{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,29]],"date-time":"2026-05-29T18:12:06Z","timestamp":1780078326583,"version":"3.54.0"},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1977,1,1]]},"abstract":"<jats:p>1. E.p.r. (electron-paramagnetic-resonance), proton-relaxation and u.v.-absorption parameters, and enzyme activity of samples of Cu2+-free bovine superoxide dismutase recombined with different amounts of Cu2+ up to the stoicheiometric [Cu2+]\/protein] ratio were investigated after attainment of equilibrium in the recovery process. 2. The e.p.r. spectra were identical with the spectrum of the native protein at all [Cu2+]\/[protein] ratios. The relaxation rate of the water protons (T1) and the u.v. absorption increase as linear functions of the added Cu2+. 3. On the other hand, in recombination experiments in the range pH 7.6-10.5 the enzyme activity shows a non-linear increase as the [Cu2+]\/[protein] ratio rises. The experimental curves can be interpreted in terms of the model of co-operative binding of Cu2+ to the two sites proposed on the basis of the electrophoretic analyses of the samples, and show that the specific activity of the molecules containing only one Cu2+ ion is twice as high as that of the molecules with two Cu2+ ions. 4. These results support the hypothesis of an anti-co-operative interaction between the two sites during the activity, which allows only one Cu2+ ion to function in catalysis.<\/jats:p>","DOI":"10.1042\/bj1610031","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:05:13Z","timestamp":1439237113000},"page":"31-35","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":28,"title":["The binding of copper ions to copper-free bovine superoxide dismutase. Properties of the protein recombined with increasing amounts of copper ions"],"prefix":"10.1042","volume":"161","author":[{"given":"A","family":"Rigo","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M","family":"Terenzi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"P","family":"Viglino","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L","family":"Calabrese","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D","family":"Cocco","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"G","family":"Rotilio","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/161\/1\/31\/568025\/bj1610031.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/161\/1\/31\/568025\/bj1610031.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T17:10:34Z","timestamp":1637946634000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/161\/1\/31\/10532\/The-binding-of-copper-ions-to-copper-free-bovine"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1977,1,1]]},"references-count":0,"journal-issue":{"issue":"1","published-print":{"date-parts":[[1977,1,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1610031","relation":{},"ISSN":["0264-6021"],"issn-type":[{"value":"0264-6021","type":"print"}],"subject":[],"published":{"date-parts":[[1977,1,1]]}}}