{"id":{"repo_id":"brock","oai_identifier":"oai:brocku.scholaris.ca:10464/1581"},"canonical_url":"https://search.dev.ndltd.org/etd/brock/oai:brocku.scholaris.ca:10464/1581","repository":{"repo_id":"brock","name":"Brock University","base_url":"https://brocku.scholaris.ca/server/oai/request"},"display":{"title":"Effect of citrate on the redox properties of cytochrome C and its kinetic and binding behaviour with cytochrome oxidase /","abstract":"Increasing 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.","abstract_html":"Increasing 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.","abstract_has_math":false,"creators":["Brooks, Stephen P. J."],"institution":"Brock University","degree_name":"M.Sc. Biological Sciences","degree_level":"Masters","degree_discipline":"Faculty of Mathematics and Science","degree_department":"Department of Biological Sciences","school":null,"contributors":[],"advisors":[],"committee_chairs":[],"committee_members":[],"year":1981,"date_issued":"1981-06-09T18:16:33Z","date_published":"1981-06-09T18:16:33Z","updated_at":"2026-07-24T01:23:16Z","subjects":["Cytochrome c.","Oxidation-reduction reaction.","Oxidases.","Citrates."],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/10464/1581","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.department","label":"Department","values":["Department of Biological Sciences"]},{"key":"dc:creator","label":"Author","values":["Brooks, Stephen P. 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Biological Sciences"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["Brock University"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Cytochrome c.","Oxidation-reduction reaction.","Oxidases.","Citrates."]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["http://hdl.handle.net/10464/1581"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Increasing 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."]},{"key":"dc:title","label":"Title","values":["Effect of citrate on the redox properties of cytochrome C and its kinetic and binding behaviour with cytochrome oxidase /"]}]}],"canonical_facts":{"dc:contributor.department":["Department of Biological Sciences"],"dc:creator":["Brooks, Stephen P. J."],"dc:date.accessioned":["2009-06-09T18:16:33Z"],"dc:date.available":["2009-06-09T18:16:33Z"],"dc:date.issued":["1981-06-09T18:16:33Z"],"dc:description.abstract":["Increasing 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."],"dc:identifier.uri":["http://hdl.handle.net/10464/1581"],"dc:language.iso":["eng"],"dc:subject":["Cytochrome c.","Oxidation-reduction reaction.","Oxidases.","Citrates."],"dc:title":["Effect of citrate on the redox properties of cytochrome C and its kinetic and binding behaviour with cytochrome oxidase /"],"dc:type":["Electronic Thesis or Dissertation"],"thesis:degree_discipline":["Faculty of Mathematics and Science"],"thesis:degree_level":["Masters"],"thesis:degree_name":["M.Sc. Biological Sciences"],"thesis:institution_name":["Brock University"]},"updated_at":"2026-07-24T01:23:16Z"}