메뉴 건너뛰기




Volumn 19, Issue 1, 2014, Pages 135-143

Artificial metalloenzymes for enantioselective catalysis

Author keywords

[No Author keywords available]

Indexed keywords

ALKENE; ANILINE DERIVATIVE; ARTIFICIAL METALLOENZYME; BOVINE SERUM ALBUMIN; CARBONATE DEHYDRATASE II; ENZYME; GRAMICIDIN S; IRIDIUM; METAL COMPLEX; NICKEL; RHODIUM COMPLEX; STILBENE OXIDE; STREPTAVIDIN; TETRAPEPTIDE; TRANSITION ELEMENT; UNCLASSIFIED DRUG; DNA; METALLOPROTEIN; PEPTIDE;

EID: 84895772201     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2014.02.002     Document Type: Review
Times cited : (122)

References (49)
  • 1
    • 0000147467 scopus 로고
    • Conversion of a protein to a homogeneous asymmetric hydrogenation catalyst by site-specific modification with a diphosphinerhodium(I) moiety
    • Wilson M.E., Whitesides G.M. Conversion of a protein to a homogeneous asymmetric hydrogenation catalyst by site-specific modification with a diphosphinerhodium(I) moiety. J Am Chem Soc 1978, 100:306-307.
    • (1978) J Am Chem Soc , vol.100 , pp. 306-307
    • Wilson, M.E.1    Whitesides, G.M.2
  • 2
    • 84890369423 scopus 로고    scopus 로고
    • Artificial metalloenzymes and metallopeptide catalysts for organic synthesis
    • Lewis J.C. Artificial metalloenzymes and metallopeptide catalysts for organic synthesis. ACS Catal 2013, 3:2954-2975.
    • (2013) ACS Catal , vol.3 , pp. 2954-2975
    • Lewis, J.C.1
  • 3
    • 84881152519 scopus 로고    scopus 로고
    • Artificial metalloenzymes constructed from hierarchically-assembled proteins
    • Ueno T., Tabe H., Tanaka Y. Artificial metalloenzymes constructed from hierarchically-assembled proteins. Chem Asian J 2013, 8:1646-1660.
    • (2013) Chem Asian J , vol.8 , pp. 1646-1660
    • Ueno, T.1    Tabe, H.2    Tanaka, Y.3
  • 4
    • 78751548138 scopus 로고    scopus 로고
    • Artificial metalloenzymes based on the biotin-avidin technology: enantioselective catalysis and beyond
    • Ward T.R. Artificial metalloenzymes based on the biotin-avidin technology: enantioselective catalysis and beyond. Acc Chem Res 2011, 44:47-57.
    • (2011) Acc Chem Res , vol.44 , pp. 47-57
    • Ward, T.R.1
  • 5
    • 78349311766 scopus 로고    scopus 로고
    • Artificial metalloenzymes
    • Rosati F., Roelfes G. Artificial metalloenzymes. ChemCatChem 2010, 2:916-927.
    • (2010) ChemCatChem , vol.2 , pp. 916-927
    • Rosati, F.1    Roelfes, G.2
  • 6
    • 84864246819 scopus 로고    scopus 로고
    • Enantioselective artificial metalloenzymes by creation of a novel active site at the protein dimer interface
    • Bos J., Fusetti F., Driessen A.J.M., Roelfes G. Enantioselective artificial metalloenzymes by creation of a novel active site at the protein dimer interface. Angew Chem Int Ed 2012, 51:7472-7475.
    • (2012) Angew Chem Int Ed , vol.51 , pp. 7472-7475
    • Bos, J.1    Fusetti, F.2    Driessen, A.J.M.3    Roelfes, G.4
  • 7
    • 84886848009 scopus 로고    scopus 로고
    • An enantioselective artificial metallo-hydratase
    • Bos J., García-Herraiz A., Roelfes G. An enantioselective artificial metallo-hydratase. Chem Sci 2013, 4:3578-3582.
    • (2013) Chem Sci , vol.4 , pp. 3578-3582
    • Bos, J.1    García-Herraiz, A.2    Roelfes, G.3
  • 9
    • 84872028143 scopus 로고    scopus 로고
    • Semi-synthesis of an artificial scandium(III) enzyme with a beta-helical bio-nanotube
    • Inaba H., Kanamaru S., Arisaka F., Kitagawa S., Ueno T. Semi-synthesis of an artificial scandium(III) enzyme with a beta-helical bio-nanotube. Dalton Trans 2012, 41:11424-11427.
