Thermodynamic Parameters of pH-dependent Optical Transition in Bovine Heart Cytochrome c Oxidase

Abubakar, M.K; Lawal, M; Bilbis, L.S

dc.contributor.author	Abubakar, M.K
dc.contributor.author	Lawal, M
dc.contributor.author	Bilbis, L.S
dc.date.accessioned	2017-10-31T12:40:00Z
dc.date.available	2017-10-31T12:40:00Z
dc.date.issued	1992-02
dc.identifier.issn	0189-4757
dc.identifier.uri	http://hdl.handle.net/123456789/309
dc.description.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.	en_US
dc.language.iso	en	en_US
dc.publisher	Nigerian Journal of Biochemistry and Molecular Biology	en_US
dc.subject	Department of Biochemistry	en_US
dc.title	Thermodynamic Parameters of pH-dependent Optical Transition in Bovine Heart Cytochrome c Oxidase	en_US
dc.type	Article	en_US