메뉴 건너뛰기




Volumn 82, Issue 12, 2007, Pages 1067-1071

Stereoselective hybrid catalysts: New opportunities

Author keywords

Artificial enzymes; Asymmetric synthesis; Biocatalysis; Hybrid catalysts; Organometallic catalysis

Indexed keywords

BIOCATALYSTS; BIOMOLECULES; BIOPOLYMERS; CATALYSIS; CHIRALITY; LIGANDS; ORGANOMETALLICS; SUPRAMOLECULAR CHEMISTRY;

EID: 36348960764     PISSN: 02682575     EISSN: 10974660     Source Type: Journal    
DOI: 10.1002/jctb.1752     Document Type: Article
Times cited : (14)

References (34)
  • 2
    • 14944349481 scopus 로고    scopus 로고
    • Drauz K and Waldmann H eds, Wiley-VCH, Weinheim
    • Drauz K and Waldmann H (eds), Enzyme Catalysis in Organic Synthesis. Wiley-VCH, Weinheim (2002).
    • (2002) Enzyme Catalysis in Organic Synthesis
  • 3
    • 36349033298 scopus 로고    scopus 로고
    • Christmann M and Bräse S eds, Wiley-VCH, Weinheim
    • Christmann M and Bräse S (eds), Asymmetric Synthesis - The Essentials. Wiley-VCH, Weinheim (2007).
    • (2007) Asymmetric Synthesis - The Essentials
  • 4
    • 6044269452 scopus 로고    scopus 로고
    • In the golden age of organocatalysis
    • Dalko PI and Moisan L, In the golden age of organocatalysis. Angew Chem Int Ed 43:5138-5175 (2004).
    • (2004) Angew Chem Int Ed , vol.43 , pp. 5138-5175
    • Dalko, P.I.1    Moisan, L.2
  • 8
    • 36348964006 scopus 로고    scopus 로고
    • Wentworth P Jr and Janda KD, Catalytic antibodies, in Comprehensive Asymmetric Catalysis, ed. by Jacobsen EN, Pfalz A and Yamamoto H. Springer-Verlag, Berlin, pp. 1403-1423 (1999).
    • Wentworth P Jr and Janda KD, Catalytic antibodies, in Comprehensive Asymmetric Catalysis, ed. by Jacobsen EN, Pfalz A and Yamamoto H. Springer-Verlag, Berlin, pp. 1403-1423 (1999).
  • 9
    • 0345646451 scopus 로고    scopus 로고
    • Catalysis of organic reactions by RNA
    • Frauendorf C and Jaschke A, Catalysis of organic reactions by RNA. Angew Chem Int Ed 37:1378-1381 (1998).
    • (1998) Angew Chem Int Ed , vol.37 , pp. 1378-1381
    • Frauendorf, C.1    Jaschke, A.2
  • 10
  • 11
    • 0000147467 scopus 로고
    • Conversion of a protein to a homogeneous asymmetric hydrogenation catalyst by site-specific modification with a diphosphinerhodium (I) moiety
    • Wilson ME and Whitesides GM, Conversion of a protein to a homogeneous asymmetric hydrogenation catalyst by site-specific modification with a diphosphinerhodium (I) moiety. J Am Chem Soc 100:306-307 (1978).
    • (1978) J Am Chem Soc , vol.100 , pp. 306-307
    • Wilson, M.E.1    Whitesides, G.M.2
  • 12
    • 33845461179 scopus 로고    scopus 로고
    • Artificial metalloenzymes for enantioselective catalysis: Recent advances
    • Letondor C and Ward TR, Artificial metalloenzymes for enantioselective catalysis: recent advances. ChemBioChem 7:1845-1852 (2006).
    • (2006) ChemBioChem , vol.7 , pp. 1845-1852
    • Letondor, C.1    Ward, T.R.2
  • 13
    • 33748634910 scopus 로고    scopus 로고
    • Biosynthetic inorganic chemistry
    • Lu Y, Biosynthetic inorganic chemistry. Angew Chem Int Ed 45:5588-5601 (2006).
    • (2006) Angew Chem Int Ed , vol.45 , pp. 5588-5601
    • Lu, Y.1
  • 14
    • 17444428945 scopus 로고    scopus 로고
    • Artificial metalloenzymes: Proteins as hosts for enantioselective catalysis
    • Thomas CM and Ward TR, Artificial metalloenzymes: proteins as hosts for enantioselective catalysis. Chem Soc Rev 34:337-346 (2005).
    • (2005) Chem Soc Rev , vol.34 , pp. 337-346
    • Thomas, C.M.1    Ward, T.R.2
  • 15
    • 0041430569 scopus 로고    scopus 로고
    • Chemical modification of biocatalysts
