Energy conservation by oxidation of formate to carbon dioxide and hydrogen via a sodium ion current in a hyperthermophilic archaeon
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Title
- Energy conservation by oxidation of formate to carbon dioxide and hydrogen via a sodium ion current in a hyperthermophilic archaeon
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Author(s)
- Lim, Jae Kyu; Mayer, Florian; Kang, Sung Gyun; Mueller, Volker
- KIOST Author(s)
- Lim, Jae Kyu(임재규); Kang, Sung Gyun(강성균)
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Alternative Author(s)
- 임재규; 강성균
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Publication Year
- 2014-08-05
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Abstract
- Thermococcus onnurineus NA1 is known to grow by the anaerobic oxidation of formate to CO2 and H-2, a reaction that operates near thermodynamic equilibrium. Here we demonstrate that this reaction is coupled to ATP synthesis by a transmembrane ion current. Formate oxidation leads to H+ translocation across the cytoplasmic membrane that then drives Na+ translocation. The ion-translocating electron transfer system is rather simple, consisting of only a formate dehydrogenase module, a membrane-bound hydrogenase module, and a multisubunit Na+/H+ antiporter module. The electrochemical Na+ gradient established then drives ATP synthesis. These data give a mechanistic explanation for chemiosmotic energy conservation coupled to formate oxidation to CO2 and H-2. Because it is discussed that the membrane-bound hydrogenase with the Na+/H+ antiporter module are ancestors of complex I of mitochondrial and bacterial electron transport these data also shed light on the evolution of ion transport in complex I-like electron transport chains.
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ISSN
- 0027-8424
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URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/2749
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DOI
- 10.1073/pnas.1407056111
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Bibliographic Citation
- PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.111, no.31, pp.11497 - 11502, 2014
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Publisher
- NATL ACAD SCIENCES
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Subject
- RESPIRATORY COMPLEX-I; CONVERTING NIFE HYDROGENASES; THERMOCOCCUS-ONNURINEUS NA1; SEA HYDROTHERMAL VENT; H-2 PRODUCTION; METHANOGENIC ARCHAEA; METHANOSARCINA-MAZEI; PYROCOCCUS-FURIOSUS; ANAEROBIC-BACTERIA; MODULAR EVOLUTION
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Keywords
- ATP synthase; proton potential; sodium ion potential; bioenergetics
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Type
- Article
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Language
- English
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Document Type
- Article
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