Effects of large anphiphilic ligands upon the spectra and kinetics of cytochrome C oxidase


Autoria(s): He, Chia.
Contribuinte(s)

Department of Biological Sciences

Data(s)

09/07/2009

09/07/2009

09/07/1992

Resumo

Cytoch ro me c oxidase (ferrocytochrome c : 02 oxidoreductase ; EC 1.9. 3.1) is the terminal enzyme in the mitochondrial electron transport chain, catalyzing the transfer of electrons from ferrocytochrome c to molecular oxygen. The effects of two large amphiphilic molecules .. valinomycin and dibucaine upon the spectra of the isolated enzyme and upon the activity of both isolated enzyme and enzyme in membrane systems are investigated by using spectrophotometric and oxygen electrode techniques. The results show that both valinomycin and dibucaine change the Soret region of the spectrum and cause a partial inhibition in a concentration range higher than that in which they act as ionophores. It is concluded that both valinomycin and dibucain~ binding induce a conformational change of the protein structure which modifies the spectrum of the a3 CUB centre and diminishes the rate of electron transfer between cytochrome a and the binuclear centre.

Identificador

http://hdl.handle.net/10464/1843

Idioma(s)

eng

Publicador

Brock University

Palavras-Chave #Cytochrome oxidase. #Cytochrome c. #Ligands. #Enzymes--Synchesis.
Tipo

Electronic Thesis or Dissertation