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It consists of three subunits, subunit I (CoxA2, 63.9\u00a0kDa), subunit II (CoxB2, 16.8\u00a0kDa), and an additional subunit IIa of 5.2\u00a0kDa. Surprisingly it is able to oxidize both reduced cytochrome\n                    <jats:italic>c<\/jats:italic>\n                    and ubiquinol in a cyanide sensitive manner. Cox2 is part of a respiratory chain supercomplex. This supercomplex contains the fully assembled cytochrome\n                    <jats:italic>bc<\/jats:italic>\n                    <jats:sub>1<\/jats:sub>\n                    complex and Cox2. Although direct ubiquinol oxidation by Cox2 conserves less energy than ubiquinol oxidation by the cytochrome\n                    <jats:italic>bc<\/jats:italic>\n                    <jats:sub>1<\/jats:sub>\n                    complex followed by cytochrome\n                    <jats:italic>c<\/jats:italic>\n                    oxidation by a cytochrome\n                    <jats:italic>c<\/jats:italic>\n                    oxidase, ubiquinol oxidation by Cox2 is of advantage when all ubiquinone would be completely reduced to ubiquinol, e.g., by the sulfide\u2236quinone oxidoreductase, because the cytochrome\n                    <jats:italic>bc<\/jats:italic>\n                    <jats:sub>1<\/jats:sub>\n                    complex requires the presence of ubiquinone to function according to the Q-cycle mechanism. In the case that all ubiquinone has been reduced to ubiquinol its reoxidation by Cox2 will enable the cytochrome\n                    <jats:italic>bc<\/jats:italic>\n                    <jats:sub>1<\/jats:sub>\n                    complex to resume working.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1121040109","type":"journal-article","created":{"date-parts":[[2012,2,15]],"date-time":"2012-02-15T01:14:46Z","timestamp":1329268486000},"page":"3275-3280","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":34,"title":["Heme-copper terminal oxidase using both cytochrome\n                    <i>c<\/i>\n                    and ubiquinol as electron donors"],"prefix":"10.1073","volume":"109","author":[{"given":"Ye","family":"Gao","sequence":"first","affiliation":[{"name":"Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bj\u00f6rn","family":"Meyer","sequence":"additional","affiliation":[{"name":"Institute of Pharmaceutical Chemistry, Goethe University, D-60438 Frankfurt, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lucie","family":"Sokolova","sequence":"additional","affiliation":[{"name":"Institute of Physics and Theoretical Chemistry, Goethe University, D-60438 Frankfurt, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Klaus","family":"Zwicker","sequence":"additional","affiliation":[{"name":"Molecular Bioenergetics, Medical School, Goethe University, D-60590 Frankfurt, Germany; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Karas","sequence":"additional","affiliation":[{"name":"Institute of Pharmaceutical Chemistry, Goethe University, D-60438 Frankfurt, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bernd","family":"Brutschy","sequence":"additional","affiliation":[{"name":"Institute of Physics and Theoretical Chemistry, Goethe University, D-60438 Frankfurt, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guohong","family":"Peng","sequence":"additional","affiliation":[{"name":"Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt, Germany;"},{"name":"Institute of Oceanology, Chinese Academy of Sciences, Qingdao 266071, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hartmut","family":"Michel","sequence":"additional","affiliation":[{"name":"Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, D-60438 Frankfurt, Germany;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2012,2,14]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"1488","DOI":"10.1126\/science.283.5407.1488","article-title":"Oxidative phosphorylation at the fin de siecle","volume":"283","author":"Saraste M","year":"1999","unstructured":"M Saraste, Oxidative phosphorylation at the fin de siecle. Science 283, 1488\u20131493 (1999).","journal-title":"Science"},{"key":"e_1_3_4_2_2","first-page":"337","article-title":"Biogenesis of respiratory cytochromes in bacteria","volume":"61","author":"Thony-Meyer L","year":"1997","unstructured":"L Thony-Meyer, Biogenesis of respiratory cytochromes in bacteria. Microbiol Mol Biol Rev 61, 337\u2013376 (1997).","journal-title":"Microbiol Mol Biol Rev"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/S0005-2728(01)00169-4","article-title":"A novel scenario for the evolution of haem-copper oxygen reductases","volume":"1505","author":"Pereira MM","year":"2001","unstructured":"MM Pereira, M Santana, M Teixeira, A novel scenario for the evolution of haem-copper oxygen reductases. 