A Calorimetric Study of the CO Bohr Effect of Monomeric Haemoglobins
- 1 March 1976
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 62 (3) , 577-582
- https://doi.org/10.1111/j.1432-1033.1976.tb10192.x
Abstract
A calorimetric study has been made of the heats of CO reaction with the monomeric haemoglobins of Chironomus thummi thummi III and IV as a function of pH. The number of Bohr protons released at pH 7.1 was determined from heats of reaction in different buffers as 0.19 and 0.31 mol H+/mol CO for haemoglobin III and IV respectively. The heat of the Bohr ionization process was found to be 6 and 8 kcal/mol H+ (25 and 34 kJ/mol) for the haemoglobins III and IV. These values are consistent with values found for histidine groups. A pH-independent part of the reaction enthalpy was determined as - 19.7 kcal/mol CO (-82.4 kJ/mol). The same reaction with myoglobin is less exothermic. From the combination of deltaG0 and deltaH0 values TdeltaS0 values have been calculated. It was found for both haemoglobins that the entropy of reaction is greater by 2 cal K-1 mol-1 (8.4 JK-1 mol-1) at pH 9.5 as compared to pH 6.0.Keywords
This publication has 10 references indexed in Scilit:
- Heats of carbon monoxide binding by hemoglobin M IwateBiochemistry, 1975
- Ligand‐Specific Bohr Effect in HaemoglobinsEuropean Journal of Biochemistry, 1974
- The Bohr Proton‐Binding Site in a Monomeric HaemoglobinEuropean Journal of Biochemistry, 1972
- Calorimetric study of the binding of carbon monoxide to myoglobinBiochemistry, 1972
- Heterotropic Allosterism of Monomeric Haemoglobins of Chironomus thummi thummiEuropean Journal of Biochemistry, 1972
- The Atomic Structure of Erythrocruorin in the Light of the Chemical Sequence and its Comparison with MyoglobinEuropean Journal of Biochemistry, 1971
- Structures of deoxy- and carbonmonoxy-erythrocruorinJournal of Molecular Biology, 1970
- Die O2‐Bindungseigenschaften einiger Larvalhamoglobine von Chironomus th. thummiEuropean Journal of Biochemistry, 1969
- Properties of the α and β Chains of Hemoglobin Prepared from Their Mercuribenzoate Derivatives by Treatment with 1-DodecanethiolPublished by Elsevier ,1967
- Linked Functions and Reciprocal Effects in Hemoglobin: A Second LookAdvances in Protein Chemistry, 1964