Site-selective chlorination of pyrrolic heterocycles by flavin dependent enzyme PrnC
Halogenation of pyrrole requires strong electrophilic reagents and often leads to undesired polyhalogenated products. Biocatalytic halogenation is a highly attractive approach given its chemoselectivity and benign reaction conditions. While there are several reports of enzymatic phenol and indole ha...
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Published in | Communications chemistry Vol. 7; no. 1; p. 7 |
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Main Authors | , , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
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Nature Publishing Group UK
05.01.2024
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Abstract | Halogenation of pyrrole requires strong electrophilic reagents and often leads to undesired polyhalogenated products. Biocatalytic halogenation is a highly attractive approach given its chemoselectivity and benign reaction conditions. While there are several reports of enzymatic phenol and indole halogenation in organic synthesis, corresponding reports on enzymatic pyrrole halogenation have been lacking. Here we describe the in vitro functional and structural characterization of PrnC, a flavin-dependent halogenase that can act on free-standing pyrroles. Computational modeling and site mutagenesis studies identified three key residues in the catalytic pocket. A moderate resolution map using single-particle cryogenic electron microscopy reveals PrnC to be a dimer. This native PrnC can halogenate a library of structurally diverse pyrrolic heterocycles in a site-selective manner and be applied in the chemoenzymatic synthesis of a chlorinated analog of the agrochemical fungicide Fludioxonil.
Pyrroles are an important scaffold in medicinal chemistry with various bioactivities; however, the selective chemical halogenation of pyrroles remains challenging. Here, the authors develop an enzymatic site-selective chlorination of pyrrolic heterocycles by a flavin-dependent halogenase PrnC and apply it to the chemoenzymatic synthesis of a chlorinated analogue of the fungicide Fludioxonil. |
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AbstractList | Halogenation of pyrrole requires strong electrophilic reagents and often leads to undesired polyhalogenated products. Biocatalytic halogenation is a highly attractive approach given its chemoselectivity and benign reaction conditions. While there are several reports of enzymatic phenol and indole halogenation in organic synthesis, corresponding reports on enzymatic pyrrole halogenation have been lacking. Here we describe the in vitro functional and structural characterization of PrnC, a flavin-dependent halogenase that can act on free-standing pyrroles. Computational modeling and site mutagenesis studies identified three key residues in the catalytic pocket. A moderate resolution map using single-particle cryogenic electron microscopy reveals PrnC to be a dimer. This native PrnC can halogenate a library of structurally diverse pyrrolic heterocycles in a site-selective manner and be applied in the chemoenzymatic synthesis of a chlorinated analog of the agrochemical fungicide Fludioxonil. Halogenation of pyrrole requires strong electrophilic reagents and often leads to undesired polyhalogenated products. Biocatalytic