Collective motion of iron and exogenous ligands in hemoglobin.
Mössbauer studies of deoxyhemoglobin (Hb), oxyhemoglobin (HbO2), and (carbonmonoxy)-hemoglobin (HbCO) have been performed providing information regarding the center shift (CS) up to 250 K and the recoil-free fraction (f) in the "solid state regime". The temperature dependence of the CS indicates that the effective mass of the iron in liganded hemoglobin includes the exogenous ligand, suggesting that vibrations of the iron are strongly coupled to those of the ligand. As a result of this coupled motion, the recoil-free fraction (f) provides a valuable probe for the shape of the potential energy surface in the ligand pocket. Thus HbO2 experiences a stronger restoring force than HbCO, which can be attributed to a steeper potential well for the oxygen into the ligand pocket.
Levy
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Laboratory of Cellular and Molecular Biology, National Institute on Aging, Gerontology Research Center, Baltimore, Maryland 21224.
D002263:Carboxyhemoglobin / Q000378:metabolism; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D006454:Hemoglobins / Q000378:metabolism*; D007501:Iron / Q000378:metabolism*; D008024:Ligands; D010108:Oxyhemoglobins / Q000378:metabolism; D015204:Spectroscopy, Mossbauer; D013696:Temperature
D006454:Hemoglobins; D008024:Ligands; D010108:Oxyhemoglobins; C100003:deoxyhemoglobin; D002263:Carboxyhemoglobin; D007501:Iron