A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H
We demonstrate a recycling system for synthetic nicotinamide cofactor analogues using a soluble hydrogenase with turnover number of >1000 for reduction of the cofactor analogues by H2. Coupling this system to an ene reductase, we show quantitative conversion of N-ethylmaleimide to N-ethylsuccinim...
| Main Authors: | , , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
Royal Society of Chemistry
2022
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| _version_ | 1826308643319971840 |
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| author | Reeve, HA Nicholson, J Altaf, F Lonsdale, TH Preissler, J Lauterbach, L Lenz, O Leimkühler, S Hollmann, F Paul, CE Vincent, KA |
| author_facet | Reeve, HA Nicholson, J Altaf, F Lonsdale, TH Preissler, J Lauterbach, L Lenz, O Leimkühler, S Hollmann, F Paul, CE Vincent, KA |
| author_sort | Reeve, HA |
| collection | OXFORD |
| description | We demonstrate a recycling system for synthetic nicotinamide cofactor analogues using a soluble hydrogenase with turnover number of >1000 for reduction of the cofactor analogues by H2. Coupling this system to an ene reductase, we show quantitative conversion of N-ethylmaleimide to N-ethylsuccinimide. The biocatalyst system retained >50% activity after 7 h. |
| first_indexed | 2024-03-07T07:22:21Z |
| format | Journal article |
| id | oxford-uuid:176efb2b-3907-4da2-bb39-4cf14d40e869 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T07:22:21Z |
| publishDate | 2022 |
| publisher | Royal Society of Chemistry |
| record_format | dspace |
| spelling | oxford-uuid:176efb2b-3907-4da2-bb39-4cf14d40e8692022-11-04T10:42:28ZA hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)HJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:176efb2b-3907-4da2-bb39-4cf14d40e869EnglishSymplectic ElementsRoyal Society of Chemistry2022Reeve, HANicholson, JAltaf, FLonsdale, THPreissler, JLauterbach, LLenz, OLeimkühler, SHollmann, FPaul, CEVincent, KAWe demonstrate a recycling system for synthetic nicotinamide cofactor analogues using a soluble hydrogenase with turnover number of >1000 for reduction of the cofactor analogues by H2. Coupling this system to an ene reductase, we show quantitative conversion of N-ethylmaleimide to N-ethylsuccinimide. The biocatalyst system retained >50% activity after 7 h. |
| spellingShingle | Reeve, HA Nicholson, J Altaf, F Lonsdale, TH Preissler, J Lauterbach, L Lenz, O Leimkühler, S Hollmann, F Paul, CE Vincent, KA A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H |
| title | A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H |
| title_full | A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H |
| title_fullStr | A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H |
| title_full_unstemmed | A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H |
| title_short | A hydrogen-driven biocatalytic approach to recycling synthetic analogues of NAD(P)H |
| title_sort | hydrogen driven biocatalytic approach to recycling synthetic analogues of nad p h |
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