    • (2012) Dalton Trans , vol.41 , pp. 11424-11427
    • Inaba, H.1    Kanamaru, S.2    Arisaka, F.3    Kitagawa, S.4    Ueno, T.5
  • 10
    • 84856397386 scopus 로고    scopus 로고
    • Hydrolytic catalysis and structural stabilization in a designed metalloprotein
    • Zastrow M.L., Peacock A.F.A., Stuckey J.A., Pecoraro V.L. Hydrolytic catalysis and structural stabilization in a designed metalloprotein. Nat Chem 2012, 4:118-123.
    • (2012) Nat Chem , vol.4 , pp. 118-123
    • Zastrow, M.L.1    Peacock, A.F.A.2    Stuckey, J.A.3    Pecoraro, V.L.4
  • 11
    • 84874039900 scopus 로고    scopus 로고
    • Designing enzyme-like catalysts: a rhodium(II) metallopeptide case study
    • Ball Z.T. Designing enzyme-like catalysts: a rhodium(II) metallopeptide case study. Acc Chem Res 2013, 46:560-570.
    • (2013) Acc Chem Res , vol.46 , pp. 560-570
    • Ball, Z.T.1
  • 12
    • 77955784263 scopus 로고    scopus 로고
    • Metallopeptides for asymmetric dirhodium catalysis
    • Sambasivan R., Ball Z.T. Metallopeptides for asymmetric dirhodium catalysis. J Am Chem Soc 2010, 132:9289-9291.
    • (2010) J Am Chem Soc , vol.132 , pp. 9289-9291
    • Sambasivan, R.1    Ball, Z.T.2
  • 13
    • 84865073495 scopus 로고    scopus 로고
    • Screening rhodium metallopeptide libraries "on bead": asymmetric cyclopropanation and a solution to the enantiomer problem
    • Sambasivan R., Ball Z.T. Screening rhodium metallopeptide libraries "on bead": asymmetric cyclopropanation and a solution to the enantiomer problem. Angew Chem Int Ed 2012, 51:8568-8572.
    • (2012) Angew Chem Int Ed , vol.51 , pp. 8568-8572
    • Sambasivan, R.1    Ball, Z.T.2
  • 14
    • 84882899103 scopus 로고    scopus 로고
    • Studies of asymmetric styrene cyclopropanation with a rhodium(II) metallopeptide catalyst developed with a high-throughput screen
    • Sambasivan R., Ball Z.T. Studies of asymmetric styrene cyclopropanation with a rhodium(II) metallopeptide catalyst developed with a high-throughput screen. Chirality 2013, 25:493-497.
    • (2013) Chirality , vol.25 , pp. 493-497
    • Sambasivan, R.1    Ball, Z.T.2
  • 15
    • 84878794621 scopus 로고    scopus 로고
    • A genetically encodable ligand for transfer hydrogenation
    • Mayer C., Hilvert D. A genetically encodable ligand for transfer hydrogenation. Eur J Org Chem 2013, 3427-3431.
    • (2013) Eur J Org Chem , pp. 3427-3431
    • Mayer, C.1    Hilvert, D.2
  • 16
    • 84867558115 scopus 로고    scopus 로고
    • A chelating tetrapeptide rhodium complex comprised of a histidylidene residue: biochemical tailoring of an NHC-Rh hydrosilylation catalyst
    • Monney A., Albrecht M. A chelating tetrapeptide rhodium complex comprised of a histidylidene residue: biochemical tailoring of an NHC-Rh hydrosilylation catalyst. Chem Commun 2012, 48:10960-10962.
    • (2012) Chem Commun , vol.48 , pp. 10960-10962
    • Monney, A.1    Albrecht, M.2
  • 17
    • 84877021204 scopus 로고    scopus 로고
    • Peptide-tethered monodentate and chelating histidylidene metal complexes: synthesis and application in catalytic hydrosilylation
    • Monney A., Nastri F., Albrecht M. Peptide-tethered monodentate and chelating histidylidene metal complexes: synthesis and application in catalytic hydrosilylation. Dalton Trans 2013, 42:5655-5660.
    • (2013) Dalton Trans , vol.42 , pp. 5655-5660
    • Monney, A.1    Nastri, F.2    Albrecht, M.3
  • 19
    • 20344389806 scopus 로고    scopus 로고
    • DNA-based asymmetric catalysis
    • Roelfes G., Feringa B.L. DNA-based asymmetric catalysis. Angew Chem Int Ed 2005, 44:3230-3240.
