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• W2073695209 abstract "X-ray absorption fine structure experiments were performed to study structural and dynamic aspects of the active site of various forms of myoglobin. The structures determined for deoxyMb, MbCO, and MbO2 are consistent with the structure established by X-ray absorption fine structure experiment and X-ray crystallography. The first shell of ferrous MbNO determined contains 5 nitrogens located at 2.02 A and a short NO bond length of 1.76 A. This study focuses on the change of the XAFS Debye-Waller factor with temperature, which is a measure of thermal and static disorder. It was found that the changes of Debye-Waller factor with temperature for the Mb proteins, except deoxyMb, are consistent with a simple Einstein model, in which a single frequency was assumed for the bond stretching modes. In contrast, the temperature dependence of deoxyMb cannot be fitted to the Einstein model and a large disorder was found at low temperatures, which indicates the existence of conformational substates of the active site." @default.
• W2073695209 created "2016-06-24" @default.
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• W2073695209 date "1991-04-01" @default.
• W2073695209 modified "2023-10-18" @default.
• W2073695209 title "Active site conformation in myoglobin as determined by X-ray absorption spectroscopy" @default.
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• W2073695209 doi "https://doi.org/10.1002/prot.340100402" @default.
• W2073695209 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1946338" @default.
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