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EMBO J 19, 1766\u20131776 (2000).","journal-title":"EMBO J"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"910","DOI":"10.1038\/82824","article-title":"The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site","volume":"7","author":"Abramson J","year":"2000","unstructured":"J Abramson, et al., The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site. Nat Struct Biol 7, 910\u2013917 (2000).","journal-title":"Nat Struct Biol"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"2458","DOI":"10.1016\/S0021-9258(18)89576-X","article-title":"Isolation of ubiquinol oxidase from Paracoccus denitrificans and resolution into cytochrome bc1 and cytochrome c-aa3 complexes","volume":"260","author":"Berry EA","year":"1985","unstructured":"EA Berry, BL Trumpower, Isolation of ubiquinol oxidase from Paracoccus denitrificans and resolution into cytochrome bc1 and cytochrome c-aa3 complexes. J Biol Chem 260, 2458\u20132467 (1985).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"2759","DOI":"10.1002\/elps.200600049","article-title":"Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and supercomplexes","volume":"27","author":"Krause F","year":"2006","unstructured":"F Krause, Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and supercomplexes. 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Biochemical, enzymatic and crystallization studies on Aquifex aeolicus sulfide\u2236quinone oxidoreductase","volume":"1798","author":"Marcia M","year":"2010","unstructured":"M Marcia, et al., Characterizing a monotopic membrane enzyme. Biochemical, enzymatic and crystallization studies on Aquifex aeolicus sulfide\u2236quinone oxidoreductase. Biochim Biophys Acta 1798, 2114\u20132123 (2010).","journal-title":"Biochim Biophys Acta"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"e21616","DOI":"10.1371\/journal.pone.0021616","article-title":"The elusive third subunit IIa of the bacterial B-type oxidases: The enzyme from the hyperthermophile Aquifex aeolicus","volume":"6","author":"Prunetti L","year":"2011","unstructured":"L Prunetti, M Brugna, R Lebrun, MT Giudici-Orticoni, M Guiral, The elusive third subunit IIa of the bacterial B-type oxidases: The enzyme from the hyperthermophile Aquifex aeolicus. PLoS One 6, e21616 (2011).","journal-title":"PLoS One"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"2068","DOI":"10.1110\/ps.9.11.2068","article-title":"Primary structure of a novel subunit in ba3-cytochrome oxidase from Thermus thermophilus","volume":"9","author":"Soulimane T","year":"2000","unstructured":"T Soulimane, ME Than, M Dewor, R Huber, G Buse, Primary structure of a novel subunit in ba3-cytochrome oxidase from Thermus thermophilus. Protein Sci 9, 2068\u20132073 (2000).","journal-title":"Protein Sci"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1111\/j.1432-1033.1997.0332a.x","article-title":"Cytochrome ba3 from Natronobacterium pharaonis\u2014an archaeal four-subunit cytochrome-c-type oxidase","volume":"250","author":"Mattar S","year":"1997","unstructured":"S Mattar, M Engelhard, Cytochrome ba3 from Natronobacterium pharaonis\u2014an archaeal four-subunit cytochrome-c-type oxidase. Eur J Biochem 250, 332\u2013341 (1997).","journal-title":"Eur J Biochem"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"1344","DOI":"10.1128\/jb.179.4.1344-1353.1997","article-title":"The terminal quinol oxidase of the hyperthermophilic archaeon Acidianus ambivalens exhibits a novel subunit structure and gene organization","volume":"179","author":"Purschke WG","year":"1997","unstructured":"WG Purschke, CL Schmidt, A Petersen, G Schafer, The terminal quinol oxidase of the hyperthermophilic archaeon Acidianus ambivalens exhibits a novel subunit structure and gene organization. J Bacteriol 179, 