{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T11:15:57Z","timestamp":1758280557527},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1979,8,15]]},"abstract":"<jats:p>1. Electron-transport particles derived from Escherichia coli grown aerobically contain three b-type cytochromes with mid-point oxidation\u2013reduction potentials at pH7 of +260mV, +80mV and \u221250mV, with n=1 for each. The variation of these values with pH was determined. 2. E. coli develops a different set of b-type cytochromes when grown anaerobically on glycerol with fumarate or nitrate as terminal electron acceptor. Electron-transport particles of fumarate-grown cells contain b-type cytochromes with mid-point potentials at pH7 of +140mV and +250mV (n=1). These two cytochromes are also present in cells grown with nitrate as terminal acceptor, where an additional cytochrome b with a mid-point potential of +10mV (n=1) is developed. 3. The wavelengths of the \u03b1-absorption-band maxima of the b-type cytochromes at 77K were: (a) for aerobically grown cells, cytochrome b (Em7 +260mV), 556nm and 563nm, cytochrome b (Em7 +80mV), 556nm and cytochrome b (Em7\u221250mV), 558nm; (b) for anaerobically grown cells, cytochrome b (Em7 +250mV), 558nm, cytochrome b (Em7 +40mV), 555nm and cytochrome b (Em7 +10mV), 556nm. 4. Cytochrome d was found to have a mid-point potential at pH7 of +280mV (n=1). 5. Cytochrome a1 was resolved as two components of equal magnitude with mid-point potentials of +260mV and +160mV (n=1). 6. Redox titrations performed in the presence of CO showed that one of the b-type cytochromes in the aerobically grown cultures was reduced, even at the upper limits of our range of electrode potentials (above +400mV). Cytochrome d was also not oxidizable in the presence of CO. Neither of the cytochromes a1 was affected by the presence of CO.<\/jats:p>","DOI":"10.1042\/bj1820465","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:18:33Z","timestamp":1439237913000},"page":"465-472","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["Characterization and phenotypic control of the cytochrome content of <i>Escherichia coli<\/i>"],"prefix":"10.1042","volume":"182","author":[{"given":"Graeme A.","family":"Reid","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, Scotland, U.K."}]},{"given":"W. John","family":"Ingledew","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, Scotland, U.K."}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/182\/2\/465\/783153\/bj1820465.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/182\/2\/465\/783153\/bj1820465.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T13:21:10Z","timestamp":1637932870000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/182\/2\/465\/4638\/Characterization-and-phenotypic-control-of-the"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1979,8,15]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1979,8,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1820465","relation":{},"ISSN":["0306-3283"],"issn-type":[{"value":"0306-3283","type":"print"}],"subject":[],"published":{"date-parts":[[1979,8,15]]}}}