{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,11,23]],"date-time":"2023-11-23T16:01:47Z","timestamp":1700755307021},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1974,2,15]]},"abstract":"<jats:p>1. A new mutant strain (AN228) of Escherichia coli K12, unable to couple phosphorylation to electron transport, has been isolated. The mutant allele (unc-405), in strain AN228, was found to map near the uncA and uncB genes at about minute 74 on the E. coli genome. 2. A transductant strain (AN285) carrying the unc-405 allele is similar to the uncA and uncB mutants described previously in that it is unable to grow on succinate, gives a low aerobic yield on limiting concentrations of glucose, has a normal rate of electron transport, is unable to couple phosphorylation to electron transport, and lacks ATP-dependent transhydrogenase activity. 3. Strain AN285 (unc-405) is similar to an uncA mutant, but different from an uncB mutant, in that it is unable to grow anaerobically in a glucose\u2013mineral-salts medium, and membrane preparations do not have Mg2+-stimulated adenosine triphosphatase activity. 4. Strain AN285 (unc-405) does not form an aggregate analogous to the membrane-bound Mg2+-stimulated adenosine triphosphatase aggregate found in normal cells. In this respect it differs from strain AN249 (uncA\u2212), which forms an inactive membrane-bound Mg2+-stimulated adenosine triphosphatase aggregate.<\/jats:p>","DOI":"10.1042\/bj1380211","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T19:52:40Z","timestamp":1439236360000},"page":"211-215","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Oxidative phosphorylation in <i>Escherichia coli<\/i> K12. An uncoupled mutant with altered membrane structure"],"prefix":"10.1042","volume":"138","author":[{"given":"G. B.","family":"Cox","sequence":"first","affiliation":[{"name":"Department of Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra, A.C.T. 2601, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"F.","family":"Gibson","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra, A.C.T. 2601, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L.","family":"McCann","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra, A.C.T. 2601, Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/138\/2\/211\/780999\/bj1380211.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/138\/2\/211\/780999\/bj1380211.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T15:52:51Z","timestamp":1637941971000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/138\/2\/211\/8857\/Oxidative-phosphorylation-in-Escherichia-coli-K12"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1974,2,15]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1974,2,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1380211","relation":{},"ISSN":["0306-3283"],"issn-type":[{"value":"0306-3283","type":"print"}],"subject":[],"published":{"date-parts":[[1974,2,15]]}}}