    • Davis BG, Chemical modification of biocatalysts. Curr Opin Biotechnol 14:379-386 (2003).
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 379-386
    • Davis, B.G.1
  • 16
    • 2142729360 scopus 로고    scopus 로고
    • Vanadium-catalysed enantioselective sulfoxidations: Rational design of biocatalytic and biomimetic systems
    • Van de Velde F, Arends IWCE and Sheldon RA, Vanadium-catalysed enantioselective sulfoxidations: rational design of biocatalytic and biomimetic systems. Topics Catal 13:259-265 (2000).
    • (2000) Topics Catal , vol.13 , pp. 259-265
    • Van de Velde, F.1    Arends, I.W.C.E.2    Sheldon, R.A.3
  • 17
    • 32944480336 scopus 로고    scopus 로고
    • Manganese-substituted carbonic anhydrase as a new peroxidase
    • Okrasa K and Kazlauskas RJ, Manganese-substituted carbonic anhydrase as a new peroxidase. Chem Eur J 12:1587-1596 (2006).
    • (2006) Chem Eur J , vol.12 , pp. 1587-1596
    • Okrasa, K.1    Kazlauskas, R.J.2
  • 18
    • 0001247133 scopus 로고
    • A new enzyme containing a synthetically formed active site
    • Polgar L and Bender ML, A new enzyme containing a synthetically formed active site. J Am Chem Soc 88:3153-3154 (1966).
    • (1966) J Am Chem Soc , vol.88 , pp. 3153-3154
    • Polgar, L.1    Bender, M.L.2
  • 20
    • 0031439169 scopus 로고    scopus 로고
    • A semisynthetic metalloenzyme based on a protein cavity that catalyzes the enantioselective hydrolysis of ester and amide substrates
    • Davis RR and DiStefano MD, A semisynthetic metalloenzyme based on a protein cavity that catalyzes the enantioselective hydrolysis of ester and amide substrates. J Am Chem Soc 119:11643-11652 (1997).
    • (1997) J Am Chem Soc , vol.119 , pp. 11643-11652
    • Davis, R.R.1    DiStefano, M.D.2
  • 22
    • 12244309473 scopus 로고    scopus 로고
    • Preparation of artificial metalloenzymes by insertion of chromium(III) Schiff base complexes into apomyoglobin mutants
    • Ohashi M, Koshiyama T, Ueno T, Yanase M, Fujii H and Watanabe Y, Preparation of artificial metalloenzymes by insertion of chromium(III) Schiff base complexes into apomyoglobin mutants. Angew Chem Int Ed 42:1005-1008 (2003).
    • (2003) Angew Chem Int Ed , vol.42 , pp. 1005-1008
    • Ohashi, M.1    Koshiyama, T.2    Ueno, T.3    Yanase, M.4    Fujii, H.5    Watanabe, Y.6
  • 24
    • 20344389806 scopus 로고    scopus 로고
    • DNA-based asymmetric catalysis
    • Roelfes G and Feringa BL, DNA-based asymmetric catalysis. Angew Chem Int Ed 44:3230-3232 (2005).
    • (2005) Angew Chem Int Ed , vol.44 , pp. 3230-3232
    • Roelfes, G.1    Feringa, B.L.2
  • 25
    • 0034583305 scopus 로고    scopus 로고
    • Diels - Alder reactions in water
    • Otto S and Engberts JBFN, Diels - Alder reactions in water. Pure Appl Chem 72:1365-1372 (2000).
    • (2000) Pure Appl Chem , vol.72 , pp. 1365-1372
    • Otto, S.1    Engberts, J.B.F.N.2
  • 27
    • 33745664610 scopus 로고    scopus 로고
    • Copper-phthalocyanine conjugates of serum albumins as enantioselective catalysts in Diels-Alder reactions
    • Reetz MT and Jiao N, Copper-phthalocyanine conjugates of serum albumins as enantioselective catalysts in Diels-Alder reactions. Angew Chem Int Ed 45:2416-2419 (2006).
    • (2006) Angew Chem Int Ed , vol.45 , pp. 2416-2419
    • Reetz, M.T.1    Jiao, N.2
  • 28
    • 14844297328 scopus 로고    scopus 로고
    • Albumin-conjugated corrole metal complexes: Extremely simple yet very efficient biomimetic oxidation systems
    • Mahammed A and Gross Z, Albumin-conjugated corrole metal complexes: extremely simple yet very efficient biomimetic oxidation systems. J Am Chem Soc 127:2883-2887 (2005).
