ORCID Profile
0000-0002-7889-9920
Current Organisation
Delft University of Technology
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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: Royal Society of Chemistry (RSC)
Date: 2022
DOI: 10.1039/D2CC02411J
Abstract: Soluble hydrogenase enables atom efficient, H 2 -driven, recycling of synthetic nicotinamide cofactors.
Publisher: American Chemical Society (ACS)
Date: 24-08-2016
DOI: 10.1021/JACS.6B05625
Abstract: Understanding the mechanisms of enzymatic hydride transfer with nicotinamide coenzyme biomimetics (NCBs) is critical to enhancing the performance of nicotinamide coenzyme-dependent biocatalysts. Here the temperature dependence of kinetic isotope effects (KIEs) for hydride transfer between "better than nature" NCBs and several ene reductase biocatalysts is used to indicate transfer by quantum mechanical tunneling. A strong correlation between rate constants and temperature dependence of the KIE (ΔΔH(⧧)) for H/D transfer implies that faster reactions with NCBs are associated with enhanced donor-acceptor distance s ling. Our analysis provides the first mechanistic insight into how NCBs can outperform their natural counterparts and emphasizes the need to optimize donor-acceptor distance s ling to obtain high catalytic performance from H-transfer enzymes.
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.
No related grants have been discovered for Caroline Paul.