Files in this item
Prosthetic group organisation and interaction in the 'Escherichia coli' oxygen reductase; cytochrome O
Item metadata
dc.contributor.advisor | Ingledew, W. John | |
dc.contributor.author | Bacon, Mark | |
dc.coverage.spatial | 235 p. | en_US |
dc.date.accessioned | 2018-06-22T08:19:57Z | |
dc.date.available | 2018-06-22T08:19:57Z | |
dc.date.issued | 1993 | |
dc.identifier.uri | https://hdl.handle.net/10023/14435 | |
dc.description.abstract | The 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.language.iso | en | en_US |
dc.publisher | University of St Andrews | |
dc.subject.lcc | QP603.C85B2 | |
dc.subject.lcsh | Cytochrome oxidase | en |
dc.title | Prosthetic group organisation and interaction in the 'Escherichia coli' oxygen reductase; cytochrome O | en_US |
dc.type | Thesis | en_US |
dc.type.qualificationlevel | Doctoral | en_US |
dc.type.qualificationname | PhD Doctor of Philosophy | en_US |
dc.publisher.institution | The University of St Andrews | en_US |
This item appears in the following Collection(s)
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.