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• W2109406609 abstract "The structure of the complex of the ambidentate ligand thiocyanate with horse methemoglobin was compared with that of acid methemoglobin and azide methemoglobin by X-ray difference Fourier techniques. Thiocyanate is co-ordinated to iron exclusively by its nitrogen atom, and thus forms the isothiocyanate complex. The ligand is bent as in the stereochemically very similar azide complex, and there is no evidence for strain in the ligand pocket of the globin, in contrast to earlier results on the cyanide complex. The higher spin of the isothiocyanate complex compared with azide is accompanied by only slight structural changes at the hemes, the most prominent of which is interpreted to be a slight lengthening of the iron—ligand nitrogen bond in the β-heme." @default.
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• W2109406609 date "1981-02-01" @default.
• W2109406609 modified "2023-09-27" @default.
• W2109406609 title "Structure of isothiocyanate methemoglobin" @default.
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• W2109406609 doi "https://doi.org/10.1016/0022-2836(81)90316-8" @default.
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