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• W1605251503 startingPage "3928" @default.
• W1605251503 abstract "The rotor subunit c of the A(1)A(O) ATP synthase of the hyperthermophilic archaeon Pyrococcus furiosus contains a conserved Na(+)-binding motif, indicating that Na(+) is a coupling ion. To experimentally address the nature of the coupling ion, we isolated the enzyme by detergent solubilization from native membranes followed by chromatographic separation techniques. The entire membrane-embedded motor domain was present in the preparation. The rotor subunit c was found to form an SDS-resistant oligomer. Under the conditions tested, the enzyme had maximal activity at 100 degrees C, had a rather broad pH optimum between pH 5.5 and 8.0, and was inhibited by diethystilbestrol and derivatives thereof. ATP hydrolysis was strictly dependent on Na(+), with a K(m) of 0.6 mM. Li(+), but not K(+), could substitute for Na(+). The Na(+) dependence was less pronounced at higher proton concentrations, indicating competition between Na(+) and H(+) for a common binding site. Moreover, inhibition of the ATPase by N',N'-dicyclohexylcarbodiimide could be relieved by Na(+). Taken together, these data demonstrate the use of Na(+) as coupling ion for the A(1)A(O) ATP synthase of Pyrococcus furiosus, the first Na(+) A(1)A(O) ATP synthase described." @default.
• W1605251503 created "2016-06-24" @default.
• W1605251503 creator A5015612352 @default.
• W1605251503 creator A5018631374 @default.
• W1605251503 creator A5060985234 @default.
• W1605251503 creator A5061802621 @default.
• W1605251503 date "2007-07-05" @default.
• W1605251503 modified "2023-09-27" @default.
• W1605251503 title "A sodium ion-dependent A1AO ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus" @default.
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• W1605251503 doi "https://doi.org/10.1111/j.1742-4658.2007.05925.x" @default.
• W1605251503 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17614964" @default.
• W1605251503 hasPublicationYear "2007" @default.
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