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Volumn 110, Issue 12, 2013, Pages 3085-3092

Overcoming co-product inhibition in the nicotinamide independent asymmetric bioreduction of activated C=C-bonds using flavin-dependent ene-reductases

Author keywords

Disproportionation; Ene reductase; In situ co product removal; Old yellow enzyme

Indexed keywords

ASYMMETRIC BIOREDUCTION; CO-PRODUCTS; CONJUGATED ENONES; DISPROPORTIONATIONS; ENE-REDUCTASE; HYDROGEN TRANSFER; OLD YELLOW ENZYMES; POLYMERIC ADSORBENT;

EID: 84886293347     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.24981     Document Type: Article
Times cited : (24)

References (52)
  • 1
    • 0017148370 scopus 로고
    • Interaction of phenols with old yellow enzyme. Physical evidence for charge-transfer complexes
    • Abramovitz AS, Massey V. 1976a. Interaction of phenols with old yellow enzyme. Physical evidence for charge-transfer complexes. J Biol Chem 251:5327-5336.
    • (1976) J Biol Chem , vol.251 , pp. 5327-5336
    • Abramovitz, A.S.1    Massey, V.2
  • 2
    • 0017170511 scopus 로고
    • Purification of intact old yellow enzyme using an affinity matrix for the sole chromatographic step
    • Abramovitz AS, Massey V. 1976b. Purification of intact old yellow enzyme using an affinity matrix for the sole chromatographic step. J Biol Chem 251:5321-5326.
    • (1976) J Biol Chem , vol.251 , pp. 5321-5326
    • Abramovitz, A.S.1    Massey, V.2
  • 4
    • 0032491154 scopus 로고    scopus 로고
    • Binding and reactivity of Candida albicans estrogen binding protein with steroid and other substrates
    • Buckman J, Miller SM. 1998. Binding and reactivity of Candida albicans estrogen binding protein with steroid and other substrates. Biochemistry 37:14326-14336.
    • (1998) Biochemistry , vol.37 , pp. 14326-14336
    • Buckman, J.1    Miller, S.M.2
  • 5
    • 0034730103 scopus 로고    scopus 로고
    • Stabilization of a novel enzyme-substrate intermediate in the Y206F mutant of Candida albicans EBP1: Evidence for acid catalysis
    • Buckman J, Miller SM. 2000a. Stabilization of a novel enzyme-substrate intermediate in the Y206F mutant of Candida albicans EBP1: Evidence for acid catalysis. Biochemistry 39:10532-10541.
    • (2000) Biochemistry , vol.39 , pp. 10532-10541
    • Buckman, J.1    Miller, S.M.2
  • 6
    • 0034730082 scopus 로고    scopus 로고
    • Transient kinetics and intermediates formed during the electron transfer reaction catalyzed by Candida albicans estrogen binding
    • Buckman J, Miller SM. 2000b. Transient kinetics and intermediates formed during the electron transfer reaction catalyzed by Candida albicans estrogen binding. Prot Biochem 39:10521-10531.
    • (2000) Prot Biochem , vol.39 , pp. 10521-10531
    • Buckman, J.1    Miller, S.M.2
  • 7
    • 33745044453 scopus 로고    scopus 로고
    • Characterization of a thermostable NADPH:FMN oxidoreductase from the mesophilic bacterium Bacillus subtilis
    • Deller S, Sollner S, Trenker-El-Toukhy R, Jelesarov I, Gübitz GM, Macheroux P. 2006. Characterization of a thermostable NADPH:FMN oxidoreductase from the mesophilic bacterium Bacillus subtilis. Biochemistry 45:7083-7091.
    • (2006) Biochemistry , vol.45 , pp. 7083-7091
    • Deller, S.1    Sollner, S.2    Trenker-El-Toukhy, R.3    Jelesarov, I.4    Gübitz, G.M.5    Macheroux, P.6
  • 8
    • 77950570908 scopus 로고    scopus 로고
    • The flavoprotein-catalyzed reduction of aliphatic nitro-compounds represents a biocatalytic equivalent to the Nef-reaction
    • Durchschein K, Ferreira-da Silva B, Wallner S, Macheroux P, Kroutil W, Glueck SM, Faber K. 2010. The flavoprotein-catalyzed reduction of aliphatic nitro-compounds represents a biocatalytic equivalent to the Nef-reaction. Green Chem 12:616-619.
