메뉴 건너뛰기




Volumn 44, Issue 1, 2011, Pages 47-57

Artificial metalloenzymes based on the biotin - Avidin technology: Enantioselective catalysis and beyond

Author keywords

[No Author keywords available]

Indexed keywords

AVIDIN; BIOTIN; METALLOPROTEINASE; PALLADIUM; PHOSPHINE; PHOSPHINE DERIVATIVE; RHODIUM; RUTHENIUM;

EID: 78751548138     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar100099u     Document Type: Article
Times cited : (286)

References (56)
  • 3
    • 0035903602 scopus 로고    scopus 로고
    • Investigating and engineering enzymes by genetic selection
    • Taylor, S. V.; Kast, P.; Hilvert, D. Investigating and engineering enzymes by genetic selection Angew. Chem., Int. Ed. 2001, 40, 3310-3335
    • (2001) Angew. Chem., Int. Ed. , vol.40 , pp. 3310-3335
    • Taylor, S.V.1    Kast, P.2    Hilvert, D.3
  • 6
    • 37049099038 scopus 로고
    • Studies on the oxidase activity of Copper(II) carboxypeptidase
    • Yamamura, K.; Kaiser, E. T. Studies on the oxidase activity of Copper(II) carboxypeptidase J. Chem. Soc., Chem. Commun. 1976, 830-831
    • (1976) J. Chem. Soc., Chem. Commun. , pp. 830-831
    • Yamamura, K.1    Kaiser, E.T.2
  • 8
    • 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
  • 9
    • 33845185284 scopus 로고
    • Conversion of a protease into an acyl transferase: Selenosubtilisin
    • Wu, Z.-P.; Hilvert, D. Conversion of a protease into an acyl transferase: selenosubtilisin J. Am. Chem. Soc. 1989, 111, 4513-4514
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 4513-4514
    • Wu, Z.-P.1    Hilvert, D.2
  • 10
    • 0242701926 scopus 로고    scopus 로고
    • Pyridoxamine-amino acid chimeras in semisynthetic aminotransferase mimics
    • Roy, R. S.; Imperiali, B. Pyridoxamine-amino acid chimeras in semisynthetic aminotransferase mimics Protein Eng. 1997, 10, 691-698
    • (1997) Protein Eng. , vol.10 , pp. 691-698
    • Roy, R.S.1    Imperiali, B.2
  • 11
    • 0033591129 scopus 로고    scopus 로고
    • Catalytic hydrogenation of itaconic acid in a biotinylated pyrphos-rhodium(I) system in a protein cavity
    • Lin, C.-C.; Lin, C.-W.; Chan, A. S. C. Catalytic hydrogenation of itaconic acid in a biotinylated pyrphos-rhodium(I) system in a protein cavity Tetrahedron: Asymmetry 1999, 10, 1887-1893
    • (1999) Tetrahedron: Asymmetry , vol.10 , pp. 1887-1893
    • Lin, C.-C.1    Lin, C.-W.2    Chan, A.S.C.3
  • 12
    • 0035471137 scopus 로고    scopus 로고
    • Generation of new enzymes via covalent modification of existing proteins
    • Qi, D.; Tann, C.-M.; Haring, D.; Distefano, M. D. Generation of new enzymes via covalent modification of existing proteins Chem. Rev. 2001, 101, 3081-3111
    • (2001) Chem. Rev. , vol.101 , pp. 3081-3111
    • Qi, D.1    Tann, C.-M.2    Haring, D.3    Distefano, M.D.4
  • 14
    • 68949195832 scopus 로고    scopus 로고
    • Design of functional metalloproteins
    • Lu, Y.; Yeung, N.; Sieracki, N.; Marshall, N. M. Design of functional metalloproteins Nature 2009, 460, 855-862
    • (2009) Nature , vol.460 , pp. 855-862
    • Lu, Y.1    Yeung, N.2    Sieracki, N.3    Marshall, N.M.4
  • 15
    • 62549124067 scopus 로고    scopus 로고
    • Directed Evolution of Stereoselective Hybrid Catalysts
    • Reetz, M. T. Directed Evolution of Stereoselective Hybrid Catalysts Top. Organomet. Chem. 2009, 25, 63-92
    • (2009) Top. Organomet. Chem. , vol.25 , pp. 63-92
    • Reetz, M.T.1
  • 16
    • 60749117181 scopus 로고    scopus 로고
