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dc.contributor.authorSato, Motoakies_ES
dc.contributor.authorSinha, Prem Kumares_ES
dc.contributor.authorTorres-Bacete, Jesúses_ES
dc.contributor.authorMatsuno-Yagi, Akemies_ES
dc.contributor.authorYagi, Takaoes_ES
dc.date.accessioned2017-09-13T08:11:05Z-
dc.date.available2017-09-13T08:11:05Z-
dc.date.issued2013-08-23-
dc.identifier.citationJ Biol Chem. 288(34):24705-16 (2013)es_ES
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10261/155054-
dc.description13 p.-7 fig.-3 tab.es_ES
dc.description.abstractThe proton-translocating NADH-quinone oxidoreductase (complex I/NDH-1) contains a peripheral and a membrane domain. Three antiporter-like subunits in the membrane domain, NuoL, NuoM, and NuoN (ND5, ND4 and ND2, respectively), are structurally similar. We analyzed the role of NuoN in Escherichia coli NDH-1. The lysine residue at position 395 in NuoN (NLys(395)) is conserved in NuoL (LLys(399)) but is replaced by glutamic acid (MGlu(407)) in NuoM. Our mutation study on NLys(395) suggests that this residue participates in the proton translocation. Furthermore, we found that MGlu(407) is also essential and most likely interacts with conserved LArg(175). Glutamic acids, NGlu(133), MGlu(144), and LGlu(144), are corresponding residues. Unlike mutants of MGlu(144) and LGlu(144), mutation of NGlu(133) scarcely affected the energy-transducing activities. However, a double mutant of NGlu(133) and nearby KGlu(72) showed significant inhibition of these activities. This suggests that NGlu(133) bears a functional role similar to LGlu(144) and MGlu(144) but its mutation can be partially compensated by the nearby carboxyl residue. Conserved prolines located at loops of discontinuous transmembrane helices of NuoL, NuoM, and NuoN were shown to play a similar role in the energy-transducing activity. It seems likely that NuoL, NuoM, and NuoN pump protons by a similar mechanism. Our data also revealed that NLys(158) is one of the key interaction points with helix HL in NuoL. A truncation study indicated that the C-terminal amphipathic segments of NTM14 interacts with the Mβ sheet located on the opposite side of helix HL. Taken together, the mechanism of H(+) translocation in NDH-1 is discussed.es_ES
dc.description.sponsorshipThis work was supported, in whole or in part, by National Institutes of Health United States Public Health Service Grant GM33712 (to T. Y.).es_ES
dc.language.isoenges_ES
dc.publisherAmerican Society for Biochemistry and Molecular Biologyes_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rightsopenAccesses_ES
dc.subjectBioenergeticses_ES
dc.subjectElectron Transport System (ETS)es_ES
dc.subjectMembrane Energeticses_ES
dc.subjectMembrane Enzymeses_ES
dc.subjectNADH Dehydrogenasees_ES
dc.subjectSite-directed Mutagenesises_ES
dc.titleEnergy transducing roles of antiporter-like subunits in Escherichia coli NDH-1 with main focus on subunit NuoN (ND2)es_ES
dc.typeartículoes_ES
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M113.482968-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/ 10.1074/jbc.M113.482968es_ES
dc.identifier.e-issn1083-351X-
dc.contributor.funderNational Institutes of Health (US)es_ES
dc.relation.csices_ES
oprm.item.hasRevisionno ko 0 false*
dc.identifier.funderhttp://dx.doi.org/10.13039/100000002es_ES
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