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TAML-ArM SIGNED

Development of an artificial alkane monooxygenase: A leap in bioinspired oxidation catalysis

Total Cost €

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EC-Contrib. €

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Partnership

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Project "TAML-ArM" data sheet

The following table provides information about the project.

Coordinator
UNIVERSITAT BASEL 

Organization address
address: PETERSPLATZ 1
city: BASEL
postcode: 4051
website: www.unibas.ch

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Switzerland [CH]
 Project website https://www.chemie.unibas.ch/
 Total cost 175˙419 €
 EC max contribution 175˙419 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2016
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2017
 Duration (year-month-day) from 2017-04-01   to  2019-03-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    UNIVERSITAT BASEL CH (BASEL) coordinator 175˙419.00

Map

 Project objective

The oxygenation of inert C-H bonds is a highly challenging reaction that has an enormous untapped potential for the European chemical industry. Indeed, it offers attractive means to upgrade cheap hydrocarbons into high value-added products. Nature relies on iron-based enzymes and oxygen to perform such transformations. In a biomimetic spirit, catalytic alkane hydroxylation is best achieved using iron-based catalysts and H2O2 as oxidant. Compared to natural enzymes, however, such systems display modest performance. In the TAML-ArM project, we aim to the development of a novel approach that consists of creating an artificial alkane monooxygenase by introducing a highly active iron complex within a protein scaffold. This strategy, pioneered in the Ward group, has ample precedent for less challenging reactions, and it potentially represents a significant step forward in bioinspired hydroxylation chemistry. To achieve this goal artificial metalloenzymes merge homogeneous- and enzymatic catalysis, two traditionally complementary strategies. We envision that this approach will: i) improve the catalytic activity by protecting the highly reactive Fe=O-moiety by shielding it from undesirable side-reactions and ii) provide novel selectivities, owing to second coordination sphere interactions between the protein and the substrate. Thanks to this innovative catalytic approach, we will develop a paradigm shifting technology for the selective hydroxylation of hydrocarbons: the reactions will be performed in water at room temperature using benign H2O2 as oxidant.

 Publications

year authors and title journal last update
List of publications.
2019 Alexandria Deliz Liang, Joan Serrano-Plana, Ryan L. Peterson, Thomas R. Ward
Artificial Metalloenzymes Based on the Biotin–Streptavidin Technology: Enzymatic Cascades and Directed Evolution
published pages: 585-595, ISSN: 0001-4842, DOI: 10.1021/acs.accounts.8b00618
Accounts of Chemical Research 52/3 2019-06-06

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