Artificial metalloenzymes derived from bovine β-lactoglobulin for the asymmetric transfer hydrogenation of an aryl ketone – synthesis, characterization and catalytic activity

2014 ◽  
Vol 43 (14) ◽  
pp. 5482-5489 ◽  
Author(s):  
Alice Chevalley ◽  
Mickael V. Cherrier ◽  
Juan C. Fontecilla-Camps ◽  
Mahsa Ghasemi ◽  
Michèle Salmain
Keyword(s):  
Catalytic Activity ◽  
Fatty Acid ◽  
Transfer Hydrogenation ◽  
Asymmetric Transfer Hydrogenation ◽  
P Protein ◽  
Artificial Metalloenzymes ◽  
Diimine Complexes ◽  
Β Lactoglobulin ◽  
Aryl Ketone

Protein hybrids resulting from the supramolecular anchoring to bovine β-lactoglobulin of fatty acid-derived Rh(iii) diimine complexes catalysed the asymmetric transfer hydrogenation of trifluoroacetophenone with up to 32% ee.

scholarly journals Ruthenium(II) complexes bearing (NNN) ligand: catalytic evaluation of different solvent-mediated coordination modes

2018 ◽  
Vol 96 (1) ◽  
pp. 40-43 ◽  
Author(s):  
Sara Pellegrino ◽  
Giorgio Facchetti ◽  
Raffella Gandolfi ◽  
Marco Fusè ◽  
Emanuela Erba ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Functional Groups ◽  
Transfer Hydrogenation ◽  
Tridentate Ligand ◽  
Asymmetric Transfer Hydrogenation ◽  
Coordination Modes ◽  
Aryl Ketones

A new (NNN) tridentate ligand was prepared, and its ability to coordinate ruthenium(II) was evaluated. The presence of different functional groups on the ligand allows bi- or tri-coordinated complexes to be obtained depending on complexation conditions. The catalytic activity of both bidentate and tridentate complexes was studied in asymmetric transfer hydrogenation of different aryl ketones, showing a comparable behavior of the two complexes in terms of efficiency and stereoselectivity.

Boron containing chiral Schiff bases: Synthesis and catalytic activity in asymmetric transfer hydrogenation (ATH) of ketones

2020 ◽  
Vol 1200 ◽  
pp. 127064 ◽  
Author(s):  
Salih Paşa ◽  
Nevin Arslan ◽  
Nermin Meri̇ç ◽  
Cezmi Kayan ◽  
Murat Bingül ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Schiff Bases ◽  
Transfer Hydrogenation ◽  
Asymmetric Transfer Hydrogenation

Directed Evolution of P450 Fatty Acid Decarboxylases via High-Throughput Screening Towards Improved Catalytic Activity

2019 ◽  
Author(s):  
Huifang Xu ◽  
Weinan Liang ◽  
Linlin Ning ◽  
Yuanyuan Jiang ◽  
Wenxia Yang ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Fatty Acid ◽  
Directed Evolution ◽  
High Throughput ◽  
High Throughput Screening ◽  
Colorimetric Detection ◽  
Screening Method ◽  
Random Mutagenesis ◽  
Direct Production ◽  
Consumption Activity

P450 fatty acid decarboxylases (FADCs) have recently been attracting considerable attention owing to their one-step direct production of industrially important 1-alkenes from biologically abundant feedstock free fatty acids under mild conditions. However, attempts to improve the catalytic activity of FADCs have met with little success. Protein engineering has been limited to selected residues and small mutant libraries due to lack of an effective high-throughput screening (HTS) method. Here, we devise a catalase-deficient <i>Escherichia coli</i> host strain and report an HTS approach based on colorimetric detection of H<sub>2</sub>O<sub>2</sub>-consumption activity of FADCs. Directed evolution enabled by this method has led to effective identification for the first time of improved FADC variants for medium-chain 1-alkene production from both DNA shuffling and random mutagenesis libraries. Advantageously, this screening method can be extended to other enzymes that stoichiometrically utilize H<sub>2</sub>O<sub>2</sub> as co-substrate.

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