Thermodynamic Parameters of pH-dependent Optical Transition in Bovine Heart Cytochrome c Oxidase
Abstract
Cytochrome c oxidase was prepared according to the method of Yonetani (1961), The pH-induced optical
transition in the oxidised (resting) enzyme was studied between 400 and 500 nm at different temperatures, The changes
in 'enthalpy, entropy and free energy for the transition were determined to be -37.89 ± 6.20KJ/mole, - 158.16 ± 8.20 JK"
mole" and -41.60KJ/inole respectively. The results are discussed in terms of the binding of a strong ligand (possibly
histidine) to the distal side of an already pentacoordinate high spin cytochrome as.
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