161219-33-6Relevant articles and documents
Trichosporon cutaneum-promoted deracemization of (±)-2-hydroxindan-1-one: a mechanistic study
Cazetta, Tarcila,Lunardi, Ines,Conceicao, Gelson J.A.,Moran, Paulo J.S.,Rodrigues, J. Augusto R.
, p. 2030 - 2036 (2008/02/11)
A mechanistic study of the deracemization of (±)-2-hydroxy-1-indanone mediated by the yeast Trichosporon cutaneum to afford pure (1S,2R)-1,2-indandiol is reported. The key aspect of the study was the use of pure (R)- and (S)-2-hydroxy-1-indanone enantiomers to ensure reliable conclusions. Experiments in the absence of yeast cells or using dead cells disclosed that the pure enantiomers were not racemized, which suggest that the whole dynamic kinetic resolution process is enzymatic in character. When living yeast cells were used the (R)-substrate was smoothly converted to (1S,2R)-1,2-indandiol, whilst the (S)-2-hydroxy-1-indanone was converted to the same diol through a more complex fashion, which requires a more lengthy oxidation-reduction pathway having the 1,2-indanedione as an achiral intermediate. An unexpected observation was that 1,2-indanone acts as a moderate inhibitor of the reductive enzymes acting in the conversion of (R)-2-hydroxy-1-indanone to (1S,2R)-1,2-indandiol.
Stereoselective benzylic hydroxylation of 2-substituted indanes using toluene dioxygenase as biocatalyst
Bowers, Nigel I.,Boyd, Derek R.,Sharma, Narain D.,Goodrich, Peter A.,Groocock, Melanie R.,Blacker, A. John,Goode, Paul,Dalton, Howard
, p. 1453 - 1461 (2007/10/03)
Indane, 1A, and a series of 2-substituted indane substrates, 1B-1D, 1G, 1I-1L, were found to undergo benzylic monohydroxylation catalysed by toluene dioxygenase, present in the intact cells of Pseudomonas putida UV 4, to yield enantiopure cis-indan-1-ols, 2A-2D, 2G, 2I-2L of the same absolute configuration at C-1 as major bioproducts. Enantiopure trans-indan-1-ols 6B, 6C, and 6G were also obtained as minor metabolites. Evidence of further sequential benzylic hydroxylation (bis-hydroxylation) was found only with substrates 2A, 1C, 1D and 1L to yield the corresponding enantiopure trans-1,3-diols, 3A, 3C, 3D and 3L. Minor enzyme-catalysed processes also observed include benzylic alcohol oxidation to ketones (4A, 5A, 4B, 4L, 5L), ketone reduction to benzylic alcohol 6A, ester hydrolysis to indan-2-ol 1B, and cis-dihydroxylation of indan-1-ol 6A to triol 7. The enantiopurities and absolute configurations of bioproducts have been determined using MTPA ester formation, circular dichroism spectroscopy and stereochemical correlation methods. The contribution of asymmetric oxidation and kinetic resolution to the production of bioproducts of high ee (>98%), and the metabolic sequence involved in their biotransformation by P. putida UV4 is discussed. Enantiocomplementarity was found during the benzylic hydroxylation of indan-2-ol 1B, using toluene dioxygenase and naphthalene dioxygenase, when both single enantiomers of the metabolites 2B, 4B and 6B of opposite configurations were obtained.
A practical synthesis of (1S, 2R)-1-amino-2-indanol, a key component of HIV protease inhibitor, indinavir
Kajiro, Hiroshi,Mitamura, Shu-Ichi,Mori, Atsunori,Hiyama, Tamejiro
, p. 51 - 52 (2007/10/03)
The synthesis of (1S,2R)-1-amino-2-indanol, a key component of HIV protease inhibitor, is accomplished in eight steps from D-phenylalanine. The starting material is converted into 2-acetoxy-1-indanone in four steps involving intramolecular Friedel-Crafts cyclization. The stereochemically labile α-acetoxy ketone is hydrolyzed to 2-hydroxy-1-indanone using a catalytic amount of scandium triflate without any loss of the optical purity. Diastereoselective hydrogenation of α-hydroxy oxime, derived from the α-hydroxy ketone, gives the amino alcohol in 96% cis-selectivity. Optical purity of the starting material is perfectly retained throughout the transformations.