    • (2005) Angew Chem Int Ed , vol.44 , pp. 3230-3240
    • Roelfes, G.1    Feringa, B.L.2
  • 20
    • 84900462724 scopus 로고    scopus 로고
    • Enantioselective catalysis at the DNA scaffold
    • Garcia-Fernandez A., Roelfes G. Enantioselective catalysis at the DNA scaffold. Met Ions Life Sci 2012, 10:249-268.
    • (2012) Met Ions Life Sci , vol.10 , pp. 249-268
    • Garcia-Fernandez, A.1    Roelfes, G.2
  • 21
    • 84857087579 scopus 로고    scopus 로고
    • Ligand denticity controls enantiomeric preference in DNA-based asymmetric catalysis
    • Boersma A.J., de Bruin B., Feringa B.L., Roelfes G. Ligand denticity controls enantiomeric preference in DNA-based asymmetric catalysis. Chem Commun 2012, 48:2394-2400.
    • (2012) Chem Commun , vol.48 , pp. 2394-2400
    • Boersma, A.J.1    de Bruin, B.2    Feringa, B.L.3    Roelfes, G.4
  • 23
    • 84879730360 scopus 로고    scopus 로고
    • Novel catalyst design by using cisplatin to covalently anchor catalytically active copper complexes to DNA
    • Gjonaj L., Roelfes G. Novel catalyst design by using cisplatin to covalently anchor catalytically active copper complexes to DNA. ChemCatChem 2013, 5:1718-1721.
    • (2013) ChemCatChem , vol.5 , pp. 1718-1721
    • Gjonaj, L.1    Roelfes, G.2
  • 24
    • 84861588155 scopus 로고    scopus 로고
    • Enantioselective Friedel-Crafts reactions in water catalyzed by a human telomeric G-quadruplex DNA metalloenzyme
    • Wang C., Li Y., Jia G., Liu Y., Lu S., Li C. Enantioselective Friedel-Crafts reactions in water catalyzed by a human telomeric G-quadruplex DNA metalloenzyme. Chem Commun 2012, 48:6232-6234.
    • (2012) Chem Commun , vol.48 , pp. 6232-6234
    • Wang, C.1    Li, Y.2    Jia, G.3    Liu, Y.4    Lu, S.5    Li, C.6
  • 25
    • 84865848787 scopus 로고    scopus 로고
    • Enantioselective Diels-Alder reactions with G-quadruplex DNA-based catalysts
    • Wang C., Jia G., Zhou J., Li Y., Liu Y., Lu S., Li C. Enantioselective Diels-Alder reactions with G-quadruplex DNA-based catalysts. Angew Chem Int Ed 2012, 51:9352-9355.
    • (2012) Angew Chem Int Ed , vol.51 , pp. 9352-9355
    • Wang, C.1    Jia, G.2    Zhou, J.3    Li, Y.4    Liu, Y.5    Lu, S.6    Li, C.7
  • 26
    • 84884677006 scopus 로고    scopus 로고
    • The influence of G-quadruplex structure on DNA-based asymmetric catalysis using the G-quadruplex-bound cationic porphyrin TMPyP4 center dot Cu
    • Wilking M., Hennecke U. The influence of G-quadruplex structure on DNA-based asymmetric catalysis using the G-quadruplex-bound cationic porphyrin TMPyP4 center dot Cu. Org Biomol Chem 2013, 11:6940-6945.
    • (2013) Org Biomol Chem , vol.11 , pp. 6940-6945
    • Wilking, M.1    Hennecke, U.2
  • 27
    • 84866896071 scopus 로고    scopus 로고
    • Deciphering DNA-based asymmetric catalysis through intramolecular Friedel-Crafts alkylations
    • Park S., Ikehata K., Watabe R., Hidaka Y., Rajendran A., Sugiyama H. Deciphering DNA-based asymmetric catalysis through intramolecular Friedel-Crafts alkylations. Chem Commun 2012, 48:10398-10400.
    • (2012) Chem Commun , vol.48 , pp. 10398-10400
    • Park, S.1    Ikehata, K.2    Watabe, R.3    Hidaka, Y.4    Rajendran, A.5    Sugiyama, H.6
  • 28
    • 84871611914 scopus 로고    scopus 로고
    • Aqueous phase transfer hydrogenation of aryl ketones catalysed by achiral ruthenium(II) and rhodium(III) complexes and their papain conjugates
    • Madern N., Talbi B., Salmain M. Aqueous phase transfer hydrogenation of aryl ketones catalysed by achiral ruthenium(II) and rhodium(III) complexes and their papain conjugates. Appl Organometal Chem 2013, 27:6-12.
