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dc.contributor.authorHe, Chia.en_US
dc.date.accessioned2009-07-09T17:34:54Z
dc.date.available2009-07-09T17:34:54Z
dc.date.issued1992-07-09T17:34:54Z
dc.identifier.urihttp://hdl.handle.net/10464/1843
dc.description.abstractCytoch 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.en_US
dc.language.isoengen_US
dc.publisherBrock Universityen_US
dc.subjectCytochrome oxidase.en_US
dc.subjectCytochrome c.en_US
dc.subjectLigands.en_US
dc.subjectEnzymes--Synchesis.en_US
dc.titleEffects of large anphiphilic ligands upon the spectra and kinetics of cytochrome C oxidaseen_US
dc.typeElectronic Thesis or Dissertationen
dc.degree.nameM.Sc. Biological Sciencesen_US
dc.degree.levelMastersen_US
dc.contributor.departmentDepartment of Biological Sciencesen_US
dc.degree.disciplineFaculty of Mathematics and Scienceen_US
refterms.dateFOA2021-08-07T02:01:27Z


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