    • (2005) J Am Chem Soc , vol.127 , pp. 2883-2887
    • Mahammed, A.1    Gross, Z.2
  • 29
    • 21244459166 scopus 로고    scopus 로고
    • Artificial metalloenzymes for enantioselective catalysis based on the noncovalent incorporation of organometallic moieties in a host protein
    • Ward TR, Artificial metalloenzymes for enantioselective catalysis based on the noncovalent incorporation of organometallic moieties in a host protein. Chem Eur J 11:3798-3804 (2005).
    • (2005) Chem Eur J , vol.11 , pp. 3798-3804
    • Ward, T.R.1
  • 30
    • 0042805254 scopus 로고    scopus 로고
    • Artificial metalloenzymes for enantioselective catalysis based on biotin-avidin
    • Collot J, Gradinaru J, Humbert N, Skander M, Zocchi A and Ward TR, Artificial metalloenzymes for enantioselective catalysis based on biotin-avidin. J Am Chem Soc 125:9030-9031 (2003).
    • (2003) J Am Chem Soc , vol.125 , pp. 9030-9031
    • Collot, J.1    Gradinaru, J.2    Humbert, N.3    Skander, M.4    Zocchi, A.5    Ward, T.R.6
  • 31
    • 7744235359 scopus 로고    scopus 로고
    • Artificial metalloenzymes: (strept)avidin as host for enantioselective hydrogenation by achiral biotinylated rhodium-diphosphine complexes
    • Skander M, Humbert N, Collot J, Gradinaru J, Klein G, Loosli A, et al, Artificial metalloenzymes: (strept)avidin as host for enantioselective hydrogenation by achiral biotinylated rhodium-diphosphine complexes. J Am Chem Soc 126:14411-14418 (2004).
    • (2004) J Am Chem Soc , vol.126 , pp. 14411-14418
    • Skander, M.1    Humbert, N.2    Collot, J.3    Gradinaru, J.4    Klein, G.5    Loosli, A.6
  • 32
    • 28744432508 scopus 로고    scopus 로고
    • Tailoring the active site of chemzymes by using a chemogenetic-optimization procedure: Towards substrate-specific artificial hydrogenases based on the biotin-avidin technology
    • Klein G, Humbert N, Gradinaru J, Ivanova A, Gilardoni F, Rusbandi UE, et al, Tailoring the active site of chemzymes by using a chemogenetic-optimization procedure: towards substrate-specific artificial hydrogenases based on the biotin-avidin technology. Angew Chem Int Ed 44:7764-7767 (2005).
    • (2005) Angew Chem Int Ed , vol.44 , pp. 7764-7767
    • Klein, G.1    Humbert, N.2    Gradinaru, J.3    Ivanova, A.4    Gilardoni, F.5    Rusbandi, U.E.6
  • 33
    • 33750070283 scopus 로고    scopus 로고
    • Directed evolution of hybrid enzymes: Evolving enantioselectivity of an achiral Rh-complex anchored to a protein
    • Reetz MT, Peyralans JJP, Maichele A, Fu Y and Maywald M, Directed evolution of hybrid enzymes: evolving enantioselectivity of an achiral Rh-complex anchored to a protein. Chem Commun 4318-4320 (2006).
    • (2006) Chem Commun , vol.4318-4320
    • Reetz, M.T.1    Peyralans, J.J.P.2    Maichele, A.3    Fu, Y.4    Maywald, M.5
  • 34
    • 33745656141 scopus 로고    scopus 로고
    • Artificial transfer hydrogenases based on the biotin- (strept)avidin technology: Fine tuning the selectivity by saturation mutagenesis of the host protein
    • Letondor D, Pordea A, Humbert N, Ivanova A, Mazurek S, Novic M, et al, Artificial transfer hydrogenases based on the biotin- (strept)avidin technology: fine tuning the selectivity by saturation mutagenesis of the host protein. J Am Chem Soc 128:8320-8328 (2006).
    • (2006) J Am Chem Soc , vol.128 , pp. 8320-8328
    • Letondor, D.1    Pordea, A.2    Humbert, N.3    Ivanova, A.4    Mazurek, S.5    Novic, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.