Enthalpy and conformational volume changes of mammalian oxy-hemoglobins investigated by pulsed photoacoustic calorimetry.
Enthalpy and conformational volume changes induced by laser photo-dissociation reactions of mammalian oxy-hemoglobin, such as human, bovine, pig, horse and rabbit oxy-hemoglobins, are investigated by pulsed photoacoustic calorimetry. Generally, the response time of the photoacoustic calorimetry is restricted by the width of the laser pulse and the bandwidth of the acoustic detector. Considering the time window of the experimental system, the enthalpy and conformational volume changes detected should be caused by the tertiary relaxation of the heme proteins. In order to calculate the enthalpy and conformational volume changes, the quantum yields of the photo-dissociation products of oxy-hemoglobins must be measured and taken into account. Finally, the enthalpy and conformational volume changes of the oxy-hemoglobins connected with the tertiary relaxation are obtained, which show that for all measured mammalian oxy-hemoglobins the values of enthalpy changes are in the range of 30.0-46.8 kcal/mol and volume changes are of 2.3-7.8 ml/mol although the quantum yields for the different species may have much bigger differences. A possible explanation of the results is presented.
Yang
Ning-li
NL
Laboratory of Modern Acoustics, Institute of Acoustics, Nanjing University, Nanjing 210093, PR China.
Zhang
Shu-yi
SY
Sun
Li
L
Qu
Min
M
Shui
Xiu-ji
XJ
Chen
Hui-lan
HL
D000465:Algorithms; D000818:Animals; D002151:Calorimetry / Q000379:methods*; D003198:Computer Simulation; D004548:Elasticity; D006801:Humans; D007834:Lasers; D008422:Materials Testing / Q000379:methods*; D008956:Models, Chemical; D010108:Oxyhemoglobins / Q000737:chemistry* / Q000648:ultrastructure*; D011487:Protein Conformation; D014465:Ultrasonics
D010108:Oxyhemoglobins