    • (2010) Green Chem , vol.12 , pp. 616-619
    • Durchschein, K.1    Ferreira-da Silva, B.2    Wallner, S.3    Macheroux, P.4    Kroutil, W.5    Glueck, S.M.6    Faber, K.7
  • 9
    • 29644436037 scopus 로고    scopus 로고
    • Production of 2-phenylethanol and 2-phenylethylacetate from L-phenylalanine by coupling whole-cell biocatalysis with organophilic pervaporation
    • Etschmann MMW, Sell D, Schrader J. 2005. Production of 2-phenylethanol and 2-phenylethylacetate from L-phenylalanine by coupling whole-cell biocatalysis with organophilic pervaporation. Biotechnol Bioeng 92:624-634.
    • (2005) Biotechnol Bioeng , vol.92 , pp. 624-634
    • Etschmann, M.M.W.1    Sell, D.2    Schrader, J.3
  • 11
    • 72149102108 scopus 로고    scopus 로고
    • Asymmetric reduction of activated alkenes by pentaerythritol tetranitrate reductase: Specificity and control of stereochemical outcome by reaction optimisation
    • Fryszkowska A, Toogood H, Sakuma M, Gardiner JM, Stephens GM, Scrutton NS. 2009. Asymmetric reduction of activated alkenes by pentaerythritol tetranitrate reductase: Specificity and control of stereochemical outcome by reaction optimisation. Adv Synth Catal 351:2976-2990.
    • (2009) Adv Synth Catal , vol.351 , pp. 2976-2990
    • Fryszkowska, A.1    Toogood, H.2    Sakuma, M.3    Gardiner, J.M.4    Stephens, G.M.5    Scrutton, N.S.6
  • 13
    • 34250782749 scopus 로고    scopus 로고
    • Asymmetric bioreduction of activated alkenes using cloned 12-oxophytodienoate reductase isoenzymes OPR-1 and OPR-3 from Lycopersicon esculentum (tomato): A striking change of stereoselectivity
    • Hall M, Stueckler C, Kroutil W, Macheroux P, Faber K. 2007. Asymmetric bioreduction of activated alkenes using cloned 12-oxophytodienoate reductase isoenzymes OPR-1 and OPR-3 from Lycopersicon esculentum (tomato): A striking change of stereoselectivity. Angew Chem Int Ed 46:3934-3937.
    • (2007) Angew Chem Int Ed , vol.46 , pp. 3934-3937
    • Hall, M.1    Stueckler, C.2    Kroutil, W.3    Macheroux, P.4    Faber, K.5
  • 14
    • 53849094459 scopus 로고    scopus 로고
    • Asymmetric bioreduction of activated C=C bonds using Zymomonas mobilis NCR enoate reductase and old yellow enzymes OYE-1-3 from yeasts
    • Hall M, Stueckler C, Hauer B, Stuermer R, Friedrich T, Breuer M, Kroutil W, Faber K. 2008. Asymmetric bioreduction of activated C=C bonds using Zymomonas mobilis NCR enoate reductase and old yellow enzymes OYE-1-3 from yeasts. Eur J Org Chem 1511-1516.
    • (2008) Eur J Org Chem , pp. 1511-1516
    • Hall, M.1    Stueckler, C.2    Hauer, B.3    Stuermer, R.4    Friedrich, T.5    Breuer, M.6    Kroutil, W.7    Faber, K.8
  • 15
    • 47149101254 scopus 로고    scopus 로고
    • 2-forming NADH oxidase from 2-phenylethanol-assimilating Brevibacterium sp. KU1309
    • 2-forming NADH oxidase from 2-phenylethanol-assimilating Brevibacterium sp. KU1309. Appl Microbiol Biotechnol 80:71-78.
    • (2008) Appl Microbiol Biotechnol , vol.80 , pp. 71-78
    • Hirano, J.-I.1    Miyamoto, K.2    Ohta, H.3
  • 16
    • 79751520578 scopus 로고    scopus 로고
    • Biocatalytic redox reactions for organic synthesis: Nonconventional regeneration methods
    • Hollmann F, Arends IWCE, Buehler K. 2010. Biocatalytic redox reactions for organic synthesis: Nonconventional regeneration methods. Chem Cat Chem 2:762-782.