halogenation is a highly attractive approach given its chemoselectivity and benign reaction conditions. While there are several reports of enzymatic phenol and indole halogenation in organic synthesis, corresponding reports on enzymatic pyrrole halogenation have been lacking. Here we describe the in vitro functional and structural characterization of PrnC, a flavin-dependent halogenase that can act on free-standing pyrroles. Computational modeling and site mutagenesis studies identified three key residues in the catalytic pocket. A moderate resolution map using single-particle cryogenic electron microscopy reveals PrnC to be a dimer. This native PrnC can halogenate a library of structurally diverse pyrrolic heterocycles in a site-selective manner and be applied in the chemoenzymatic synthesis of a chlorinated analog of the agrochemical fungicide Fludioxonil. Pyrroles are an important scaffold in medicinal chemistry with various bioactivities; however, the selective chemical halogenation of pyrroles remains challenging. Here, the authors develop an enzymatic site-selective chlorination of pyrrolic heterocycles by a flavin-dependent halogenase PrnC and apply it to the chemoenzymatic synthesis of a chlorinated analogue of the fungicide Fludioxonil. Halogenation of pyrrole requires strong electrophilic reagents and often leads to undesired polyhalogenated products. Biocatalytic halogenation is a highly attractive approach given its chemoselectivity and benign reaction conditions. While there are several reports of enzymatic phenol and indole halogenation in organic synthesis, corresponding reports on enzymatic pyrrole halogenation have been lacking. Here we describe the in vitro functional and structural characterization of PrnC, a flavin-dependent halogenase that can act on free-standing pyrroles. Computational modeling and site mutagenesis studies identified three key residues in the catalytic pocket. A moderate resolution map using single-particle cryogenic electron microscopy reveals PrnC to be a dimer. This native PrnC can halogenate a library of structurally diverse pyrrolic heterocycles in a site-selective manner and be applied in the chemoenzymatic synthesis of a chlorinated analog of the agrochemical fungicide Fludioxonil.Pyrroles are an important scaffold in medicinal chemistry with various bioactivities; however, the selective chemical halogenation of pyrroles remains challenging. Here, the authors develop an enzymatic site-selective chlorination of pyrrolic heterocycles by a flavin-dependent halogenase PrnC and apply it to the chemoenzymatic synthesis of a chlorinated analogue of the fungicide Fludioxonil. Abstract Halogenation of pyrrole requires strong electrophilic reagents and often leads to undesired polyhalogenated products. Biocatalytic halogenation is a highly attractive approach given its chemoselectivity and benign reaction conditions. While there are several reports of enzymatic phenol and indole halogenation in organic synthesis, corresponding reports on enzymatic pyrrole halogenation have been lacking. Here we describe the in vitro functional and structural characterization of PrnC, a flavin-dependent halogenase that can act on free-standing pyrroles. Computational modeling and site mutagenesis studies identified three key residues in the catalytic pocket. A moderate resolution map using single-particle cryogenic electron microscopy reveals PrnC to be a dimer. This native PrnC can halogenate a library of structurally diverse pyrrolic heterocycles in a site-selective manner and be applied in the chemoenzymatic synthesis of a chlorinated analog of the agrochemical fungicide Fludioxonil. |
