{"title":"Resonance Raman spectra of deoxyhemoproteins. Heme structure in relation to dioxygen binding","authors":"A. Desbois , M. Lutz , R. Banerjee","doi":"10.1016/0005-2795(81)90132-X","DOIUrl":null,"url":null,"abstract":"<div><p>The low-frequency regions of the resonance Raman spectra of deoxygenated ferrous forms of soybean leghemoglobin <span><math><mtext>a</mtext></math></span>, horse myoglobin, sperm whale myoglobin, <em>Aplysia</em> myoglobin, stripped normal human hemoglobin (T quaternary form) and of stripped human NESdesArg-hemoglobin (R quaternary form) are reported. Differences observed among these spectra show that the globins of these hemoproteins impose various heme structures. In particular, the variable frequencies of band II (210–224 cm<sup>−1</sup>) and of band I<sub>b</sub> (121–163 cm<sup>−1</sup>) show that an increase in dioxygen affinity corresponds to a decrease in Fe-N(pyrrole) bond length.</p></div>","PeriodicalId":100165,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1981-12-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2795(81)90132-X","citationCount":"12","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/000527958190132X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 12
Abstract
The low-frequency regions of the resonance Raman spectra of deoxygenated ferrous forms of soybean leghemoglobin , horse myoglobin, sperm whale myoglobin, Aplysia myoglobin, stripped normal human hemoglobin (T quaternary form) and of stripped human NESdesArg-hemoglobin (R quaternary form) are reported. Differences observed among these spectra show that the globins of these hemoproteins impose various heme structures. In particular, the variable frequencies of band II (210–224 cm−1) and of band Ib (121–163 cm−1) show that an increase in dioxygen affinity corresponds to a decrease in Fe-N(pyrrole) bond length.