    • (2010) Chem Cat Chem , vol.2 , pp. 762-782
    • Hollmann, F.1    Arends, I.W.C.E.2    Buehler, K.3
  • 17
    • 4644234429 scopus 로고    scopus 로고
    • Hydrogen peroxide-producing NADH oxidase (nox-1) from Lactococcus lactis
    • Jiang R, Bommarius AS. 2004. Hydrogen peroxide-producing NADH oxidase (nox-1) from Lactococcus lactis. Tetrahedron Asymmetry 15:2939-2944.
    • (2004) Tetrahedron Asymmetry , vol.15 , pp. 2939-2944
    • Jiang, R.1    Bommarius, A.S.2
  • 18
    • 0029557273 scopus 로고
    • Structure-function relations for old yellow enzyme
    • Karplus PA, Fox KM, Massey V. 1995. Structure-function relations for old yellow enzyme. FASEB J 9:1518-1826.
    • (1995) FASEB J , vol.9 , pp. 1518-1826
    • Karplus, P.A.1    Fox, K.M.2    Massey, V.3
  • 20
    • 0033213860 scopus 로고    scopus 로고
    • Application of in situ product removal techniques to biocatalytic processes
    • Lye GJ, Woodley JM. 1999. Application of in situ product removal techniques to biocatalytic processes. Trends Biotechnol 17:395-402.
    • (1999) Trends Biotechnol , vol.17 , pp. 395-402
    • Lye, G.J.1    Woodley, J.M.2
  • 21
    • 12344257726 scopus 로고    scopus 로고
    • Glyoxylic acid and MP-glyoxylate: Efficient formaldehyde equivalents in the 3-CC of 2-aminoazines, aldehydes, and isonitriles
    • Lyon MA, Kercher TS. 2004. Glyoxylic acid and MP-glyoxylate: Efficient formaldehyde equivalents in the 3-CC of 2-aminoazines, aldehydes, and isonitriles. Org Lett 6:4989-4992.
    • (2004) Org Lett , vol.6 , pp. 4989-4992
    • Lyon, M.A.1    Kercher, T.S.2
  • 22
    • 65349190562 scopus 로고    scopus 로고
    • Recent progress in biocatalysis for asymmetric oxidation and reduction
    • Matsuda T, Yamanaka R, Nakamura K. 2009. Recent progress in biocatalysis for asymmetric oxidation and reduction. Tetrahedron Asymmetry 20:513-557.
    • (2009) Tetrahedron Asymmetry , vol.20 , pp. 513-557
    • Matsuda, T.1    Yamanaka, R.2    Nakamura, K.3
  • 23
    • 0016766271 scopus 로고
    • Identification of p-hydroxybenzaldehyde as the ligand in the green form of old yellow enzyme
    • Matthews RG, Massey V, Sweeley CC. 1975. Identification of p-hydroxybenzaldehyde as the ligand in the green form of old yellow enzyme. J Biol Chem 250:9294-9298.
    • (1975) J Biol Chem , vol.250 , pp. 9294-9298
    • Matthews, R.G.1    Massey, V.2    Sweeley, C.C.3
  • 25
    • 62249218236 scopus 로고    scopus 로고
    • Epoxidation of conjugated C=C-bonds and sulfur-oxidation of thioethers mediated by NADH:FMN-dependent oxidoreductases
    • Mueller NJ, Stueckler C, Hall M, Macheroux P, Faber K. 2009. Epoxidation of conjugated C=C-bonds and sulfur-oxidation of thioethers mediated by NADH:FMN-dependent oxidoreductases. Org Biomol Chem 7:1115-1119.
    • (2009) Org Biomol Chem , vol.7 , pp. 1115-1119
    • Mueller, N.J.1    Stueckler, C.2    Hall, M.3    Macheroux, P.4    Faber, K.5
  • 26
    • 77149145484 scopus 로고    scopus 로고
    • The substrate spectra of pentaerythritol tetranitrate reductase, morphinone reductase, N-ethylmaleimide reductase and estrogen-binding protein in the asymmetric bioreduction of activated alkenes
    • Mueller NJ, Stueckler C, Hauer B, Baudendistel N, Housden H, Bruce NC, Faber K. 2010. The substrate spectra of pentaerythritol tetranitrate reductase, morphinone reductase, N-ethylmaleimide reductase and estrogen-binding protein in the asymmetric bioreduction of activated alkenes. Adv Synth Catal 352:387-394.
