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Volumn 52, Issue 35, 2013, Pages 9323-9326

Highly enantioselective reduction of α-methylated nitroalkenes

Author keywords

asymmetric catalysis; biocatalysis; nitroalkanes; nitroalkenes; reduction

Indexed keywords

ASYMMETRIC CATALYSIS; BIOCATALYSIS; ENANTIOMERIC EXCESS; ENANTIOSELECTIVE REDUCTION; GLUCONOBACTER OXYDANS; NITROALKANES; NITROALKENES; OPTIMIZED REACTION CONDITIONS;

EID: 84882990717     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201301814     Document Type: Article
Times cited : (33)

References (28)
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    • Y. Li, T. Izumi, J. Chin. Chem. Soc. 2002, 49, 505-508 (ee values: 0-10 %ee)
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  • 9
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    • (Eds.: K. Drauz, H. Gröger, O. May), 3 nd ed., Wiley-VCH, Weinheim, chap. 27
    • D. J. Bougioukou, J. D. Stewart, in Enzyme Catalysis in Organic Synthesis, Vol.2 (Eds.:, K. Drauz, H. Gröger, O. May,), 3 nd ed., Wiley-VCH, Weinheim, 2012, chap. 27, p. 1111-1163.
    • (2012) Enzyme Catalysis in Organic Synthesis , vol.2 , pp. 1111-1163
    • Bougioukou, D.J.1    Stewart, J.D.2
  • 18
    • 84883046534 scopus 로고    scopus 로고
    • unpublished results
    • [6c,d] This agrees with our observation of a low tendency of racemization under our reaction conditions: T. Reß, C. Giese, H. Gröger, unpublished results.
    • Reß, T.1
  • 19
    • 84879462871 scopus 로고    scopus 로고
    • The difficulty of the controlled formation of such stereogenic centers and the particular challenge of the enantioselective reduction of α-substituted nitroalkenes 5 are illustrated by the fact that in contrast to α-substituted nitroalkenes 5 the analogous reductions of β,β-disubstituted nitroalkenes proceed highly enantioselectively with numerous catalysts, comprising enzymes (see references[5, 6]) as well as chemocatalysts, see, e.g.:, S. Li, K. Huang, B. Cao, J. Zhang, W. Wu, X. Zhang, Angew. Chem. 2012, 124, 8701-8704
    • (2012) Angew. Chem. , vol.124 , pp. 8701-8704
    • Li, S.1    Huang, K.2    Cao, B.3    Zhang, J.4    Wu, W.5    Zhang, X.6
  • 20
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    • references therein
    • Angew. Chem. Int. Ed. 2012, 51, 8573-8576, and references therein.
    • (2012) Angew. Chem. Int. Ed. , vol.51 , pp. 8573-8576
  • 23
    • 84882970224 scopus 로고    scopus 로고
    • unpublished results
    • E. Burda, T. Reß, H. Gröger, unpublished results.
    • Burda, E.1
  • 25
    • 84868087352 scopus 로고    scopus 로고
    • With regard to a rational explanation for the high enantioselectivity of the ene reductase from G.oxydans, homology modeling was carried out. This showed that a catalytically active tyrosine (Y177) is responsible for the protonation of the α-C atom of the substrate, which is in accordance with most members of the "Old Yellow Enzyme" family. A particular structural basis for the observed high enantioselectivity of the reduction of nitroalkenes 5 with the ene reductase from G.oxydans could not be deduced yet from the homology modeling; at the same time this aspect is a subject of current studies. The structure of the ene reductase NCR from Zymomonas mobilis (PDB entry: 4a3u) served as a template for the structure modeling of the ene reductase from G.oxydans due to the high sequence homology of the two enzymes (70 %). The ene reductase from Z.mobilis is described in:, S. Reich, H. W. Hoeffken, B. Rosche, B. M. Nestl, B. Hauer, ChemBioChem 2012, 13, 2400-2407.
    • (2012) ChemBioChem , vol.13 , pp. 2400-2407
    • Reich, S.1    Hoeffken, H.W.2    Rosche, B.3    Nestl, B.M.4    Hauer, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.