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Studies of its energy transduction mechanism are hindered by the extreme hydrophobicity of Q<jats:sub>10<\/jats:sub>, and they have so far relied on native membranes with many components or on hydrophilic Q<jats:sub>10<\/jats:sub> analogues that partition into membranes and undergo side reactions. Herein, we present a self\u2010assembled system without these limitations: proteoliposomes containing mammalian complex\u2005I, Q<jats:sub>10<\/jats:sub>, and a quinol oxidase (the alternative oxidase, AOX) to recycle Q<jats:sub>10<\/jats:sub>H<jats:sub>2<\/jats:sub> to Q<jats:sub>10<\/jats:sub>. AOX is present in excess, so complex\u2005I is completely rate determining and the Q<jats:sub>10<\/jats:sub> pool is kept oxidized under steady\u2010state catalysis. The system was used to measure a fully\u2010defined <jats:italic>K<\/jats:italic><jats:sub>M<\/jats:sub> value for Q<jats:sub>10<\/jats:sub>. The strategy is suitable for any enzyme with a hydrophobic quinone\/quinol substrate, and could be used to characterize hydrophobic inhibitors with potential applications as pharmaceuticals, pesticides, or fungicides.<\/jats:p>","DOI":"10.1002\/ange.201507332","type":"journal-article","created":{"date-parts":[[2015,11,23]],"date-time":"2015-11-23T11:48:10Z","timestamp":1448279290000},"page":"738-741","source":"Crossref","is-referenced-by-count":4,"title":["A Self\u2010Assembled Respiratory Chain that Catalyzes NADH Oxidation by Ubiquinone\u201010 Cycling between Complex\u2005I and the Alternative Oxidase"],"prefix":"10.1002","volume":"128","author":[{"given":"Andrew J. Y.","family":"Jones","sequence":"first","affiliation":[]},{"given":"James N.","family":"Blaza","sequence":"additional","affiliation":[]},{"given":"Hannah R.","family":"Bridges","sequence":"additional","affiliation":[]},{"given":"Benjamin","family":"May","sequence":"additional","affiliation":[]},{"given":"Anthony L.","family":"Moore","sequence":"additional","affiliation":[]},{"given":"Judy","family":"Hirst","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2015,11,23]]},"reference":[{"key":"e_1_2_3_1_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev-biochem-070511-103700"},{"key":"e_1_2_3_2_2","doi-asserted-by":"publisher","DOI":"10.1021\/acs.biochem.5b00385"},{"key":"e_1_2_3_3_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi501403t"},{"key":"e_1_2_3_4_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M704519200"},{"key":"e_1_2_3_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(95)00803-H"},{"key":"e_1_2_3_6_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1973.tb02767.x"},{"key":"e_1_2_3_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(93)80498-J"},{"key":"e_1_2_3_8_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi802282h"},{"key":"e_1_2_3_9_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1218386110"},{"key":"e_1_2_3_10_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbabio.2009.12.021"},{"key":"e_1_2_3_11_2","first-page":"120","volume":"70","author":"Vinogradov A. 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