Biotransformations of hydroxylamine derivatives
The results presented herein represent a programme focussed towards producing a deracemisation system for hydroxylamines. A number of different avenues have been explored. The use of a number of biocatalytic systems was investigated in an attempt to construct a one-pot system. These included a novel...
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University of Edinburgh
2007
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ndltd-bl.uk-oai-ethos.bl.uk-6504212016-06-21T03:22:27ZBiotransformations of hydroxylamine derivativesEve, Tom S. C.2007The results presented herein represent a programme focussed towards producing a deracemisation system for hydroxylamines. A number of different avenues have been explored. The use of a number of biocatalytic systems was investigated in an attempt to construct a one-pot system. These included a novel application of monoamine N and laccase enzymes. The enantioselective oxidation of hydroxylamine ethers by MAO-N was a novel discovery. A further development is the engineering of a MAO-N variant which displayed improved catalytic activity for a model hydroxylamine ether substrate compared with the parental enzyme. A second research programme lead to the discovery of the applicability of a laccase:mediator system to the oxidation of hydroxylamines. Investigations into oxime reduction systems with reaction conditions that were complementary to the biocatalytic systems were performed.572.7University of Edinburghhttp://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.650421http://hdl.handle.net/1842/14813Electronic Thesis or Dissertation |
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572.7 |
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572.7 Eve, Tom S. C. Biotransformations of hydroxylamine derivatives |
| description |
The results presented herein represent a programme focussed towards producing a deracemisation system for hydroxylamines. A number of different avenues have been explored. The use of a number of biocatalytic systems was investigated in an attempt to construct a one-pot system. These included a novel application of monoamine N and laccase enzymes. The enantioselective oxidation of hydroxylamine ethers by MAO-N was a novel discovery. A further development is the engineering of a MAO-N variant which displayed improved catalytic activity for a model hydroxylamine ether substrate compared with the parental enzyme. A second research programme lead to the discovery of the applicability of a laccase:mediator system to the oxidation of hydroxylamines. Investigations into oxime reduction systems with reaction conditions that were complementary to the biocatalytic systems were performed. |
| author |
Eve, Tom S. C. |
| author_facet |
Eve, Tom S. C. |
| author_sort |
Eve, Tom S. C. |
| title |
Biotransformations of hydroxylamine derivatives |
| title_short |
Biotransformations of hydroxylamine derivatives |
| title_full |
Biotransformations of hydroxylamine derivatives |
| title_fullStr |
Biotransformations of hydroxylamine derivatives |
| title_full_unstemmed |
Biotransformations of hydroxylamine derivatives |
| title_sort |
biotransformations of hydroxylamine derivatives |
| publisher |
University of Edinburgh |
| publishDate |
2007 |
| url |
http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.650421 |
| work_keys_str_mv |
AT evetomsc biotransformationsofhydroxylaminederivatives |
| _version_ |
1718312554487349248 |