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Title: Selective hydroxylations catalysed by cytochrome P-450 monooxygenases
Author: Chow, Cathy Sze-Yu
Awarding Body: University of Edinburgh
Current Institution: University of Edinburgh
Date of Award: 1998
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The biohydroxylation potential of the mutant enzyme, cytochrome P-450 cam Y96A monooxygenase (Y96A), has been investigated with a series of substrates which differ structurally from that of the natural substrate, D-(+)-camphor. Design of substrates essentially consisted of coupling an aromatic side-chain with an alicyclic moiety via an ester, ether or amide link. Assays have been performed with Y96A in order to obtain data on key factors of the biohydroxylation reaction such as substrate binding and turnover to give hydroxylated products. Y96A research has been complemented by a thorough investigation of the biohydroxylation capability of bacterium, Rhodococcus rhodochrous NCIMB 9703. Compounds found to be inactive with Y96A were reacted with this whole cell system, and positive results have been achieved in all cases.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available