186312-96-9Relevant articles and documents
Benzylic hydroxylation of aromatic compounds by P450 BM3
Neufeld, Katharina,Marienhagen, Jan,Schwaneberg, Ulrich,Pietruszka, Joerg
, p. 2408 - 2421 (2013/09/12)
Cytochrome P450 BM3 monooxygenase from Bacillus megaterium and its variants are promising catalysts for organic synthesis. Aiming at the identification of variants for selective hydroxylation of functionalised aromatic compounds, the double mutant F87A L188C showed remarkably improved catalytic activity towards a set of tested toluene derivatives. The apparent catalytic efficiency of this variant towards the model substrate methyl 2-methoxy-3-methylbenzoate was 63.6 s-1 M-1, which is 535-fold higher compared to that of wild-type BM3. Furthermore, the double mutant selectively catalysed the benzylic hydroxylation of numerous toluene derivatives, especially in the presence of carbonyl- or carboxyl-functions that are directly attached to the aromatic ring. Preparative scale conversion resulted in efficient production of methyl 3-(hydroxymethyl)-2-methoxybenzoate (73% yield) which proved that F87A L188C is a suitable, efficient and sustainable catalyst for the introduction of benzylic hydroxyl groups in general.
The synthesis and evaluation of benzofuranones as β-lactamase substrates
Adediran,Cabaret,Drouillat,Pratt,Wakselman
, p. 1175 - 1183 (2007/10/03)
6- and 7-Carboxy-3-phenylacetamido-3H-1-benzofuran-2-one have been synthesized as potential β-lactamase substrates and/or inhibitors. These compounds were prepared by lactonization of the corresponding, appropriately substituted phenylglycines. The latter compounds were prepared by either the Strecker or the Buecherer-Berg method. The benzofuran-2-ones were less stable in aqueous solution than the analogous acyclic phenaceturate esters but comparably stable to analogous benzopyran-2-ones. They differed from the latter compounds however in that the C-3 hydrogen of the furan-2-ones, adjacent to the lactone carbonyl group, was distinctly acidic; 7-carboxy-3-phenylacetamido-3H-1-benzofuran-2-one exists largely as an enolate at pH 7.5. The furan-2-ones were β-lactamase substrates with reactivity very similar to the analogous acyclic phenaceturates. They were not, however, DD-peptidase inhibitors and are thus unlikely to have antibiotic activity. The structural basis for these observations is discussed.
