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Title: Mechanistic aspects of the monooxygenase system from Methylococcus capsulatus
Author: Waters, Barry Williams
ISNI:       0000 0001 3563 8758
Awarding Body: University of Warwick
Current Institution: University of Warwick
Date of Award: 1982
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The soluble nature of the monooxygenase system from Methylococcus casulatus (Bath) makes it an ideal monooxygenase enzyme for mechanistic studies. Oxidation of substituted aromatic substrates gave products that were oxidised in the para-position of the ring, the efficiency of the process being dependent upon the size of the substituent group. During these oxidations of aromatic substrates products resulting from an 'NIH' shift were observed. In the case of naphthalene, this led to substantial quantities of 2-naphthol in addition to the more usual product, l-naphthol, observed with this type of enzyme. Substituted aromatic compounds were also oxidised on the side chain, predominantly  to the aromatic ring, with -methylstyrene providing the only exception. The efficiency of the oxidation of the aromatic side-chain was also found to be dependent on the nature of the substituent group. Oxidation of cyclopropane to cyclopropanol, of methyl- cyclopropane to cyclopropylcarbinol and of olefinic groups with retention of configuration suggests an oxenoid mechanism.
Supervisor: Not available Sponsor: Imperial Chemical Industries Ltd ; Science and Engineering Research Council
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available
Keywords: QP Physiology ; QR Microbiology