ArticleNumber | 7 |
Author | Tay, Terence Tan, Cheryl Jia Xin Wong, Fong Tian Peh, GuangRong Ang, Ee Lui Tan, Lee Ling Tan, Yong Zi Zhao, Huimin Wong, Joel Bi, Jiawu Lim, Yee Hwee Tiong, Elaine Goh, Yi Ling Lin, Fu Ye, Suming |
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Cites_doi | 10.1038/s41592-019-0396-9 10.1016/bs.mie.2016.03.024 10.1039/C4RA15710A 10.1002/cbic.202100210 10.1021/acs.chemrev.6b00571 10.1002/anie.201509573 10.1128/aem.63.6.2147-2154.1997 10.1016/j.ejmech.2011.01.031 10.1039/c0np00014k 10.1016/j.jsb.2005.07.007 10.1002/1615-4169(200108)343:6/7<591::AID-ADSC591>3.0.CO;2-E 10.1126/science.1151831 10.1021/acs.chemrev.7b00032 10.1080/00304948.2011.629553 10.1002/cbic.200800186 10.1007/s00253-018-09595-w 10.1039/D0QO01574A 10.1016/j.jmb.2009.06.008 10.1074/jbc.RA120.016004 10.1002/jobm.3620320312 10.1038/s41467-019-09215-9 10.1002/cctc.201901827 10.1002/1521-3773(20000703)39:13<2300::AID-ANIE2300>3.0.CO;2-I 10.1080/1061186X.2019.1703189 10.1016/B978-0-08-101033-4.00005-X 10.1002/anie.201706342 10.1002/jcc.20084 10.1038/nchembio.1564 10.1080/00021369.1964.10858275 10.1021/ja305670f 10.1016/S0960-894X(98)00526-5 10.1007/978-3-662-38441-1_32 10.1016/j.jsb.2013.11.002 10.1038/ncomms11873 10.2174/0929867054020864 10.1039/C9RA07399J 10.3390/catal9121030 10.1021/cr900356p 10.1146/annurev-biochem-062917-012042 10.1021/bi0621213 10.1038/nmeth.4169 10.1039/b822933n 10.1038/s41467-021-23503-3 10.1002/slct.202001344 10.1107/S2053230X22006586 10.1007/s11426-021-1018-0 10.1021/acscatal.6b02707 10.1016/j.cbpa.2018.01.002 10.1146/annurev-biochem-032620-110705 10.1038/s41929-022-00800-8 10.1039/C9OB00847K 10.1038/s41557-019-0349-z 10.1002/cctc.201301090 10.1021/acscentsci.9b00835 10.1073/pnas.0506964102 10.1039/D0CS01551B 10.1016/j.tet.2018.12.016 10.1126/science.1116510 10.1021/jacs.5b04525 10.1074/jbc.RA118.005393 10.1016/j.ejmech.2015.12.017 |
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References | SanaBEngineered RebH halogenase variants demonstrating a specificity switch from tryptophan towards novel indole compoundsChemBioChem202122279127981:CAS:528:DC%2BB3MXhs1yqtbfM34240527851885910.1002/cbic.202100210 HammerPEHillDSLamSTPéeKHVLigonJMFour genes from Pseudomonas fluorescens that encode the biosynthesis of pyrrolnitrinAppl. Environ. Microbiol.199763214721541:CAS:528:DyaK2sXjsFCnt7w%3D917233216850510.1128/aem.63.6.2147-2154.1997 KellerSPurification and partial characterization of tryptophan 7-halogenase (PrnA) from Pseudomonas fluorescensAngew. Chem. Int. Ed.200039230023021:CAS:528:DC%2BD3cXltlGkurY%3D10.1002/1521-3773(20000703)39:13<2300::AID-ANIE2300>3.0.CO;2-I MoriSPangAHThamban ChandrikaNGarneau-TsodikovaSTsodikovOVNat. Commun.20191030890712642497310.1038/s41467-019-09215-9 PettersenEFUCSF Chimera—A visualization system for exploratory research and analysisJ. computational Chem.200425160516121:CAS:528:DC%2BD2cXmvVOhsbs%3D10.1002/jcc.20084 HölzerMBurdWReißigH-UPéeK-HVAdv. Synth. Catal.200134359159510.1002/1615-4169(200108)343:6/7<591::AID-ADSC591>3.0.CO;2-E SantoRDPyrrolnitrin and related pyrroles