganic sulfur compounds was studied in the moderately thermophilic acidophileAcidithiobacillus caldus (strain KU) (formerly Thiohacillus caldus). The phosphorylation potential increased during the oxidation of all reduced inorganic sulfur compounds tested compared with resting cells. The generation of ATP in whole cells was inhibited by the F0F1 ATPase inhibitor oligomycin, electron transport chain inhibitors, valinomycin and potassium ions. There was no increase in the phosphorylation potential, nor synthesis of ATP. in the absence of electron transport. An apparent lack of substrate-level phosphorylation was indicated by the lack of adenosine 5-phosphosulfate reductase in tetrathionate-grown At. caldus. Studies were also performed on the synthesis of ATP by membrane vesicles of At. caldus when presented with an artificial proton gradient. Complete inhibition of ATP synthesis in these vesicles occurred when they were loaded with N,N-dicyclohexylcarbodiimide (DCCD), but not when they were loaded with oligomycin, vanadate or electron transport chain inhibitors. The data presented here suggest that during the oxidation of reduced inorganic sulfur compounds by At. caldus, all ATP is synthesized by oxidative phosphorylation via a membrane-bound F0F1 ATPase driven by a proton gradient.

Place, publisher, year, edition, pages
2002. Vol. 6, no 2, p. 123-129
National Category
Microbiology
Research subject
Natural Science, Microbiology
Identifiers
URN: urn:nbn:se:lnu:diva-37320DOI: 10.1007/s007920100231ISI: 000175220800005PubMedID: 12013432OAI: oai:DiVA.org:lnu-37320DiVA, id: diva2:750348
Available from: 2014-09-29 Created: 2014-09-29 Last updated: 2017-12-05Bibliographically approved

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Dopson, Mark

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