    • (2010) Adv Synth Catal , vol.352 , pp. 387-394
    • Mueller, N.J.1    Stueckler, C.2    Hauer, B.3    Baudendistel, N.4    Housden, H.5    Bruce, N.C.6    Faber, K.7
  • 27
    • 34548240307 scopus 로고    scopus 로고
    • Asymmetric alkene reduction by yeast old yellow enzymes and by a novel Zymomonas mobilis reductase
    • Muller A, Hauer B, Rosche B. 2007. Asymmetric alkene reduction by yeast old yellow enzymes and by a novel Zymomonas mobilis reductase. Biotechnol Bioeng 98:22-29.
    • (2007) Biotechnol Bioeng , vol.98 , pp. 22-29
    • Muller, A.1    Hauer, B.2    Rosche, B.3
  • 28
    • 41949115394 scopus 로고    scopus 로고
    • A novel chromate reductase from Thermus scotoductus SA-01 related to old yellow enzyme
    • Opperman DJ, Piater LA, van Heerden E. 2008. A novel chromate reductase from Thermus scotoductus SA-01 related to old yellow enzyme. J Bacteriol 190:3076-3082.
    • (2008) J Bacteriol , vol.190 , pp. 3076-3082
    • Opperman, D.J.1    Piater, L.A.2    van Heerden, E.3
  • 33
    • 0035938403 scopus 로고    scopus 로고
    • Solution-phase parallel synthesis of 5-carboxamido 1-benzyl-3-(3-dimethylaminopropyloxy)-1H-pyrazoles as activators of soluble guanylate cyclase with improved oral bioavailability
    • Selwood DL, Brummell DG, Glen RC, Goggin MC, Reynolds K, Tatlock MA, Wishart G. 2001. Solution-phase parallel synthesis of 5-carboxamido 1-benzyl-3-(3-dimethylaminopropyloxy)-1H-pyrazoles as activators of soluble guanylate cyclase with improved oral bioavailability. Bioorg Med Chem Lett 11:1089-1092.
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 1089-1092
    • Selwood, D.L.1    Brummell, D.G.2    Glen, R.C.3    Goggin, M.C.4    Reynolds, K.5    Tatlock, M.A.6    Wishart, G.7
  • 34
    • 33846970531 scopus 로고    scopus 로고
    • Lot6p from Saccharomyces cerevisiae is a FMN-dependent reductase with a potential role in quinone detoxification
    • Sollner S, Nebauer R, Ehammer H, Prem A, Deller S, Palfey BA, Daum G, Macheroux P. 2007. Lot6p from Saccharomyces cerevisiae is a FMN-dependent reductase with a potential role in quinone detoxification. FEBS J 274:1328-1339.
    • (2007) FEBS J , vol.274 , pp. 1328-1339
    • Sollner, S.1    Nebauer, R.2    Ehammer, H.3    Prem, A.4    Deller, S.5    Palfey, B.A.6    Daum, G.7    Macheroux, P.8
  • 35
    • 77950866209 scopus 로고    scopus 로고
    • Cysteine as a modulator residue in the active site of xenobiotic reductase A: A structural, thermodynamic and kinetic study
    • Spiegelhauer O, Mende S, Dickert F, Knauer SH, Ullmann GM, Dobbek H. 2010. Cysteine as a modulator residue in the active site of xenobiotic reductase A: A structural, thermodynamic and kinetic study. J Mol Biol 398:66-82.
    • (2010) J Mol Biol , vol.398 , pp. 66-82
    • Spiegelhauer, O.1    Mende, S.2    Dickert, F.3    Knauer, S.H.4    Ullmann, G.M.5    Dobbek, H.6
  • 36
    • 0037948335 scopus 로고    scopus 로고
    • In situ product removal (ISPR) in whole cell biotechnology during the last twenty years
    • Stark D, von Stockar U. 2003. In situ product removal (ISPR) in whole cell biotechnology during the last twenty years. Adv Biochem Eng Biotechnol 80:149-175.
