Analysis of oxygen binding by hemoglobin on the basis of mean intrinsic thermodynamic quantities

• Authors: Abdol-Khalegh Bordbar , Sayed Habib-Allah Mousavi , Hamid Dazhampanah
• Languages of publication: EN

Abstracts

EN

The binding data for oxygenation of human hemoglobin, Hb, at various temperatures and in the absence and presence of 2,3-diphosphoglycerate, DPG, and inositol hexakis phosphate, IHP, were analyzed for extraction of mean intrinsic Gibbs free energy, ΔGo, enthalpy, ΔHo, and entropy, ΔSo, of binding at various partial oxygen pressures. This method of analysis considers all the protein species present such as dimer and tetramer forms which were not considered by Imai et al. (Imai K et al., 1970, Biochim Biophys Acta 200: 189 - 196) , in their analysis which was based on Adair equation. In this regard, the values of Hill equation parameters were estimated with high precision at all points of the binding curve and used for calculation of ΔGo, ΔHo and ΔSo were also calculated by analysis of ΔGo values at various temperatures using van't Hoff equation. The results represent the enthalpic nature of the cooperativity in Hb oxygenation and the compensation effect of intrinsic entropy. The interpretation of results also to be, into account the decrease of the binding affinity of sites for oxygen in the presence of DPG and IHP without any considerable changes in the site - site interaction (extent of cooperativity). In other words, the interactions between bound ligands, organic phosphates and oxygen, are more due to a decreasing binding affinity and not to the reduction of the cooperative interaction between sites. The results also document the more heterotropic effect of IHP compared to DPG.

Keywords

EN

cooperativity; mean intrinsic Gibbs free energy; linkage phenomena; hemoglobin

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2006
• Volume: 53
• Issue: 3
• Pages: 563-568

Dates

published

2006

received

2006-05-01

revised

2006-08-18

accepted

2006-09-04

(unknown)

2006-10-01

Contributors

author

Abdol-Khalegh Bordbar

• Laboratory of Biophysical Chemistry, Department of Chemistry, Isfahan University, Isfahan, Iran

author

Sayed Habib-Allah Mousavi

• Laboratory of Biophysical Chemistry, Department of Chemistry, Isfahan University, Isfahan, Iran

author

Hamid Dazhampanah

• Laboratory of Biophysical Chemistry, Department of Chemistry, Isfahan University, Isfahan, Iran

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