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dc.contributor.authorBrooks, Stephen P. J.en_US
dc.date.accessioned2009-06-09T18:16:33Z
dc.date.available2009-06-09T18:16:33Z
dc.date.issued1981-06-09T18:16:33Z
dc.identifier.urihttp://hdl.handle.net/10464/1581
dc.description.abstractIncreasing citrate concentration, at constant ionic strength (30 mM) decreases the rate of cytochrome ~ reduction by ascorbate. This effect is also seen at both high (600 mM) and low (19 mM) ionic strengths, and the Kapp for citrate increases with increasing ionic strength. Citrate binds d both ferri -and ferrocytochrome ~, but with a lower affinity for the latter form (Kox . .red d = 2 mM, Kd = 8 mM) as shown by an equilibrium assay with N,N,N',N', Tetramethyl E- phenylenediamine. The reaction of ferricytochrome ~with cyanide is also altered in the presence of citrate: citrate increases the K~PP for cyanide. Column chromatography of cytochrome ~-cytochrome oxidase mixtures shows citrate increases the dissociation constant of the complex. These results are confirmed in kinetic assays for the "loose"site (Km = 20 pM) only. The effect of increasing citrate observable at the "tight" site (Km = 0.25 pM) is on the turnover number and not on the K . These results suggest a mechanism m where anion binding to cytochrome £ at the tight site affects the equilibrium between two forms of cytochrome c bound cytochrome oxidase: an active and an inactive one.en_US
dc.language.isoengen_US
dc.publisherBrock Universityen_US
dc.subjectCytochrome c.en_US
dc.subjectOxidation-reduction reaction.en_US
dc.subjectOxidases.en_US
dc.subjectCitrates.en_US
dc.titleEffect of citrate on the redox properties of cytochrome C and its kinetic and binding behaviour with cytochrome oxidase /en_US
dc.typeElectronic Thesis or Dissertationen_US
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


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