Explore the words cloud of the enzC-Hem project. It provides you a very rough idea of what is the project "enzC-Hem" about.
The following table provides information about the project.
THE UNIVERSITY OF MANCHESTER
|Coordinator Country||United Kingdom [UK]|
|Total cost||1˙492˙424 €|
|EC max contribution||1˙492˙424 € (100%)|
1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
|Duration (year-month-day)||from 2018-01-01 to 2022-12-31|
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|1||THE UNIVERSITY OF MANCHESTER||UK (MANCHESTER)||coordinator||1˙492˙424.00|
The availability of a versatile catalytic platform to precisely target and functionalize individual C-H bonds in complex organic molecules would revolutionize our synthetic strategies, leading to streamlined routes to high value chemicals and supporting the development of a ‘greener’ chemical industry. Although an impressive range of C-H functionalizations can be achieved with small transition metal complexes, site selectivity is often determined by features of the substrate, and not by the catalyst. A general approach to achieve the more aspirational ‘catalyst controlled’ transformations requires molecular recognition elements within the catalyst which: a) allow precise substrate orientation and b) can be tuned to alter selectivity. In principle, these requirements could be perfectly addressed by protein catalysts which can be readily adapted via laboratory evolution. However, enzyme engineering strategies are currently limited to Nature’s twenty amino acid alphabet, severely limiting the range of metal co-ordination environments, and thus catalytic activities, that are accessible within proteins. In enzC-Hem, I will exploit advanced protein engineering technology available in my laboratory to install ‘chemically programmed’ ligands and/or noble metal co-factors into selected enzyme scaffolds. I will show that the resulting C-H activation catalysts can be systematically optimized via directed evolution with an expanded genetic code using modern ultra-high throughput methods (>100 variants per second), yielding biocatalysts with augmented selectivity/activity profiles. Thus my approach merges the broad range of C-H functionalizations accessible with small molecule catalysts with precise control of selectivity provided by proteins. The biocatalysts developed will address major global challenges in biotechnology and synthetic chemistry, from enhancing lignocellulose derived biofuel production to revealing novel bioactive molecules via late-stage functionalizations.
|year||authors and title||journal||last update|
Moritz Pott, Takahiro Hayashi, Takahiro Mori, Peer R. E. Mittl, Anthony P. Green, Donald Hilvert
A Noncanonical Proximal Heme Ligand Affords an Efficient Peroxidase in a Globin Fold
published pages: 1535-1543, ISSN: 0002-7863, DOI: 10.1021/jacs.7b12621
|Journal of the American Chemical Society 140/4||2019-08-29|
Takahiro Hayashi, Donald Hilvert, Anthony P. Green
Engineered Metalloenzymes with Nonâ€Canonical Coordination Environments
published pages: 11821-11830, ISSN: 0947-6539, DOI: 10.1002/chem.201800975
|Chemistry â€“ A European Journal 24/46||2019-08-29|
Ashleigh J. Burke, Sarah L. Lovelock, Amina Frese, Rebecca Crawshaw, Mary Ortmayer, Mark Dunstan, Colin Levy, Anthony P. Green
Design and evolution of an enzyme with a non-canonical organocatalytic mechanism
published pages: 219-223, ISSN: 0028-0836, DOI: 10.1038/s41586-019-1262-8
Jin Xu, Anthony P. Green, Nicholas J. Turner
Chemo-Enzymatic Synthesis of Pyrazines and Pyrroles
published pages: 16760-16763, ISSN: 1433-7851, DOI: 10.1002/anie.201810555
|Angewandte Chemie International Edition 57/51||2019-08-29|
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