    • (2003) Adv Biochem Eng Biotechnol , vol.80 , pp. 149-175
    • Stark, D.1    von Stockar, U.2
  • 37
    • 0022393945 scopus 로고
    • Potentiometric studies of native and flavin-substituted old yellow enzyme
    • Stewart RC, Massey V. 1985. Potentiometric studies of native and flavin-substituted old yellow enzyme. J Biol Chem 260:13639-13647.
    • (1985) J Biol Chem , vol.260 , pp. 13639-13647
    • Stewart, R.C.1    Massey, V.2
  • 38
    • 0041031592 scopus 로고    scopus 로고
    • A homolog of old yellow enzyme in tomato. Spectral properties and substrate specificity of the recombinant protein
    • Strassner J, Furholz A, Macheroux P, Amrhein N, Schaller A. 1999. A homolog of old yellow enzyme in tomato. Spectral properties and substrate specificity of the recombinant protein. J Biol Chem 274:35067-35073.
    • (1999) J Biol Chem , vol.274 , pp. 35067-35073
    • Strassner, J.1    Furholz, A.2    Macheroux, P.3    Amrhein, N.4    Schaller, A.5
  • 39
    • 38349186682 scopus 로고    scopus 로고
    • Stereocomplementary bioreduction of α,β-unsaturated dicarboxylic acids and dimethyl esters using enoate reductases: Enzyme- and substrate-based stereocontrol
    • Stueckler C, Hall M, Ehammer H, Pointner E, Kroutil W, Macheroux P, Faber K. 2007. Stereocomplementary bioreduction of α, β-unsaturated dicarboxylic acids and dimethyl esters using enoate reductases: Enzyme- and substrate-based stereocontrol. Org Lett 9:5409-5411.
    • (2007) Org Lett , vol.9 , pp. 5409-5411
    • Stueckler, C.1    Hall, M.2    Ehammer, H.3    Pointner, E.4    Kroutil, W.5    Macheroux, P.6    Faber, K.7
  • 40
    • 71649109063 scopus 로고    scopus 로고
    • Nicotinamide-independent asymmetric bioreduction of C=C-bonds via disproportionation of enones catalyzed by enoate reductases
    • Stueckler C, Reiter TC, Baudendistel N, Faber K. 2010. Nicotinamide-independent asymmetric bioreduction of C=C-bonds via disproportionation of enones catalyzed by enoate reductases. Tetrahedron 66:663-667.
    • (2010) Tetrahedron , vol.66 , pp. 663-667
    • Stueckler, C.1    Reiter, T.C.2    Baudendistel, N.3    Faber, K.4
  • 41
    • 34047189417 scopus 로고    scopus 로고
    • Asymmetric bioreduction of activated C=C bonds using enoate reductases from the old yellow enzyme family
    • Stuermer R, Hauer B, Hall M, Faber K. 2007. Asymmetric bioreduction of activated C=C bonds using enoate reductases from the old yellow enzyme family. Curr Opin Chem Biol 11:203-213.
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 203-213
    • Stuermer, R.1    Hauer, B.2    Hall, M.3    Faber, K.4
  • 42
    • 40949135111 scopus 로고    scopus 로고
    • Light-driven biocatalytic oxidation and reduction reactions: Scope and limitations
    • Taglieber A, Schulz F, Hollmann F, Rusek M, Reetz MT. 2008. Light-driven biocatalytic oxidation and reduction reactions: Scope and limitations. ChemBioChem 9:565-572.
    • (2008) ChemBioChem , vol.9 , pp. 565-572
    • Taglieber, A.1    Schulz, F.2    Hollmann, F.3    Rusek, M.4    Reetz, M.T.5
  • 43
    • 79954522978 scopus 로고    scopus 로고
    • A highly efficient ADH-coupled NADH-recycling system for the asymmetric bioreduction of carbon-carbon double bonds using enoate reductases
    • Tauber K, Hall M, Kroutil W, Fabian WMF, Faber K, Glueck SM. 2011. A highly efficient ADH-coupled NADH-recycling system for the asymmetric bioreduction of carbon-carbon double bonds using enoate reductases. Biotechnol Bioeng 108:1462-1467.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 1462-1467
    • Tauber, K.1    Hall, M.2    Kroutil, W.3    Fabian, W.M.F.4    Faber, K.5    Glueck, S.M.6
  • 44
    • 78149436277 scopus 로고    scopus 로고
    • Biocatalytic reductions and chemical versatility of the old yellow enzyme family of flavoprotein oxidoreductases
    • Toogood HS, Gardiner JM, Scrutton NS. 2010. Biocatalytic reductions and chemical versatility of the old yellow enzyme family of flavoprotein oxidoreductases. ChemCatChem 2:892-914.
