ORCID Profile
0000-0002-9262-8000
Current Organisation
University of Oxford
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Publisher: Wiley
Date: 12-06-2020
Publisher: Royal Society of Chemistry (RSC)
Date: 2023
DOI: 10.1039/D3SC01718D
Publisher: Wiley
Date: 11-05-2021
Abstract: A new activity for the [NiFe] uptake hydrogenase 1 of Escherichia coli (Hyd1) is presented. Direct reduction of biological flavin cofactors FMN and FAD is achieved using H 2 as a simple, completely atom‐economical reductant. The robust nature of Hyd1 is exploited for flavin reduction across a broad range of temperatures (25–70 °C) and extended reaction times. The utility of this system as a simple, easy to implement FMNH 2 or FADH 2 regenerating system is then demonstrated by supplying reduced flavin to Old Yellow Enzyme “ene‐reductases” to support asymmetric alkene reductions with up to 100 % conversion. Hyd1 turnover frequencies up to 20.4 min −1 and total turnover numbers up to 20 200 were recorded during flavin recycling.
Publisher: The Royal Society
Date: 08-2016
Abstract: Life has existed on the Earth for approximately four billion years. The sheer depth of evolutionary time, and the ersity of extant species, makes it tempting to assume that all the key biochemical innovations underpinning life have already happened. But we are only a little over halfway through the trajectory of life on our planet. In this Opinion piece, we argue: (i) that sufficient time remains for the evolution of new processes at the heart of metabolic biochemistry and (ii) that synthetic biology is providing predictive insights into the nature of these innovations. By way of ex le, we focus on engineered solutions to existing inefficiencies in energy generation, and on the complex, synthetic regulatory circuits that are currently being implemented.
Publisher: Springer Science and Business Media LLC
Date: 19-03-2020
DOI: 10.1038/S41467-020-15310-Z
Abstract: Enzymes dependent on nicotinamide cofactors are important components of the expanding range of asymmetric synthetic techniques. New challenges in asymmetric catalysis are arising in the field of deuterium labelling, where compounds bearing deuterium ( 2 H) atoms at chiral centres are becoming increasingly desirable targets for pharmaceutical and analytical chemists. However, utilisation of NADH-dependent enzymes for 2 H-labelling is not straightforward, owing to difficulties in supplying a suitably isotopically-labelled cofactor ([4- 2 H]-NADH). Here we report on a strategy that combines a clean reductant (H 2 ) with a cheap source of 2 H-atoms ( 2 H 2 O) to generate and recycle [4- 2 H]-NADH. By coupling [4- 2 H]-NADH-recycling to an array of C=O, C=N, and C=C bond reductases, we demonstrate asymmetric deuteration across a range of organic molecules under ambient conditions with near-perfect chemo-, stereo- and isotopic selectivity. We demonstrate the synthetic utility of the system by applying it in the isolation of the heavy drug (1 S ,3’ R )-[2’,2’,3’- 2 H 3 ]-solifenacin fumarate on a preparative scale.
Publisher: Wiley
Date: 11-05-2021
Abstract: A new activity for the [NiFe] uptake hydrogenase 1 of Escherichia coli (Hyd1) is presented. Direct reduction of biological flavin cofactors FMN and FAD is achieved using H 2 as a simple, completely atom‐economical reductant. The robust nature of Hyd1 is exploited for flavin reduction across a broad range of temperatures (25–70 °C) and extended reaction times. The utility of this system as a simple, easy to implement FMNH 2 or FADH 2 regenerating system is then demonstrated by supplying reduced flavin to Old Yellow Enzyme “ene‐reductases” to support asymmetric alkene reductions with up to 100 % conversion. Hyd1 turnover frequencies up to 20.4 min −1 and total turnover numbers up to 20 200 were recorded during flavin recycling.
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Miguel Ramirez Hernandez.