    • (2013) Appl Organometal Chem , vol.27 , pp. 6-12
    • Madern, N.1    Talbi, B.2    Salmain, M.3
  • 29
    • 79960999137 scopus 로고    scopus 로고
    • Chemically engineered papain as artificial formate dehydrogenase for NAD(P)H regeneration
    • Haquette P., Talbi B., Barilleau L., Madern N., Fosse C., Salmain M. Chemically engineered papain as artificial formate dehydrogenase for NAD(P)H regeneration. Org & Biomol Chem 2011, 9:5720-5727.
    • (2011) Org & Biomol Chem , vol.9 , pp. 5720-5727
    • Haquette, P.1    Talbi, B.2    Barilleau, L.3    Madern, N.4    Fosse, C.5    Salmain, M.6
  • 30
    • 84869996080 scopus 로고    scopus 로고
    • Enantioselective transfer hydrogenation of ketone catalysed by artificial metalloenzymes derived from bovine beta-lactoglobulin
    • Chevalley A., Salmain M. Enantioselective transfer hydrogenation of ketone catalysed by artificial metalloenzymes derived from bovine beta-lactoglobulin. Chem Commun 2012, 48:11984-11986.
    • (2012) Chem Commun , vol.48 , pp. 11984-11986
    • Chevalley, A.1    Salmain, M.2
  • 31
    • 84880165083 scopus 로고    scopus 로고
    • Structural basis for enantioselectivity in the transfer hydrogenation of a ketone catalyzed by an artificial metalloenzyme
    • Cherrier M.V., Engilberge S., Amara P., Chevalley A., Salmain M., Fontecilla-Camps J.C. Structural basis for enantioselectivity in the transfer hydrogenation of a ketone catalyzed by an artificial metalloenzyme. Eur J Inorg Chem 2013, 3596-3600.
    • (2013) Eur J Inorg Chem , pp. 3596-3600
    • Cherrier, M.V.1    Engilberge, S.2    Amara, P.3    Chevalley, A.4    Salmain, M.5    Fontecilla-Camps, J.C.6
  • 34
    • 84881269283 scopus 로고    scopus 로고
    • Genetic optimization of the catalytic efficiency of artificial imine reductases based on biotin-streptavidin technology
    • Schwizer F., Koehler V., Dürrenberger M., Knörr L., Ward T.R. Genetic optimization of the catalytic efficiency of artificial imine reductases based on biotin-streptavidin technology. ACS Catal 2013, 3:1752-1760.
    • (2013) ACS Catal , vol.3 , pp. 1752-1760
    • Schwizer, F.1    Koehler, V.2    Dürrenberger, M.3    Knörr, L.4    Ward, T.R.5
  • 35
    • 84876053295 scopus 로고    scopus 로고
    • A dual anchoring strategy for the localization and activation of artificial metalloenzymes based on the biotin-streptavidin technology
    • Zimbron J.M., Heinisch T., Schmid M., Hamels D., Nogueira E.S., Schirmer T., Ward T.R. A dual anchoring strategy for the localization and activation of artificial metalloenzymes based on the biotin-streptavidin technology. J Am Chem Soc 2013, 135:5384-5390.
    • (2013) J Am Chem Soc , vol.135 , pp. 5384-5390
    • Zimbron, J.M.1    Heinisch, T.2    Schmid, M.3    Hamels, D.4    Nogueira, E.S.5    Schirmer, T.6    Ward, T.R.7
  • 36
    • 84874208733 scopus 로고    scopus 로고
    • Fluorescence-based assay for the optimization of the activity of artificial transfer hydrogenase within a biocompatible compartment
    • Heinisch T., Langowska K., Tanner P., Reymond J., Meier W., Palivan C., Ward T.R. Fluorescence-based assay for the optimization of the activity of artificial transfer hydrogenase within a biocompatible compartment. ChemCatChem 2013, 5:720-723.
    • (2013) ChemCatChem , vol.5 , pp. 720-723
    • Heinisch, T.1    Langowska, K.2    Tanner, P.3    Reymond, J.4    Meier, W.5    Palivan, C.6    Ward, T.R.7
  • 37
    • 84880018698 scopus 로고    scopus 로고
    • Human carbonic anhydrase II as host protein for the creation of artificial metalloenzymes: the asymmetric transfer hydrogenation of imines
    • Monnard F.W., Nogueira E.S., Heinisch T., Schirmer T., Ward T.R. Human carbonic anhydrase II as host protein for the creation of artificial metalloenzymes: the asymmetric transfer hydrogenation of imines. Chem Sci 2013, 4:3269-3270.