1344\u20131353 (1997).","journal-title":"J Bacteriol"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1002\/j.1460-2075.1992.tb05117.x","article-title":"An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes","volume":"11","author":"Lubben M","year":"1992","unstructured":"M Lubben, B Kolmerer, M Saraste, An archaebacterial terminal oxidase combines core structures of two mitochondrial respiratory complexes. EMBO J 11, 805\u2013812 (1992).","journal-title":"EMBO J"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"S53","DOI":"10.1002\/(SICI)1520-6343(1999)5:5+<S53::AID-BSPY6>3.0.CO;2-2","article-title":"The active site structure of ba3 oxidase from Thermus thermophilus studied by resonance raman spectroscopy","volume":"5","author":"Gerscher S","year":"1999","unstructured":"S Gerscher, P Hildebrandt, G Buse, T Soulimane, The active site structure of ba3 oxidase from Thermus thermophilus studied by resonance raman spectroscopy. Biospectroscopy 5, S53\u2013S63 (1999).","journal-title":"Biospectroscopy"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"5779","DOI":"10.1073\/pnas.85.16.5779","article-title":"Properties of a copper-containing cytochrome ba3: A second terminal oxidase from the extreme thermophile Thermus thermophilus","volume":"85","author":"Zimmermann BH","year":"1988","unstructured":"BH Zimmermann, CI Nitsche, JA Fee, F Rusnak, E Munck, Properties of a copper-containing cytochrome ba3: A second terminal oxidase from the extreme thermophile Thermus thermophilus. Proc Natl Acad Sci USA 85, 5779\u20135783 (1988).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"3195","DOI":"10.1073\/pnas.89.8.3195","article-title":"Reaction of cyanide with cytochrome ba3 from Thermus thermophilus: Spectroscopic characterization of the Fe(II)a3-CN.Cu(II)B-CN complex suggests four 14N atoms are coordinated to CuB","volume":"89","author":"Surerus KK","year":"1992","unstructured":"KK Surerus, et al., Reaction of cyanide with cytochrome ba3 from Thermus thermophilus: Spectroscopic characterization of the Fe(II)a3-CN.Cu(II)B-CN complex suggests four 14N atoms are coordinated to CuB. Proc Natl Acad Sci USA 89, 3195\u20133199 (1992).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"6194","DOI":"10.1016\/S0021-9258(20)65125-0","article-title":"Kinetic characterization of the interaction between cytochrome oxidase and cytochrome c","volume":"257","author":"Antalis TM","year":"1982","unstructured":"TM Antalis, G Palmer, Kinetic characterization of the interaction between cytochrome oxidase and cytochrome c. J Biol Chem 257, 6194\u20136206 (1982).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/0003-2697(76)90067-1","article-title":"An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels","volume":"75","author":"Thomas PE","year":"1976","unstructured":"PE Thomas, D Ryan, W Levin, An improved staining procedure for the detection of the peroxidase activity of cytochrome P-450 on sodium dodecyl sulfate polyacrylamide gels. Anal Biochem 75, 168\u2013176 (1976).","journal-title":"Anal Biochem"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/0014-5793(77)80044-6","article-title":"Heme spin-states of cytochrome c oxidase derived from room temperature magnetic susceptibility measurements","volume":"75","author":"Falk KE","year":"1977","unstructured":"KE Falk, T Vanngard, J Angstrom, Heme spin-states of cytochrome c oxidase derived from room temperature magnetic susceptibility measurements. FEBS Lett 75, 23\u201327 (1977).","journal-title":"FEBS Lett"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1042\/bj1650327","article-title":"Variable-temperature magnetic-circular-dichroism spectra of cytochrome c oxidase and its derivatives","volume":"165","author":"Thomson AJ","year":"1977","unstructured":"AJ Thomson, T Brittain, C Greenwood, JP Springall, Variable-temperature magnetic-circular-dichroism spectra of cytochrome c oxidase and its derivatives. Biochem J 165, 327\u2013336 (1977).","journal-title":"Biochem J"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"8065","DOI":"10.1016\/S0021-9258(17)34362-4","article-title":"Electronic state of heme in cytochrome oxidase III. The magnetic susceptibility of beef heart cytochrome oxidase and some of its derivatives from 7\u2013200\u00a0K. Direct evidence for an antiferromagnetically coupled Fe (III)\/Cu (II) pair","volume":"253","author":"Tweedle MF","year":"1978","unstructured":"MF Tweedle, LJ Wilson, Electronic state of heme in cytochrome oxidase III. The magnetic susceptibility of beef heart cytochrome oxidase and some of its derivatives from 7\u2013200\u00a0K. Direct evidence for an antiferromagnetically coupled Fe (III)\/Cu (II) pair. J Biol Chem 253, 8065\u20138071 (1978).