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• W2051817967 abstract "The low-frequency regions of resonance Raman spectra of various low-spin ferrous forms of normal human hemoglobin, soybean leghemoglobin a and of horse myoglobin are reported. Differences observed among the spectra of oxygenated and nitrosyl forms of these hemoproteins show that their globins impose various low-spin heme structures. A quantitative correlation between the variable frequency of resonance Raman band II (215–271 cm−1) and the iron atom-heme plane distance was observed for hemoproteins and heme models, either ferrous or ferric, high-spin or low-spin. From this correlation, the iron atom-heme plane distance should be 0.3 Å in nitrosyl and oxymyoglobin (band II at 256 cm−1) whereas the iron position should be near to or in the heme plane for nitrosyl and oxy forms of hemoglobin and leghemoglobin (band II between 266 and 273 cm−1). A new method is proposed for monitoring the photodissociation processes in ferrohemoproteins." @default.
• W2051817967 created "2016-06-24" @default.
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• W2051817967 date "1981-12-01" @default.
• W2051817967 modified "2023-09-26" @default.
• W2051817967 title "Protoheme conformations in low-spin ferrohemoproteins. Resonance raman spectroscopy" @default.
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• W2051817967 doi "https://doi.org/10.1016/0005-2795(81)90133-1" @default.
• W2051817967 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7198917" @default.
• W2051817967 hasPublicationYear "1981" @default.
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