    • (2013) Chem Sci , vol.4 , pp. 3269-3270
    • Monnard, F.W.1    Nogueira, E.S.2    Heinisch, T.3    Schirmer, T.4    Ward, T.R.5
  • 38
    • 80155131668 scopus 로고    scopus 로고
    • An artificial metalloenzyme for olefin metathesis
    • Mayer C., Gillingham D.G., Ward T.R., Hilvert D. An artificial metalloenzyme for olefin metathesis. Chem Commun 2011, 47:12068-12070.
    • (2011) Chem Commun , vol.47 , pp. 12068-12070
    • Mayer, C.1    Gillingham, D.G.2    Ward, T.R.3    Hilvert, D.4
  • 39
    • 80155179922 scopus 로고    scopus 로고
    • Artificial metalloenzymes for olefin metathesis based on the biotin-(strept)avidin technology
    • Lo C., Ringenberg M.R., Gnandt D., Wilson Y., Ward T.R. Artificial metalloenzymes for olefin metathesis based on the biotin-(strept)avidin technology. Chem Commun 2011, 47:12065-12067.
    • (2011) Chem Commun , vol.47 , pp. 12065-12067
    • Lo, C.1    Ringenberg, M.R.2    Gnandt, D.3    Wilson, Y.4    Ward, T.R.5
  • 40
    • 84856650934 scopus 로고    scopus 로고
    • Creation of an artificial metalloprotein with a Hoveyda-Grubbs catalyst moiety through the intrinsic inhibition mechanism of alpha-chymotrypsin
    • Matsuo T., Imai C., Yoshida T., Saito T., Hayashi T., Hirota S. Creation of an artificial metalloprotein with a Hoveyda-Grubbs catalyst moiety through the intrinsic inhibition mechanism of alpha-chymotrypsin. Chem Commun 2012, 48:1662-1670.
    • (2012) Chem Commun , vol.48 , pp. 1662-1670
    • Matsuo, T.1    Imai, C.2    Yoshida, T.3    Saito, T.4    Hayashi, T.5    Hirota, S.6
  • 41
    • 77955035554 scopus 로고    scopus 로고
    • Rhodium-catalyzed oxidative cycloaddition of benzamides and alkynes via CH/NH activation
    • Hyster T.K., Rovis T. Rhodium-catalyzed oxidative cycloaddition of benzamides and alkynes via CH/NH activation. J Am Chem Soc 2010, 132:10565-10569.
    • (2010) J Am Chem Soc , vol.132 , pp. 10565-10569
    • Hyster, T.K.1    Rovis, T.2
  • 42
    • 84867768045 scopus 로고    scopus 로고
    • Biotinylated Rh(III) complexes in engineered streptavidin for accelerated asymmetric CH activation
    • Hyster T.K., Knörr L., Ward T.R., Rovis T. Biotinylated Rh(III) complexes in engineered streptavidin for accelerated asymmetric CH activation. Science 2012, 338:500-503.
    • (2012) Science , vol.338 , pp. 500-503
    • Hyster, T.K.1    Knörr, L.2    Ward, T.R.3    Rovis, T.4
  • 43
    • 84862161014 scopus 로고    scopus 로고
    • DNA-based catalytic enantioselective intermolecular oxa-Michael addition reactions
    • Megens R.P., Roelfes G. DNA-based catalytic enantioselective intermolecular oxa-Michael addition reactions. Chem Commun 2012, 48:6366-6370.
    • (2012) Chem Commun , vol.48 , pp. 6366-6370
    • Megens, R.P.1    Roelfes, G.2
  • 44
    • 84875776320 scopus 로고    scopus 로고
    • DNA-based asymmetric organometallic catalysis in water
    • Oelerich J., Roelfes G. DNA-based asymmetric organometallic catalysis in water. Chem Sci 2013, 4:2013-2020.
    • (2013) Chem Sci , vol.4 , pp. 2013-2020
    • Oelerich, J.1    Roelfes, G.2
  • 48
    • 84890591937 scopus 로고    scopus 로고
    • Co-immobilization of an enzyme and a metal into the compartments of mesoporous silica for cooperative tandem catalysis: an artificial metalloenzyme
    • Engström K., Johnston E.V., Verho O., Gustafson K.P.J., Shakeri M., Tai C., Bäckvall J. Co-immobilization of an enzyme and a metal into the compartments of mesoporous silica for cooperative tandem catalysis: an artificial metalloenzyme. Angew Chem Int Ed 2013, 52:14006-14010.
    • (2013) Angew Chem Int Ed , vol.52 , pp. 14006-14010
    • Engström, K.1    Johnston, E.V.2    Verho, O.3    Gustafson, K.P.J.4    Shakeri, M.5    Tai, C.6    Bäckvall, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.