{"title":"The optical and magnetic properties of copper in Chenopodium album plastocyanin","authors":"W.E. Blumberg, J. Peisach","doi":"10.1016/0926-6585(66)90063-X","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. The visible and near-ultraviolet optical absorption and optical rotary dispersion spectra of <em>Chenopodium album</em> plastocyanin were examined. Cotton effects were observed for the optical peaks in this region indicating the asymmetry of the copper chromophoric site.</p></span></li><li><span>2.</span><span><p>2. Electron paramagnetic resonance spectra showed that the two copper atoms in the protein are divalent and both are in equivalent sites.</p></span></li><li><span>3.</span><span><p>3. Proton relaxation rate studies showed that the copper is not on the surface of the molecule.</p></span></li></ul></div>","PeriodicalId":100158,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","volume":"126 2","pages":"Pages 269-273"},"PeriodicalIF":0.0000,"publicationDate":"1966-10-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6585(66)90063-X","citationCount":"51","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/092665856690063X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 51
Abstract
1.
1. The visible and near-ultraviolet optical absorption and optical rotary dispersion spectra of Chenopodium album plastocyanin were examined. Cotton effects were observed for the optical peaks in this region indicating the asymmetry of the copper chromophoric site.
2.
2. Electron paramagnetic resonance spectra showed that the two copper atoms in the protein are divalent and both are in equivalent sites.
3.
3. Proton relaxation rate studies showed that the copper is not on the surface of the molecule.
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