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• W2068505529 abstract "57Fe-enriched complexes of hemoglobin and myoglobin with CO and O2 were photodissociated at 4.2°K, and the resulting spectra were compared with those of the deoxy forms. Differences in both quadrupole splitting and isomer shift were noted for each protein, the photoproducts having smaller isomer shift and larger quadrupole splitting than the deoxy forms. The photoproducts of HbCO and HbCO2 had narrow absorption lines, indicating a well-defined iron environment. The corresponding myoglobin species had broader absorption lines, as did both deoxy forms. The weak absorption lines of photodissociated NO complexes appeared to be wide, possibly indicating magnetic interaction with the unpaired electron of the nearby NO." @default.
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• W2068505529 date "1976-04-01" @default.
• W2068505529 modified "2023-09-25" @default.
• W2068505529 title "Low temperature photodissociation studies of ferrous hemoglobin and myoglobin complexes by Mössbauer spectroscopy" @default.
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• W2068505529 doi "https://doi.org/10.1016/0304-4165(76)90036-2" @default.
• W2068505529 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1276159" @default.
• W2068505529 hasPublicationYear "1976" @default.
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