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Title: Alternative approaches to the study of Rieske dioxygenases provide new insights into biotransformation properties and mechanisms
Author: Mundi, Harpinder
ISNI:       0000 0004 2722 2105
Awarding Body: Queen's University Belfast
Current Institution: Queen's University Belfast
Date of Award: 2011
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Rieske dioxygenase systems, particularly the naphthalene dioxygenase from Piputida 9816-4, have been extensively studied over the years. However, the emergence of Rieske dioxygenases with no associated electron transport proteins, such as the naphthalene dioxygenase from Rhodococcus sp. NCIMB 12038, presents new challenges for this field. This study aims to further the understanding of Rieske dioxygenases by establish novel methods to investigate them and the naphthalene ClS- dihydrodiol dehydrogenase associated. During the course of this investigation, new features on Rieske dioxygenase mechanism are revealed with key amino acids in the active sites being identified, and the discovery of peroxidase-like capabilities of the naphthalene dioxygenase opens the door to new investigations of this group of enzymes. Three very different lines of study come together to reveal capability of Rieske dioxygenases that have previously not been reported.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available