Determination of the zero-field splitting of Fe 3+ in heme proteins from the temperature dependence of the spin-lattice relaxation rate

A sensitive method for obtaining the zero-field crystalline field splitting is described and applied to ferrimyoglobin (H 2O) and ferrimyoglobin (F −). The high accuracy (1–2%) with which the splitting can be determined should make it possible to explore the environmental (conformatinal) changes at...

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Bibliographic Details
Published inBiochimica et biophysica acta Vol. 244; no. 1; pp. 206 - 210
Main Authors Scholes, Charles P., Isaacson, Roger A., Feher, George
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 20.07.1971
Subjects
Animals
Cetacea
Electron Spin Resonance Spectroscopy
Heme
Iron
Mathematics
Myoglobin
Oxidation-Reduction
Protein Conformation
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Summary:A sensitive method for obtaining the zero-field crystalline field splitting is described and applied to ferrimyoglobin (H 2O) and ferrimyoglobin (F −). The high accuracy (1–2%) with which the splitting can be determined should make it possible to explore the environmental (conformatinal) changes at the Fe 3+ site.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0304-4165
0006-3002
1872-8006
DOI:10.1016/0304-4165(71)90138-3