    • (2010) ChemCatChem , vol.2 , pp. 892-914
    • Toogood, H.S.1    Gardiner, J.M.2    Scrutton, N.S.3
  • 45
    • 0028911853 scopus 로고
    • Old yellow enzyme: Aromatization of cyclic enones and the mechanism of a novel dismutation reaction
    • Vaz ADN, Chakraborty S, Massey V. 1995. Old yellow enzyme: Aromatization of cyclic enones and the mechanism of a novel dismutation reaction. Biochemistry 34:4246-4256.
    • (1995) Biochemistry , vol.34 , pp. 4246-4256
    • Vaz, A.D.N.1    Chakraborty, S.2    Massey, V.3
  • 46
    • 7044227654 scopus 로고    scopus 로고
    • Biochemical reaction engineering for redox reactions
    • Wandrey C. 2004. Biochemical reaction engineering for redox reactions. Chem Rec 4:254-265.
    • (2004) Chem Rec , vol.4 , pp. 254-265
    • Wandrey, C.1
  • 47
    • 85178465304 scopus 로고
    • Umwandlungen der Ketoxidoverbindungen; Bildung von β-Keto-aldehyden aus α,β-ungesättigten Ketonen
    • Weitz E, Scheffer A. 1921. Umwandlungen der Ketoxidoverbindungen; Bildung von β-Keto-aldehyden aus α, β-ungesättigten Ketonen. Ber Dtsch Chem Ges 54:2344-2353.
    • (1921) Ber Dtsch Chem Ges , vol.54 , pp. 2344-2353
    • Weitz, E.1    Scheffer, A.2
  • 48
    • 84871651706 scopus 로고    scopus 로고
    • Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds
    • Winkler CK, Tasnadi G, Clay D, Hall M, Faber K. 2012. Asymmetric bioreduction of activated alkenes to industrially relevant optically active compounds. J Biotechnol 162:381-389.
    • (2012) J Biotechnol , vol.162 , pp. 381-389
    • Winkler, C.K.1    Tasnadi, G.2    Clay, D.3    Hall, M.4    Faber, K.5
  • 50
    • 77950323964 scopus 로고    scopus 로고
    • Nitroreductase from Salmonella typhimurium: Characterization and catalytic activity
    • Yanto Y, Hall M, Bommarius AS. 2010a. Nitroreductase from Salmonella typhimurium: Characterization and catalytic activity. Org Biomol Chem 8:1826-1832.
    • (2010) Org Biomol Chem , vol.8 , pp. 1826-1832
    • Yanto, Y.1    Hall, M.2    Bommarius, A.S.3
  • 51
    • 78549238543 scopus 로고    scopus 로고
    • Characterization of xenobiotic reductase A (XenA): Study of active site residues, substrate spectrum and stability
    • Yanto Y, Yu H-H, Hall M, Bommarius AS. 2010b. Characterization of xenobiotic reductase A (XenA): Study of active site residues, substrate spectrum and stability. Chem Commun 46:8809-8811.
    • (2010) Chem Commun , vol.46 , pp. 8809-8811
    • Yanto, Y.1    Yu, H.-H.2    Hall, M.3    Bommarius, A.S.4
  • 52
    • 79956148088 scopus 로고    scopus 로고
    • Asymmetric bioreduction of alkenes using ene-reductases YersER and KYE1 and effects of organic solvents
    • Yanto Y, Winkler CK, Lohr S, Hall M, Faber K, Bommarius AS. 2011. Asymmetric bioreduction of alkenes using ene-reductases YersER and KYE1 and effects of organic solvents. Org Lett 13:2540-2543.
    • (2011) Org Lett , vol.13 , pp. 2540-2543
    • Yanto, Y.1    Winkler, C.K.2    Lohr, S.3    Hall, M.4    Faber, K.5    Bommarius, A.S.6


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