Author
G. I. Niklshin
Bio: G. I. Niklshin is an academic researcher from Russian Academy of Sciences. The author has contributed to research in topics: Tautomer & Steric effects. The author has an hindex of 1, co-authored 1 publications receiving 1 citations.
Topics: Tautomer, Steric effects, Hemiacetal, Free-radical addition
Papers
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TL;DR: According to the data of the IR spectra, the 4-hydroxy ketones exist in both the open and cyclic (hemiacetal) forms as discussed by the authors, the amount of the open form increases with increase in the steric hindrance in the cyclization step.
Abstract: 1.
Some 4- and 5-hydroxyketones were synthesized by the free-radical addition of alcohols toα,β-unsaturated ketones.
2.
According to the data of the IR spectra, the 4-hydroxyketones exist in both the open and cyclic (hemiacetal) forms. The amount of the open form increases with increase in the steric hindrance in the cyclization step. The 5-hydroxyketones exist only in the open form.
1 citations
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TL;DR: This study compares the whole-cell biocatalytic route with the enzymatic route to enantiopure (S)-2 and investigates factors determining performance and outcome of the bioreductions.
Abstract: Biocatalytical approaches have been investigated in order to improve accessibility of the bifunctional chiral building block (5S)-hydroxy-2-hexanone ((S)-2). As a result, a new synthetic route starting from 2,5-hexanedione (1) was developed for (S)-2, which is produced with high enantioselectivity (ee >99%). Since (S)-2 can be reduced further to furnish (2S,5S)-hexanediol ((2S,5S)-3), chemoselectivity is a major issue. Among the tested biocatalysts the whole-cell system S. cerevisiae L13 surpasses the bacterial dehydrogenase ADH-T in terms of chemoselectivity. The use of whole-cells of S. cerevisiae L13 affords (S)-2 from prochiral 1 with 85% yield, which is 21% more than the value obtained with ADH-T. This is due to the different reaction rates of monoreduction (1→2) and consecutive reduction (2→3) of the respective biocatalysts. In order to optimise the performance of the whole-cell-bioreduction 1→2 with S. cerevisiae, the system was studied in detail, revealing interactions between cell-physiology and xenobiotic substrate and by-products, respectively. This study compares the whole-cell biocatalytic route with the enzymatic route to enantiopure (S)-2 and investigates factors determining performance and outcome of the bioreductions.
23 citations