Microsecond Laser Flash Photolysis of the CO-Complex of Bovine Heart Cytochrome c Oxidase

Abubakar, M.K; Bilbis, L.S; Shehu, R.A

dc.contributor.author	Abubakar, M.K
dc.contributor.author	Bilbis, L.S
dc.contributor.author	Shehu, R.A
dc.date.accessioned	2017-10-31T09:22:53Z
dc.date.available	2017-10-31T09:22:53Z
dc.date.issued	1999
dc.identifier.issn	0189·4757
dc.identifier.uri	http://hdl.handle.net/123456789/258
dc.description.abstract	the fully reduced and mixed valence enzyme was prepared as described by Bicker et al. (1984). Kinetics of CO rebinding subsequent to Laser photolysis was studied at 430nm by using a 20ns pulsed at 532nm vertically polarized Laser beam of 2mJ energy. The results suggest differences in photodynamic behaviour of the fully reduced and mixed valence forms of the enzyme. The most important implication of this, is at the conformational changes associated with the reduction of the low spin cytochrome a affects the ligation dynamic of the oxygen reduction site via heterotropic interaction.	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	Microsecond Laser Flash Photolysis of the CO-Complex of Bovine Heart Cytochrome c Oxidase	en_US
dc.type	Article	en_US