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dc.contributor.advisorIngledew, W. John
dc.contributor.authorBacon, Mark
dc.coverage.spatial235 p.en_US
dc.description.abstractThe prosthetic groups of cytochrome o, the terminal ubiquinol:dioxygen oxido-reductase of Escherichia coli, were investigated in the purified and in situ enzyme. The interactions between the redox-active centres, of which there are three, were characterised using optical, magnetic resonance and X-ray absorption spectroscopy techniques. The copper complement of this enzyme was investigated and the available data suggested a single copper centre associated with the ligand binding haem centre (haem o) forming a binuclear oxygen binding and reduction site. Two redox-active copper atoms are known to exist in the mammalian cytochrome c oxidase complex and the consequences of the different copper stoicheiometries, in these enzymes, are discussed. Spatial and organisational investigations are described and a model for the binuclear reaction site presented. The location of the haem centres was determined using low-temperature EPR spectroscopy by observing the effects on the relaxation behaviour of these centres in the presence of an extrinsic paramagnetic probe.en_US
dc.publisherUniversity of St Andrews
dc.subject.lcshCytochrome oxidaseen
dc.titleProsthetic group organisation and interaction in the 'Escherichia coli' oxygen reductase; cytochrome Oen_US
dc.type.qualificationnamePhD Doctor of Philosophyen_US
dc.publisher.institutionThe University of St Andrewsen_US

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