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Measurement of the protein-ligand bond energy of carboxymyoglobin by pulsed photoacoustic calorimetry

✍ Scribed by W.P. Leung; K.C. Cho; S.K. Chau; C.L. Choy

Publisher
Elsevier Science
Year
1987
Tongue
English
Weight
414 KB
Volume
141
Category
Article
ISSN
0009-2614

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✦ Synopsis

Pulsed photoacoustic spectroscopy has been used to study two horse heart myoglobin derivatives, deoxymyoglobin and carboxymyoglobin, in the temperature range of O-25%. The myoglobin-CO bond energy has been measured to be 13.4+ 0.5 kcal/mole. The volume change associated with the photodissociation of carboxymyoglobin into deoxymyoglobin and CO has also been observed.

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