endowed with antibacterial activities against Mycobacterium tuberculosisBioorg. Med. Chem. Lett.1998829312936987365010.1016/S0960-894X(98)00526-5 YehEBlasiakLCKoglinADrennanCLWalshCTChlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenasesBiochemistry200746128412921:CAS:528:DC%2BD2sXlsl2htg%3D%3D1726095710.1021/bi0621213 PunjaniARubinsteinJLFleetDJBrubakerMAcryoSPARC: algorithms for rapid unsupervised cryo-EM structure determinationNat. methods2017142902961:CAS:528:DC%2BC2sXitlGisbs%3D2816547310.1038/nmeth.4169 MastronardeDNAutomated electron microscope tomography using robust prediction of specimen movementsJ. Struct. Biol.200515236511618256310.1016/j.jsb.2005.07.007 MathiyazhaganADAnilkumarGRecent advances and applications of p-toluenesulfonylmethyl isocyanide (TosMIC)Org. Biomol. Chem.201917673567471:CAS:528:DC%2BC1MXhtF2gtbnK3125086210.1039/C9OB00847K GkotsiDSDhaliwalJMcLachlanMMWMulholandKRGossRJMHalogenases: powerful tools for biocatalysis (mechanisms applications and scope)Curr. Opin. Chem. Biol.2018431191261:CAS:528:DC%2BC1cXisVCgsLs%3D2941453010.1016/j.cbpa.2018.01.002 ZhouPMocekUSieselBFlossHGBiosynthesis of pyrrolnitrin. Incorporation of13C,15N double‐labelled D‐ and L‐tryptophanJ. Basic Microbiol.1992322092141:CAS:528:DyaK38XmsVygsLk%3D151271210.1002/jobm.3620320312 BüchlerJPapadopoulouABullerRRecent advances in flavin-dependent halogenase biocatalysis: sourcing, engineering, and applicationCatalysts20199103010.3390/catal9121030 MoritzerA-CStructure-based switch of regioselectivity in the flavin-dependent tryptophan 6-halogenase ThalJ. Biol. Chem.2019294252925421:CAS:528:DC%2BC1MXjtFGmtLk%3D3055928810.1074/jbc.RA118.005393 YoungISThorntonPDThompsonASynthesis of natural products containing the pyrrolic ringNat. Prod. Rep.201027180118391:CAS:528:DC%2BC3cXhsVagurfN2093622210.1039/c0np00014k HeideLUse of a halogenase of hormaomycin biosynthesis for formation of new clorobiocin analogues with 5-chloropyrrole moietiesChemBioChem20089199219991:CAS:528:DC%2BD1cXhtVegs7bN1865507610.1002/cbic.200800186 CroweCHalogenases: a palette of emerging opportunities for synthetic biology–synthetic chemistry and C–H functionalisationChem. Soc. Rev.202150944394811:CAS:528:DC%2BB3MXhslCjs7nE34368824840714210.1039/D0CS01551B AndorferMCUnderstanding flavin-dependent halogenase reactivity via substrate activity profilingACS Catal.20177189719041:CAS:528:DC%2BC2sXhvVyksbg%3D28989809562751610.1021/acscatal.6b02707 PrakineeKMechanism-guided tunnel engineering to increase the efficiency of a flavin-dependent halogenaseNat. Catal.202255345441:CAS:528:DC%2BB38XhsFCrsrzK10.1038/s41929-022-00800-8 AndorferMCLewisJCUnderstanding and improving the activity of flavin-dependent halogenases via random and targeted mutagenesisAnnu. Rev. Biochem.2018871591851:CAS:528:DC%2BC1cXmsVensr0%3D29589959601337410.1146/annurev-biochem-062917-012042 MondalDFisherBFJiangYLewisJCFlavin-dependent halogenases catalyze enantioselective olefin halocyclizationNat. Commun.2021121:CAS:528:DC%2BB3MXhsVOqsbjI34075034816966010.1038/s41467-021-23503-3 GkotsiDSA marine viral halogenase that iodinates diverse substratesNat. Chem.201911109110971:CAS:528:DC%2BC1MXhvFyhsr3N31611633687543010.1038/s41557-019-0349-z DorresteinPCYehEGarneau-TsodikovaSKelleherNLWalshCTDichlorination of a pyrrolyl-S-carrier protein by FADH2-dependent halogenase PltA during pyoluteorin