• Aucun résultat trouvé

Designed evolution of artificial metalloenzymes: protein catalysts made to order

N/A
N/A
Protected

Academic year: 2022

Partager "Designed evolution of artificial metalloenzymes: protein catalysts made to order"

Copied!
10
0
0

Texte intégral

(1)

Published in Organic & Biomolecular Chemistry 5, issue 12, 1835-1844, 2007

which should be used for any reference to this work 1

(2)

2

(3)

3

(4)

4

(5)

5

(6)

6

(7)

7

(8)

8

(9)

9

(10)

10

Références

Documents relatifs

Le test non paramétrique de Wilcoxon a ensuite été utilisé pour comparer les résultats liés aux quatre dimensions et au score global de l’Inventaire de l’équilibre de

When co-variation analysis aims to gain evolutionary information, OMES and ELSC are well suited to identify the co-evolving residues that contributed to the divergence within

Abstract: The Mn(TpCPP)-Xln10A artificial metalloenzyme, obtained by non-covalent insertion of Mn(III)-meso-tetrakis(p-carboxyphenyl)porphyrin [Mn(TpCPP), 1-Mn] into xylanase 10A

The ability to optimize or to find new catalysts for enantioselective transformations has a major impact in today’s chemistry. Artificial metalloenzymes lie at

Lu and co-workers recently reported an enantiose- lective artificial sulfoxidation metalloenzyme based on a dual covalent anchoring strategy of a Mn(Schiff base) within Mb (Table

Having demonstrated that the introduction of a short achiral amino acid spacer between the biotin anchor and the rhodium- diphosphine moiety has, in some cases, a positive influence

Based on the incorporation of biotinylated organometallic catalyst precursors within (strept)avidin, we have developed artificial metalloenzymes for the oxidation of secondary

Indeed, similarly to what was inferred from the high- potential data of Av, the inactivation rate is independent of potential over the whole potential range (including the conditions