    • Stereoselective hydrogenation of olefins using rhodium-substituted carbonic anhydrase - A new reductase
    • Jing, Q.; Okrasa, K.; Kazlauskas, R. J. Stereoselective hydrogenation of olefins using rhodium-substituted carbonic anhydrase-A new reductase Chem. - Eur. J. 2009, 15, 1370-1376
    • (2009) Chem. - Eur. J. , vol.15 , pp. 1370-1376
    • Jing, Q.1    Okrasa, K.2    Kazlauskas, R.J.3
  • 17
    • 62549084238 scopus 로고    scopus 로고
    • Artificial metalloproteins exploiting vacant space: Preparation, structures, and functions
    • Abe, S.; Ueno, T.; Watanabe, Y. Artificial metalloproteins exploiting vacant space: preparation, structures, and functions Top. Organomet. Chem. 2009, 25, 25-43
    • (2009) Top. Organomet. Chem. , vol.25 , pp. 25-43
    • Abe, S.1    Ueno, T.2    Watanabe, Y.3
  • 19
    • 0035178343 scopus 로고    scopus 로고
    • Design and synthesis of compartmental ligands and their complexes for catalytic antibodies
    • Duclos, S.; Ward, T. R.; Stoeckli-Evans, H. Design and synthesis of compartmental ligands and their complexes for catalytic antibodies Helv. Chim. Acta 2001, 84, 3148-3161
    • (2001) Helv. Chim. Acta , vol.84 , pp. 3148-3161
    • Duclos, S.1    Ward, T.R.2    Stoeckli-Evans, H.3
  • 20
    • 13444251466 scopus 로고    scopus 로고
    • Electrophoretic behavior of streptavidin complexed to a biotinylated probe: A functional screening assay for biotin-binding proteins
    • Humbert, N.; Zocchi, A.; Ward, T. R. Electrophoretic behavior of streptavidin complexed to a biotinylated probe: a functional screening assay for biotin-binding proteins Electrophoresis 2005, 26, 47-52
    • (2005) Electrophoresis , vol.26 , pp. 47-52
    • Humbert, N.1    Zocchi, A.2    Ward, T.R.3
  • 21
  • 22
    • 41149149567 scopus 로고    scopus 로고
    • Counter propagation artificial neural networks modeling of an enantioselectivity of artificial metalloenzymes
    • Mazurek, S.; Ward, T. R.; Novic, M. Counter propagation artificial neural networks modeling of an enantioselectivity of artificial metalloenzymes Mol. Diversity 2007, 11, 141-152
    • (2007) Mol. Diversity , vol.11 , pp. 141-152
    • Mazurek, S.1    Ward, T.R.2    Novic, M.3
  • 23
    • 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, U. E.; Ward, T. R. 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. 2005, 44, 7764-7767
    • (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    Ward, T.R.7
  • 24
    • 2242424513 scopus 로고    scopus 로고
    • Enzyme fingerprints of activity, stereo and enantioselectivity from fluorogenic and chromogenic substrate arrays
    • Wahler, D.; Badalassi, F.; Crotti, P.; Reymond, J.-L. Enzyme fingerprints of activity, stereo and enantioselectivity from fluorogenic and chromogenic substrate arrays Chem. - Eur. J. 2002, 8, 3211-3228
    • (2002) Chem. - Eur. J. , vol.8 , pp. 3211-3228
    • Wahler, D.1    Badalassi, F.2    Crotti, P.3    Reymond, J.-L.4
  • 25
    • 34548421899 scopus 로고    scopus 로고
    • Second generation artificial hydrogenases based on the biotin avidin technology: Improving activity, stability and selectivity by introduction of enantiopure aminoacid spacers
    • Rusbandi, U. E.; Lo, C.; Skander, M.; Ivanova, A.; Creus, M.; Humbert, N.; Ward, T. R. Second generation artificial hydrogenases based on the biotin avidin technology: improving activity, stability and selectivity by introduction of enantiopure aminoacid spacers Adv. Synth. Catal. 2007, 349, 1923-1930