biosynthesisProc. Natl Acad. Sci. USA200510213843138481:CAS:528:DC%2BD2MXhtVOqsbrF16162666123659210.1073/pnas.0506964102 YamanakaKRyanKSGulderTAMHughesCCMooreBSFlavoenzyme-catalyzed atropo-selective N,C-bipyrrole homocoupling in marinopyrrole biosynthesisJ. Am. Chem. Soc.201213412434124371:CAS:528:DC%2BC38XhtVemur%2FN22800473341571310.1021/ja305670f AgarwalVEnzymatic halogenation and dehalogenation reactions: pervasive and mechanistically diverseChem. Rev.2017117561956741:CAS:528:DC%2BC2sXht1Gisr0%3D28106994557588510.1021/acs.chemrev.6b00571 WynandsIvan PéeKHFEMS Microbiol. Lett.20042373633671:CAS:528:DC%2BD2cXmsVGiuro%3D15321684 GholapSSPyrrole: An emerging scaffold for construction of valuable therapeutic agentsEur. J. Med. Chem.201611013311:CAS:528:DC%2BC28Xhtl2nurc%3D2680754110.1016/j.ejmech.2015.12.017 in Organic Chemistry: A Series of Monographs, eds. R. A. Jones and G. P. Bean, Academic Press, 1977, vol. 34, pp. 115–207. MarrCRBenlekbirSRubinsteinJLFabrication of carbon films with ∼500 nm holes for cryo-EM with a direct detector deviceJ. Struct. Biol.201418542471:CAS:528:DC%2BC3sXitVShtrbE2426948410.1016/j.jsb.2013.11.002 ArimaKImanakaHKousakaMFukutaATamuraGPyrrolnitrin, a new antibiotic substance, produced by PseudomonasAgric. Biol. Chem.1964285755761:CAS:528:DyaF2MXhtVWgsQ%3D%3D10.1080/00021369.1964.10858275 FisherBFSnodgrassHMJonesKAAndorferMCLewisJCSite-selective C–H halogenation using flavin-dependent halogenases identified via family-wide activity profilingACS Cent. Sci.20195184418561:CAS:528:DC%2BC1MXitVSksL3L31807686689186610.1021/acscentsci.9b00835 ZhuXStructural insights into regioselectivity in the enzymatic chlorination of tryptophanJ. Mol. Biol.200939174851:CAS:528:DC%2BD1MXoslant7g%3D19501593271378110.1016/j.jmb.2009.06.008 BhardwajVGumberDAbbotVDhimanSSharmaPPyrrole: a resourceful small molecule in key medicinal hetero-aromaticsRSC Adv.2015515233152661:CAS:528:DC%2BC2MXhtlOks7o%3D10.1039/C4RA15710A MingesHTargeted enzyme engineering unveiled unexpected patterns of halogenase stabilizationChemCatChem2020128188311:CAS:528:DC%2BC1MXitlyhsr%2FL10.1002/cctc.201901827 HagfeldtABoschlooGSunLKlooLPetterssonHDye-sensitized solar cellsChem. Rev.2010110659566631:CAS:528:DC%2BC3cXhtFChs77M2083117710.1021/cr900356p ChuaEYDBetter, faster, cheaper: recent advances in cryo–electron microscopyAnnu. Rev. Biochem.2022911321:CAS:528:DC%2BB38XnvVOmurw%3D353206831039318910.1146/annurev-biochem-032620-110705 EliseenkoSSLiuFSwitchable pyrrole-based hydrogen bonding motif in enantioselective trifunctional organocatalysisTetrahedron2019755185261:CAS:528:DC%2BC1cXisFyms7bF10.1016/j.tet.2018.12.016 WeicholdVMilbredtDvan PéeK-HSpecific enzymatic halogenation—from the discovery of halogenated enzymes to their applications in vitro and in vivoAngew. Chem. Int. Ed.201655637463891:CAS:528:DC%2BC28XlvVagsbY%3D10.1002/anie.201509573 AgarwalVBiosynthesis of polybrominated aromatic organic compounds by marine bacteriaNat. Chem. Biol.2014106406471:CAS:528:DC%2BC2cXhtVKlsrbP24974229410413810.1038/nchembio.1564 VeisiHGhorbani-VagheiRZolfigolMARecent progress in the use ofN-halo compounds in organic synthesisOrg. Preparations Proced. Int.2011434895401:CAS:528:DC%2BC3MXhsVyksr3I10.1080/00304948.2011.629553 KuznietsovaHPyrrole derivatives as potential anti-cancer therapeutics: synthesis, mechanisms of action, safetyJ. Drug