Extreme halophilic alcohol dehydrogenase mediated highly efficient syntheses of enantiopure aromatic alcohols
Enzymatic synthesis of enantiopure aromatic secondary alcohols (including substituted, heteroaromatic and bicyclic structures) were carried out using the halophilic alcohol dehydrogenase ADH2 from Haloferax volcanii (HvADH2). This enzyme showed an unprecedented substrate scope and absolute enatiosel...
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| Format: | Article |
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Royal Society of Chemistry
2017
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| Online Access: | https://eprints.nottingham.ac.uk/47804/ |
| _version_ | 1848797633290698752 |
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| author | Alsafadi, Diya Alsalman, Safaa Paradisi, Francesca |
| author_facet | Alsafadi, Diya Alsalman, Safaa Paradisi, Francesca |
| author_sort | Alsafadi, Diya |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | Enzymatic synthesis of enantiopure aromatic secondary alcohols (including substituted, heteroaromatic and bicyclic structures) were carried out using the halophilic alcohol dehydrogenase ADH2 from Haloferax volcanii (HvADH2). This enzyme showed an unprecedented substrate scope and absolute enatioselectivity. The cofactor NADPH was used catalytically and regenerated in-situ by the biocatalyst, in the presence of 5% ethanol. The efficiency of HvADH2 for conversion of aromatic ketones was markedly influenced by the steric and electronic factors as well as the solubility of ketones in the reaction medium. Furthermore, carbonyl stretching bands frequencies ν ( ) have been measured for different ketones to understand the effect of electron withdrawing or donating properties of the ketones substituents on the reaction rate catalyzed by HvADH2. Good correlation was observed between ν ( ) of methyl aryl-ketones and the reaction rate catalyzed by HvADH2. The enzyme catalyzed the reductions of ketone substrates on the preparative scale, demonstrating that HvADH2 would be a valuable biocatalyst for the preparation of chiral aromatic alcohols of pharmaceutical interest. |
| first_indexed | 2025-11-14T20:06:59Z |
| format | Article |
| id | nottingham-47804 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T20:06:59Z |
| publishDate | 2017 |
| publisher | Royal Society of Chemistry |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-478042020-05-04T19:12:51Z https://eprints.nottingham.ac.uk/47804/ Extreme halophilic alcohol dehydrogenase mediated highly efficient syntheses of enantiopure aromatic alcohols Alsafadi, Diya Alsalman, Safaa Paradisi, Francesca Enzymatic synthesis of enantiopure aromatic secondary alcohols (including substituted, heteroaromatic and bicyclic structures) were carried out using the halophilic alcohol dehydrogenase ADH2 from Haloferax volcanii (HvADH2). This enzyme showed an unprecedented substrate scope and absolute enatioselectivity. The cofactor NADPH was used catalytically and regenerated in-situ by the biocatalyst, in the presence of 5% ethanol. The efficiency of HvADH2 for conversion of aromatic ketones was markedly influenced by the steric and electronic factors as well as the solubility of ketones in the reaction medium. Furthermore, carbonyl stretching bands frequencies ν ( ) have been measured for different ketones to understand the effect of electron withdrawing or donating properties of the ketones substituents on the reaction rate catalyzed by HvADH2. Good correlation was observed between ν ( ) of methyl aryl-ketones and the reaction rate catalyzed by HvADH2. The enzyme catalyzed the reductions of ketone substrates on the preparative scale, demonstrating that HvADH2 would be a valuable biocatalyst for the preparation of chiral aromatic alcohols of pharmaceutical interest. Royal Society of Chemistry 2017-10-16 Article PeerReviewed Alsafadi, Diya, Alsalman, Safaa and Paradisi, Francesca (2017) Extreme halophilic alcohol dehydrogenase mediated highly efficient syntheses of enantiopure aromatic alcohols. Organic and Biomolecular Chemistry . ISSN 1477-0520 http://pubs.rsc.org/en/content/articlelanding/2017/ob/c7ob02299a#!divAbstract doi:10.1039/C7OB02299A doi:10.1039/C7OB02299A |
| spellingShingle | Alsafadi, Diya Alsalman, Safaa Paradisi, Francesca Extreme halophilic alcohol dehydrogenase mediated highly efficient syntheses of enantiopure aromatic alcohols |
| title | Extreme halophilic alcohol dehydrogenase mediated highly efficient syntheses of enantiopure aromatic alcohols |
| title_full | Extreme halophilic alcohol dehydrogenase mediated highly efficient syntheses of enantiopure aromatic alcohols |
| title_fullStr | Extreme halophilic alcohol dehydrogenase mediated highly efficient syntheses of enantiopure aromatic alcohols |
| title_full_unstemmed | Extreme halophilic alcohol dehydrogenase mediated highly efficient syntheses of enantiopure aromatic alcohols |
| title_short | Extreme halophilic alcohol dehydrogenase mediated highly efficient syntheses of enantiopure aromatic alcohols |
| title_sort | extreme halophilic alcohol dehydrogenase mediated highly efficient syntheses of enantiopure aromatic alcohols |
| url | https://eprints.nottingham.ac.uk/47804/ https://eprints.nottingham.ac.uk/47804/ https://eprints.nottingham.ac.uk/47804/ |