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- W1982384920 abstract "The thermochromism of ferric azide hemoglobin and myoglobin was examined in a 0–35°C range and the visible spectra of the two spin isomers were separated from the analysis of the thermochromism. (1) The separated low-spin spectra exhibit intensified 540 and 570 nm peaks and a red-shifted Soret band. The high-spin spectra show characteristic 4-banded visible absorption, which is significantly different from the spectrum of 5-coordinate azide hemin, suggesting that the heme iron of azide hemoprotein remains 6-coordinate during the spin-state transition. (2) A larger thermochromism was observed in carp azide methemoglobin bound with inositol hexaphosphate, in contrast with the results reported on human hemoglobin. The difference between the human and carp hemoglobins was consistently explained in terms of an equilibrium coexistence of the R and T conformers in human azide methemoglobin bound with inositol hexaphosphate." @default.
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- W1982384920 date "1985-04-01" @default.
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- W1982384920 title "Thermochromism of the azide complexes of ferric hemoproteins" @default.
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- W1982384920 doi "https://doi.org/10.1016/0167-4838(85)90303-6" @default.
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