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. 1999 Mar;76(3):1532–1536. doi: 10.1016/S0006-3495(99)77312-1

Heterotropic effectors exert more significant strain on monoligated than on unligated hemoglobin.

M Coletta 1, M Angeletti 1, I Ascone 1, G Boumis 1, A C Castellano 1, M Dell'Ariccia 1, S Della Longa 1, G De Sanctis 1, A M Priori 1, R Santucci 1, A Feis 1, G Amiconi 1
PMCID: PMC1300129  PMID: 10049333

Abstract

The effect of allosteric effectors, such as inositol hexakisphosphate and/or bezafibrate, has been investigated on the unliganded human adult hemoglobin both spectroscopically (employing electronic absorption, circular dichroism, resonance Raman, and x-ray absorption near-edge spectroscopies) and functionally (following the kinetics of the first CO binding step up to a final 4% ligand saturation degree). All data indicate that the unliganded T-state is not perturbed by the interaction with either one or both effectors, suggesting that their functional influence is only exerted when a ligand molecule is bound to the heme. This is confirmed by the observation that CO dissociation from partially liganded hemoglobin ( </= 0.04) is strongly altered by the presence of either effector, and the effect is enhanced whenever the two effectors are simultaneously present. Altogether, these data are a direct demonstration of the occurrence of a strain induced by the presence of a ligand molecule bound to the heme, and for the first time there is a clear indication that the expression of the functional heterotropic effect by these non-heme ligands requires this strain, which is not present in the unliganded molecule.

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Selected References

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