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- W2041330227 abstract "Allosteric parameters (KT, KR, and Ln) of hemoglobin (Hb) are normally determined by thermodynamic analyses of oxygen-binding isotherma according to the Monod-Wyman-Changeux two-state concerted model [1]. KT and KR are independent of ligation states [1,2], whereas Ln is a function of the number of ligands bound. On the other hands, in structure-linked graded models such as the Koshland-Nemethy-Filmer sequential model [3], the Perutz steroechemical model [4], and the Eaton et al. tertiary two-state (TTS) model [5], the oxygen-affinity (Kn (n = 1, 2, 3, & 4)) of Hb is linked to certain ligation-induced structural changes (tertiary and/or quaternary) such as changes in salt bridges and T/R-quaternary structures. Then, the oxygen-binding processes become circular reversible kinetic processes, as schematically shown in the figure, rather than the truely reversible kinetic process as expected thermodynamically. Supported by NIH HL14508. Reference: [1] Monod, Wyman,Changeux J. Mol. Biol 12 (1965) 88-118. [2] Yonetani, Laberge BBA 1784 (2008) 1146-1158. [3] Koshland, Nemethy, Filmer Biochemistry 5 (1966) 365-385. [4] Perutz Nature 228 (1970) 726-739. [5] Eaton et al. IUBMB Life 59 (2007) 586-599." @default.
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- W2041330227 date "2009-02-01" @default.
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- W2041330227 title "Allosteric Mechanism of Hemoglobin: Concerted Mechanisms or Graded Mechanisms" @default.
- W2041330227 doi "https://doi.org/10.1016/j.bpj.2008.12.2244" @default.
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