{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T13:30:46Z","timestamp":1760189446246},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1981,2,15]]},"abstract":"<jats:p>The oxidation-reduction midpoint potential of the cytochrome b found in the plasma membrane of human neutrophils has been determined at pH 7.0 (Em,7.0) from measurements of absorption spectra at fixed potentials. In both unstimulated and phorbol myristate acetate-stimulated cells Em,7.0 was -245 mV. Changes in pH affected the Em of the cytochrome b, with a slope of approx. 25 mV\/pH unit change. The Em,7.0 of the haem group(s) of the membrane-bound myeloperoxidase of human neutrophils was found to be +34 mV. The plasma membranes contained no detectable ubiquinone, and no iron-sulphur compounds were detected by e.p.r. spectroscopy at 5-20 K. No flavins were detected by e.p.r. spectroscopy. The cytochrome b-245 was not reduced by added NADH or NADPH. Dithionite-reduced cytochrome b-245 formed a complex with CO, supplied as a saturated solution, which was dissociated with 26 microseconds illumination from a xenon flash lamp, and the recombination with CO had a half-time of approx. 6 ms. Partly (80%) reduced cytochrome b-245 was oxidized by added air-saturated buffer with a half-time faster than 1 s at 20 degrees C, a resolution limited by mixing time. These results are compatible with cytochrome b-245 acting as an oxidase.<\/jats:p>","DOI":"10.1042\/bj1940599","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:26:47Z","timestamp":1439238407000},"page":"599-606","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":165,"title":["Oxidation-reduction properties of the cytochrome <i>b<\/i> found in the plasma-membrane fraction of human neutrophils. A possible oxidase in the respiratory burst"],"prefix":"10.1042","volume":"194","author":[{"given":"A R","family":"Cross","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"O T","family":"Jones","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A M","family":"Harper","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A W","family":"Segal","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/194\/2\/599\/783853\/bj1940599.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/194\/2\/599\/783853\/bj1940599.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T13:52:55Z","timestamp":1637848375000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/194\/2\/599\/16201\/Oxidation-reduction-properties-of-the-cytochrome-b"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1981,2,15]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1981,2,15]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1940599","relation":{},"ISSN":["0306-3283"],"issn-type":[{"value":"0306-3283","type":"print"}],"subject":[],"published":{"date-parts":[[1981,2,15]]}}}