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To characterize the mechanism by which this subunit inhibits the F\n                    <jats:sub>1<\/jats:sub>\n                    F\n                    <jats:sub>O<\/jats:sub>\n                    nanomotor, the \u03b6 subunit of\n                    <jats:italic>Paracoccus denitrificans<\/jats:italic>\n                    (Pd\u2010\u03b6 was analyzed by the combination of kinetic, biochemical, bioinformatic, proteomic, and structural approaches. The \u03b6 subunit causes full inhibition of the sulfite\u2010activated PdF\n                    <jats:sub>1<\/jats:sub>\n                    \u2010ATPase with an apparent IC\n                    <jats:sub>50<\/jats:sub>\n                    of 270 nM by a mechanism independent of the 8 subunit. The inhibitory region of the \u03b6 subunit resides in the first 14 N\u2010terminal residues of the protein, which protrude from the 4\u2010\u03b1\u2010helix bundle structure of the isolated \u03b6 subunit, as resolved by NMR. Cross\u2010linking experiments show that the \u03b6 subunit interacts with rotor (\u03b3)and stator (\u03b1, \u03b2) subunits of the F\n                    <jats:sub>1<\/jats:sub>\n                    \u2010ATPase, indicating that the \u03b6 subunit hinders rotation of the central stalk. In addition, a putatively regulatory nucleotide\u2010binding site was found in the \u03b6 subunit by isothermal titration calorimetry. Together, the data show that the \u03b6 subunit controls the rotation of F\n                    <jats:sub>1<\/jats:sub>\n                    F\n                    <jats:sub>O<\/jats:sub>\n                    \u2010ATPase by a mechanism reminiscent of, but different from, those described for mitochondrial IF\n                    <jats:sub>1<\/jats:sub>\n                    and bacterial \u03b5 subunits where the 4\u2010\u03b1\u2010helix bundle of \u03b6 seems to work as an anchoring domain that orients the N\u2010terminal inhibitory domain to hinder rotation of the central stalk.\u2014Zarco\u2010Zavala, M., Morales\u2010R\u00edos, E., Mendoza\u2010Hern\u00e1ndez, G., Ram\u00edrez\u2010Silva, L., P\u00e9rez\u2010Hern\u00e1ndez, G., Garc\u00eda\u2010Trejo, J. J. The \u03b6 subunit of the F\n                    <jats:sub>1<\/jats:sub>\n                    F\n                    <jats:sub>O<\/jats:sub>\n                    \u2010ATP synthase of \u03b1\u2010proteobacteria controls rotation of the nanomotor with a different structure.\n                    <jats:italic>FASEB J<\/jats:italic>\n                    . 28, 2146\u20132157 (2014).\n                    <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/www.fasebj.org\">www.fasebj.org<\/jats:ext-link>\n                  <\/jats:p>","DOI":"10.1096\/fj.13-241430","type":"journal-article","created":{"date-parts":[[2014,2,13]],"date-time":"2014-02-13T01:02:50Z","timestamp":1392253370000},"page":"2146-2157","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":34,"title":["The \u03b6 subunit of the F\n                    <sub>1<\/sub>\n                    F\n                    <sub>O<\/sub>\n                    \u2010ATP synthase of \u03b1\u2010proteobacteria controls rotation of the nanomotor with a different structure"],"prefix":"10.1096","volume":"28","author":[{"given":"Mariel","family":"Zarco\u2010Zavala","sequence":"first","affiliation":[{"name":"Departamento de Biolog\u00eda, Facultad de Qu\u00edmica Universidad Nacional Aut\u00f3noma de M\u00e9xico Coyoac\u00e1n M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Edgar","family":"Morales\u2010R\u00edos","sequence":"additional","affiliation":[{"name":"Medical Research Council Mitochondrial Research Unit Cambridge UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guillermo","family":"Mendoza\u2010Hern\u00e1ndez","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica, Facultad de Medicina Universidad Nacional Aut\u00f3noma de M\u00e9xico Coyoac\u00e1n M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Leticia","family":"Ram\u00edrez\u2010Silva","sequence":"additional","affiliation":[{"name":"Departamento de Bioqu\u00edmica, Facultad de Medicina Universidad Nacional Aut\u00f3noma de M\u00e9xico Coyoac\u00e1n M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gerardo","family":"P\u00e9rez\u2010Hern\u00e1ndez","sequence":"additional","affiliation":[{"name":"Universidad Aut\u00f3noma Metropolitana de M\u00e9xico Tlalpan M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jos\u00e9 J.","family":"Garc\u00eda\u2010Trejo","sequence":"additional","affiliation":[{"name":"Departamento de Biolog\u00eda, Facultad de Qu\u00edmica Universidad Nacional Aut\u00f3noma de M\u00e9xico Coyoac\u00e1n M\u00e9xico"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2014,2,12]]},"reference":[{"key":"e_1_2_8_2_1","doi-asserted-by":"publisher","DOI":"10.1007\/s10867-008-9114-z"},{"key":"e_1_2_8_3_1","doi-asserted-by":"publisher","DOI":"10.1042\/BST20110773"},{"key":"e_1_2_8_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)75338-1"},{"key":"e_1_2_8_5_1","doi-asserted-by":"publisher","DOI":"10.1023\/A:1022514008462"},{"key":"e_1_2_8_6_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00544a021"},{"key":"e_1_2_8_7_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.111128098"},{"key":"e_1_2_8_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2006.02.017"},{"key":"e_1_2_8_9_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M109.003798"},{"key":"e_1_2_8_10_1","doi-asserted-by":"publisher","DOI":"10.1096\/fj.09-137356"},{"key":"e_1_2_8_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(86)90304-0"},{"key":"e_1_2_8_12_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF02110340"},{"key":"e_1_2_8_13_1","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1042\/bj2030339","article-title":"A method for determining kinetic parameters at high enzyme concentrations","volume":"203","author":"Halfman C. 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