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1923-1930
    • Rusbandi, U.E.1    Lo, C.2    Skander, M.3    Ivanova, A.4    Creus, M.5    Humbert, N.6    Ward, T.R.7
  • 26
    • 33750070283 scopus 로고    scopus 로고
    • Directed evolution of hybrid enzymes: Evolving enantioselectivity of an achiral Rh-complex anchored to a protein
    • Reetz, M. T.; Peyeralans, J. J.-P.; Maichele, A.; Fu, Y.; Maywald, M. Directed evolution of hybrid enzymes: evolving enantioselectivity of an achiral Rh-complex anchored to a protein Chem. Commun. 2006, 4318-4320
    • (2006) Chem. Commun. , pp. 4318-4320
    • Reetz, M.T.1    Peyeralans, J.J.-P.2    Maichele, A.3    Fu, Y.4    Maywald, M.5
  • 27
    • 0042379988 scopus 로고    scopus 로고
    • Asymmetric transition-metal-catalyzed allylic alkylations: Applications in total synthesis
    • Trost, B. M.; Crawley, M. L. Asymmetric transition-metal-catalyzed allylic alkylations: applications in total synthesis Chem. Rev. 2003, 103, 2921-2943
    • (2003) Chem. Rev. , vol.103 , pp. 2921-2943
    • Trost, B.M.1    Crawley, M.L.2
  • 28
    • 27544497732 scopus 로고    scopus 로고
    • Springer: Berlin, Heidelberg and New York
    • Tsuji, J. Palladium in Organic Synthesis; Springer: Berlin, Heidelberg and New York, 2005; Vol. 14.
    • (2005) Palladium in Organic Synthesis , vol.14
    • Tsuji, J.1
  • 29
    • 0033949478 scopus 로고    scopus 로고
    • Phosphinooxazolines: A new class of versatile, modular P, N-ligands for asymmetric catalysis
    • Helmchen, G.; Pfaltz, A. Phosphinooxazolines: a new class of versatile, modular P, N-ligands for asymmetric catalysis Acc. Chem. Res. 2000, 33, 336-345
    • (2000) Acc. Chem. Res. , vol.33 , pp. 336-345
    • Helmchen, G.1    Pfaltz, A.2
  • 31
    • 0002123299 scopus 로고    scopus 로고
    • Asymmetric Transfer Hydrogenation Catalyzed by Chiral Ruthenium Complexes
    • Noyori, R.; Hashiguchi, S. Asymmetric transfer hydrogenation catalyzed by chiral ruthenium complexes Acc. Chem. Res. 1997, 30, 97-102 (Pubitemid 127472554)
    • (1997) Accounts of Chemical Research , vol.30 , Issue.2 , pp. 97-102
    • Noyori, R.1    Hashiguchi, S.2
  • 32
    • 33645681534 scopus 로고    scopus 로고
    • Bifunctional transition metal-based molecular catalysts for asymmetric syntheses
    • Ikariya, T.; Murata, K.; Noyori, R. Bifunctional transition metal-based molecular catalysts for asymmetric syntheses Org Biomol Chem 2006, 4, 393-406
    • (2006) Org Biomol Chem , vol.4 , pp. 393-406
    • Ikariya, T.1    Murata, K.2    Noyori, R.3
  • 33
    • 0030984352 scopus 로고    scopus 로고
    • The catalyst precursor, catalyst and intermediate in the Ru(II)-promoted asymmetric hydrogen transfer between alcohols and ketones
    • Haack, K.-J.; Hashiguchi, S.; Fujii, A.; Ikariya, T.; Noyori, R. The catalyst precursor, catalyst and intermediate in the Ru(II)-promoted asymmetric hydrogen transfer between alcohols and ketones Angew. Chem., Int. Ed. Engl. 1997, 36, 285-288
    • (1997) Angew. Chem., Int. Ed. Engl. , vol.36 , pp. 285-288
    • Haack, K.-J.1    Hashiguchi, S.2    Fujii, A.3    Ikariya, T.4    Noyori, R.5
  • 35
    • 16444378860 scopus 로고    scopus 로고
    • Artificial metalloenzymes based on biotin-avidin technology for the enantioselective reduction of ketones by transfer hydrogenation
