{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,31]],"date-time":"2025-10-31T13:34:36Z","timestamp":1761917676911},"reference-count":35,"publisher":"Wiley","issue":"2-3","license":[{"start":{"date-parts":[[2001,5,22]],"date-time":"2001-05-22T00:00:00Z","timestamp":990489600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[2001,5,25]]},"abstract":"<jats:p>The cytochrome <jats:italic>aa<\/jats:italic>\n<jats:sub>3<\/jats:sub>\u2010type quinol oxidase from the archaeon <jats:italic>Acidianus ambivalens<\/jats:italic> and the <jats:italic>ba<jats:sub>3<\/jats:sub>\n<\/jats:italic>\u2010type cytochrome <jats:italic>c<\/jats:italic> oxidase from <jats:italic>Thermus thermophilus<\/jats:italic> are divergent members of the heme\u2010copper oxidase superfamily of enzymes. In particular they lack most of the key residues involved in the proposed proton transfer pathways. The pumping capability of the <jats:italic>A. ambivalens<\/jats:italic> enzyme was investigated and found to occur with the same efficiency as the canonical enzymes. This is the first demonstration of pumping of 1 H<jats:sup>+<\/jats:sup>\/electron in a heme\u2010copper oxidase that lacks most residues of the K\u2010 and D\u2010channels. Also, the structure of the <jats:italic>ba<jats:sub>3<\/jats:sub>\n<\/jats:italic> oxidase from <jats:italic>T. thermophilus<\/jats:italic> was simulated by mutating Phe274 to threonine and Glu278 to isoleucine in the D\u2010pathway of the <jats:italic>Paracoccus denitrificans<\/jats:italic> cytochrome <jats:italic>c<\/jats:italic> oxidase. This modification resulted in full efficiency of proton translocation albeit with a substantially lowered turnover. Together, these findings show that multiple structural solutions for efficient proton conduction arose during evolution of the respiratory oxidases, and that very few residues remain invariant among these enzymes to function in a common proton\u2010pumping mechanism.<\/jats:p>","DOI":"10.1016\/s0014-5793(01)02431-0","type":"journal-article","created":{"date-parts":[[2002,7,25]],"date-time":"2002-07-25T22:04:50Z","timestamp":1027634690000},"page":"159-164","source":"Crossref","is-referenced-by-count":36,"title":["Heme\u2010copper oxidases with modified D\u2010 and K\u2010pathways are yet efficient proton pumps"],"prefix":"10.1002","volume":"497","author":[{"given":"Cl\u00e1udio M.","family":"Gomes","sequence":"first","affiliation":[]},{"given":"Camilla","family":"Backgren","sequence":"additional","affiliation":[]},{"given":"Miguel","family":"Teixeira","sequence":"additional","affiliation":[]},{"given":"Anne","family":"Puustinen","sequence":"additional","affiliation":[]},{"given":"Marina L.","family":"Verkhovskaya","sequence":"additional","affiliation":[]},{"given":"M\u00e5rten","family":"Wikstr\u00f6m","sequence":"additional","affiliation":[]},{"given":"Michael I.","family":"Verkhovsky","sequence":"additional","affiliation":[]}],"member":"311","published-online":{"date-parts":[[2001,5,22]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6968.1994.tb07067.x"},{"key":"e_1_2_5_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0005-2728(99)00073-0"},{"key":"e_1_2_5_4_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi981807v"},{"key":"e_1_2_5_5_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.75.1.298"},{"key":"e_1_2_5_6_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00092a029"},{"key":"e_1_2_5_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00091a048"},{"key":"e_1_2_5_8_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00013a035"},{"key":"e_1_2_5_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0005-2728(98)00075-9"},{"key":"e_1_2_5_10_1","doi-asserted-by":"publisher","DOI":"10.1038\/376660a0"},{"key":"e_1_2_5_11_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.272.5265.1136"},{"key":"e_1_2_5_12_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.94.19.10128"},{"key":"e_1_2_5_13_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF00831534"},{"key":"e_1_2_5_14_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi00172a024"},{"key":"e_1_2_5_15_1","doi-asserted-by":"publisher","DOI":"10.1023\/A:1020524014920"},{"key":"e_1_2_5_16_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.95.22.12819"},{"key":"e_1_2_5_17_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi9910934"},{"key":"e_1_2_5_18_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.96.17.9591"},{"key":"e_1_2_5_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0005-2728(00)00068-2"},{"key":"e_1_2_5_20_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6968.1994.tb06779.x"},{"key":"e_1_2_5_21_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1997.0383a.x"},{"key":"e_1_2_5_22_1","doi-asserted-by":"publisher","DOI":"10.1128\/jb.179.4.1344-1353.1997"},{"key":"e_1_2_5_23_1","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/19.8.1766"},{"key":"e_1_2_5_24_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0014-5793(98)00942-9"},{"key":"e_1_2_5_25_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1995.tb20392.x"},{"key":"e_1_2_5_26_1","first-page":"2751","volume":"135","author":"Tricone A.","year":"1989","journal-title":"J. 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