{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,27]],"date-time":"2025-09-27T17:01:11Z","timestamp":1758992471467},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1982,10,1]]},"abstract":"<jats:p>The magnetic-circular-dichroism (m.c.d.) spectra of oxidized \u2018resting\u2019 bovine cytochrome c oxidase and the cyanide-inhibited form are reported at 5.15 T and at 4.2 K along with m.c.d. magnetization curves plotted at selected wavelengths. In both spectra there are features at 790nm and 1564nm due to Cua and haem a respectively, the e.p.r.-detectable components of the enzyme. There is a new peak at 1946nm only in the spectrum of the cyanide-inhibited enzyme. Arguments are advanced that assign this to low-spin ferric haem a3 bridged to Cua3, thereby forming a ferromagnetically coupled pair of metal ions.<\/jats:p>","DOI":"10.1042\/bj2070167","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:34:27Z","timestamp":1439238867000},"page":"167-170","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":32,"title":["The nature of haem <i>a<\/i>3 in the oxidized state of cytochrome <i>c<\/i> oxidase. Evidence from low-temperature magnetic-circular-dichroism spectroscopy in the near infrared region"],"prefix":"10.1042","volume":"207","author":[{"given":"A J","family":"Thomson","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D G","family":"Englinton","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"B C","family":"Hill","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C","family":"Greenwood","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\/207\/1\/167\/577656\/bj2070167.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/207\/1\/167\/577656\/bj2070167.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,25]],"date-time":"2021-11-25T12:48:44Z","timestamp":1637844524000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/207\/1\/167\/14066\/The-nature-of-haem-a3-in-the-oxidized-state-of"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1982,10,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1982,10,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj2070167","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1982,10,1]]}}}