    • Letondor, C.; Humbert, N.; Ward, T. R. Artificial metalloenzymes based on biotin-avidin technology for the enantioselective reduction of ketones by transfer hydrogenation Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 4683-4687
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 4683-4687
    • Letondor, C.1    Humbert, N.2    Ward, T.R.3
  • 36
    • 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, C.; Pordea, A.; Humbert, N.; Ivanova, A.; Mazurek, S.; Novic, M.; Ward, T. R. 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. 2006, 128, 8320-8328
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 8320-8328
    • Letondor, C.1    Pordea, A.2    Humbert, N.3    Ivanova, A.4    Mazurek, S.5    Novic, M.6    Ward, T.R.7
  • 39
    • 48249096140 scopus 로고    scopus 로고
    • Enantioselective transfer hydrogenation of aliphatic ketones catalyzed by ruthenium complexes linked to the secondary face of beta-cyclodextrin
    • Schlatter, A.; Woggon, W.-D. Enantioselective transfer hydrogenation of aliphatic ketones catalyzed by ruthenium complexes linked to the secondary face of beta-cyclodextrin Adv. Synth. Catal. 2008, 350, 995-1000
    • (2008) Adv. Synth. Catal. , vol.350 , pp. 995-1000
    • Schlatter, A.1    Woggon, W.-D.2
  • 40
    • 0037090667 scopus 로고    scopus 로고
    • New methods for the high-throughput screening of enantioselective catalysts and biocatalysts
    • Reetz, M. T. New methods for the high-throughput screening of enantioselective catalysts and biocatalysts Angew. Chem., Int. Ed. 2002, 41, 1335-1338
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 1335-1338
    • Reetz, M.T.1
  • 41
    • 0036084211 scopus 로고    scopus 로고
    • Emerging methods for the rapid determination of enantiomeric excess
    • Finn, M. G. Emerging methods for the rapid determination of enantiomeric excess Chirality 2002, 14, 534-540
    • (2002) Chirality , vol.14 , pp. 534-540
    • Finn, M.G.1
  • 43
    • 27144466404 scopus 로고    scopus 로고
    • Aqueous oxidation of alcohols catalyzed by artificial metalloenzymes based on the biotin-avidin technology
    • DOI 10.1016/j.jorganchem.2005.02.001, PII S0022328X05000860
    • Thomas, C. M.; Letondor, C.; Humbert, N.; Ward, T. R. Aqueous oxidation of alcohols catalyzed by artificial metalloenzymes based on the biotin-avidin technology J. Organomet. Chem. 2005, 690, 4488-4491 (Pubitemid 41508809)
    • (2005) Journal of Organometallic Chemistry , vol.690 , Issue.20 SPEC. ISS. , pp. 4488-4491
    • Thomas, C.M.1    Letondor, C.2    Humbert, N.3    Ward, T.R.4
  • 44
    • 36448950558 scopus 로고    scopus 로고
    • Homogeneous catalytic reduction of dioxygen using transfer hydrogenation catalysts
    • Heiden, Z.; Rauchfuss, T. Homogeneous catalytic reduction of dioxygen using transfer hydrogenation catalysts J. Am. Chem. Soc. 2007, 129, 14303-14310
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 14303-14310
    • Heiden, Z.1    Rauchfuss, T.2
  • 45
    • 47249088167 scopus 로고    scopus 로고
    • Aerobic oxidative kinetic resolution of racemic secondary alcohols with chiral bifunctional amido complexes
    • Arita, S.; Koike, T.; Kayaki, Y.; Ikariya, T. Aerobic oxidative kinetic resolution of racemic secondary alcohols with chiral bifunctional amido complexes Angew. Chem., Int. Ed. 2008, 47, 2447-2449
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 2447-2449
    • Arita, S.1    Koike, T.2    Kayaki, Y.3    Ikariya, T.4
  • 46
    • 60749108585 scopus 로고    scopus 로고