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"10800","DOI":"10.1021\/bi034452a","article-title":"The naphthoquinol oxidizing cytochrome bc1 complex of the hyperthermophilic knallgasbacterium Aquifex aeolicus: Properties and phylogenetic relationships","volume":"42","author":"Schutz M","year":"2003","unstructured":"M Schutz, et al., The naphthoquinol oxidizing cytochrome bc1 complex of the hyperthermophilic knallgasbacterium Aquifex aeolicus: Properties and phylogenetic relationships. Biochemistry 42, 10800\u201310808 (2003).","journal-title":"Biochemistry"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1016\/j.bbabio.2003.10.010","article-title":"Interaction of cytochrome c with cytochrome oxidase: Two different docking scenarios","volume":"1655","author":"Maneg O","year":"2004","unstructured":"O Maneg, F Malatesta, B Ludwig, V Drosou, Interaction of cytochrome c with cytochrome oxidase: Two different docking scenarios. Biochim Biophys Acta 1655, 274\u2013281 (2004).","journal-title":"Biochim Biophys Acta"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/0014-5793(93)80156-O","article-title":"Comparison of ubiquinol and cytochrome c terminal oxidases. An alternative view","volume":"327","author":"Musser SM","year":"1993","unstructured":"SM Musser, MH Stowell, SI Chan, Comparison of ubiquinol and cytochrome c terminal oxidases. An alternative view. FEBS Lett 327, 131\u2013136 (1993).","journal-title":"FEBS Lett"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/0968-0004(94)90071-X","article-title":"The cytochrome oxidase superfamily of redox-driven proton pumps","volume":"19","author":"Calhoun MW","year":"1994","unstructured":"MW Calhoun, JW Thomas, RB Gennis, The cytochrome oxidase superfamily of redox-driven proton pumps. Trends Biochem Sci 19, 325\u2013330 (1994).","journal-title":"Trends Biochem Sci"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"14109","DOI":"10.1073\/pnas.1018958108","article-title":"Adaptation of aerobic respiration to low O2 environments","volume":"108","author":"Han H","year":"2011","unstructured":"H Han, et al., Adaptation of aerobic respiration to low O2 environments. Proc Natl Acad Sci USA 108, 14109\u201314114 (2011).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_39_2","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/S0014-5793(98)00942-9","article-title":"Electrical current generation and proton pumping catalyzed by the ba3-type cytochrome c oxidase from Thermus thermophilus","volume":"434","author":"Kannt A","year":"1998","unstructured":"A Kannt, et al., Electrical current generation and proton pumping catalyzed by the ba3-type cytochrome c oxidase from Thermus thermophilus. FEBS Lett 434, 17\u201322 (1998).","journal-title":"FEBS Lett"},{"key":"e_1_3_4_40_2","doi-asserted-by":"crossref","first-page":"9625","DOI":"10.1073\/pnas.0904165106","article-title":"The structure of Aquifex aeolicus sulfide\u2236quinone oxidoreductase, a basis to understand sulfide detoxification and respiration","volume":"106","author":"Marcia M","year":"2009","unstructured":"M Marcia, U Ermler, G Peng, H Michel, The structure of Aquifex aeolicus sulfide\u2236quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proc Natl Acad Sci USA 106, 9625\u20139630 (2009).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_41_2","doi-asserted-by":"crossref","first-page":"3032","DOI":"10.1021\/bi026876v","article-title":"Isolation, characterization and electron microscopic single particle analysis of the NADH\u2236ubiquinone oxidoreductase (complex I) from the hyperthermophilic eubacterium Aquifex aeolicus","volume":"42","author":"Peng G","year":"2003","unstructured":"G Peng, et al., Isolation, characterization and electron microscopic single particle analysis of the NADH\u2236ubiquinone oxidoreductase (complex I) from the hyperthermophilic eubacterium Aquifex aeolicus. 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