    • Incorporation of biotinylated manganese-salen complexes into streptavidin: New artificial metalloenzymes for enantioselective sulfoxidation
    • Pordea, A.; Mathis, D.; Ward, T. R. Incorporation of biotinylated manganese-salen complexes into streptavidin: new artificial metalloenzymes for enantioselective sulfoxidation J. Organomet. Chem. 2009, 694, 930-936
    • (2009) J. Organomet. Chem. , vol.694 , pp. 930-936
    • Pordea, A.1    Mathis, D.2    Ward, T.R.3
  • 47
    • 21844444521 scopus 로고    scopus 로고
    • Enantioselective sulfoxidation mediated by vanadium-incorporated phytase: A hydrolase acting as a peroxidase
    • van de Velde, F.; Könemann, L.; Rantwijk, F. v.; Sheldon, R. A. Enantioselective sulfoxidation mediated by vanadium-incorporated phytase: a hydrolase acting as a peroxidase Chem. Commun. 1998, 1891-1892
    • (1998) Chem. Commun. , pp. 1891-1892
    • Van De Velde, F.1    Könemann, L.2    F, V.R.3    Sheldon, R.A.4
  • 49
    • 0033515037 scopus 로고    scopus 로고
    • Affinity modulation of small-molecule ligands by borrowing endogenous protein surfaces
    • Briesewitz, R.; Ray, G.; Wandless, T.; Crabtree, G. Affinity modulation of small-molecule ligands by borrowing endogenous protein surfaces Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 1953-1958
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1953-1958
    • Briesewitz, R.1    Ray, G.2    Wandless, T.3    Crabtree, G.4
  • 50
    • 0037133312 scopus 로고    scopus 로고
    • Forced engagement of a RNA/protein complex by a chemical inducer of dimerization to modulate gene expression
    • Harvey, I.; Garneau, P.; Pelletier, J. Forced engagement of a RNA/protein complex by a chemical inducer of dimerization to modulate gene expression Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 1882-1887
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1882-1887
    • Harvey, I.1    Garneau, P.2    Pelletier, J.3
  • 51
    • 27144530274 scopus 로고    scopus 로고
    • Organometallic chemistry, biology and medicine: Ruthenium arene anticancer complexes
    • Yan, Y. K.; Melchart, M.; Habtemariam, A.; Sadler, P. J. Organometallic chemistry, biology and medicine: ruthenium arene anticancer complexes Chem. Commun. 2005, 4764-4776
    • (2005) Chem. Commun. , pp. 4764-4776
    • Yan, Y.K.1    Melchart, M.2    Habtemariam, A.3    Sadler, P.J.4
  • 52
    • 34249900982 scopus 로고    scopus 로고
    • Direct cellular response to platinum-induced DNA damage
    • Jung, A.; Lippard, S. J. Direct cellular response to platinum-induced DNA damage Chem. Rev. 2007, 107, 1387-1407
    • (2007) Chem. Rev. , vol.107 , pp. 1387-1407
    • Jung, A.1    Lippard, S.J.2
  • 53
    • 43049147578 scopus 로고    scopus 로고
    • New Trends for metal complexes with anticancer activity
    • Bruijnincx, P. C. A.; Sadler, P. J. New Trends for metal complexes with anticancer activity Curr. Opin. Chem. Biol. 2008, 12, 197-206
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 197-206
    • Bruijnincx, P.C.A.1    Sadler, P.J.2
  • 55
    • 0033594341 scopus 로고    scopus 로고
    • Structural basis for the differential effects on telomerase inhibition
    • Han, F. X.; Wheelhouse, R. T.; Hurley, L. H. Structural basis for the differential effects on telomerase inhibition J. Am. Chem. Soc. 1999, 121, 3561-3569
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 3561-3569
    • Han, F.X.1    Wheelhouse, R.T.2    Hurley, L.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.