Target.2020285475631:CAS:528:DC%2BC1MXisVaqsbnL3181445610.1080/1061186X.2019.1703189 SchorbMHaberboschIHagenWJSchwabYMastronardeDNSoftware tools for automated transmission electron microscopyNat. methods2019164714771:CAS:528:DC%2BC1MXhtVSqs7zL31086343700023810.1038/s41592-019-0396-9 RatherIAWagaySAHasnainMSAliRNew dimensions in calix[4]pyrrole: the land of opportunity in supramolecular chemistryRSC Adv.2019938309383441:CAS:528:DC%2BC1MXit1SrtLvF35540221907602410.1039/C9RA07399J Singh, N. et al. Recent progress in the total synthesis of pyrrole-containing natural products (2011–2020). Organic Chemistry Frontiers 8, 5550–5573 (2021). LathamJIntegrated catalysis opens new arylation pathways via regiodivergent enzymatic C–H activationNat. Commun.2016727283121490640410.1038/ncomms11873 NguyenTKMKiMRSonRGPackSPThe NT11, a novel fusion tag for enhancing protein expression in Escherichia coliAppl. Microbiol. Biotechnol.2019103220522161:CAS:528:DC%2BC1MXlvVWktb0%3D3061029010.1007/s00253-018-09595-w MenonBRKRadH: a versatile halogenase for integration into synthetic pathwaysAngew. Chem. Int. Ed.20175611841118451:CAS:528:DC%2BC2sXhtlKhu7%2FF10.1002/anie.201706342 YinLCrystal structure determination of the halogenase CtcP from Streptomyces aureofaciensActa Crystallogr. Sect. F2022782702751:CAS:528:DC%2BB38Xhs12ls7jL10.1107/S2053230X22006586 ZhangYAryl C-H iodination: are there actual flavin-dependent iodinases in natureSci. China Chem.202164173017351:CAS:528:DC%2BB3MXhsVCltrzM10.1007/s11426-021-1018-0 HuffmanJWPadgettLWRecent developments in the medicinal chemistry of cannabimimetic indoles, pyrroles and indenesCurr. Med. Chem.200512139514111:CAS:528:DC%2BD2MXkvF2qt78%3D1597499110.2174/0929867054020864 Ji Ram, V., Sethi, A., Nath, M. & Pratap, R. in The Chemistry of Heterocycles, eds. V. Ji Ram, A. Sethi, M. Nath and R. Pratap, Elsevier, 2019, https://doi.org/10.1016/B978-0-08-101033-4.00005-X, pp. 149–478. PhinthaADissecting the low catalytic capability of flavin-dependent halogenasesJ. Biol. Chem.20212961000681:CAS:528:DC%2BB3MXjtlCltr0%3D3346570810.1074/jbc.RA120.016004 KumarKTosMIC: a powerful synthon for cyclization and sulfonylation J Latham (1083_CR17) 2018; 118 MC Andorfer (1083_CR21) 2018; 87 S Keller (1083_CR42) 2000; 39 1083_CR12 MJ Jaremko (1083_CR36) 2015; 137 1083_CR15 M Hölzer (1083_CR41) 2001; 343 K Kumar (1083_CR57) 2020; 5 J Büchler (1083_CR23) 2019; 9 MC Andorfer (1083_CR31) 2017; 7 EYD Chua (1083_CR52) 2022; 91 A Punjani (1083_CR61) 2017; 14 BRK Menon (1083_CR28) 2017; 56 A-C Moritzer (1083_CR54) 2019; 294 P Zhou (1083_CR40) 1992; 32 DS Gkotsi (1083_CR16) 2018; 43 JT Payne (1083_CR22) 2016; 575 I Wynands (1083_CR29) 2004; 237 PE Hammer (1083_CR30) 1997; 63 A Hagfeldt (1083_CR8) 2010; 110 V Agarwal (1083_CR18) 2017; 117 K Prakinee (1083_CR47) 2022; 5 CR Marr (1083_CR58) 2014; 185 M Schorb (1083_CR60) 2019; 16 A Phintha (1083_CR44) 2021; 296 K Arima (1083_CR38) 1964; 28 H Minges (1083_CR55) 2020; 12 H Kuznietsova (1083_CR7) 2020; 28 E Yeh (1083_CR49) 2007; 46 C Ayats (1083_CR63) 2009; 7 V Weichold (1083_CR19) 2016; 55 J Latham (1083_CR26) 2016; 7 X Zhu (1083_CR53) 2009; 391 V Agarwal (1083_CR33) 2014; 10 JW Huffman (1083_CR4) 2005; 12 Y Zhang (1083_CR45) 2021; 64 1083_CR39 DN Mastronarde (1083_CR59) 2005; 152 L Heide (1083_CR34) 2008; 9 BF Fisher (1083_CR32) 2019; 5 SS Eliseenko (1083_CR11) 2019; 75 H Veisi (1083_CR14) 2011; 43 B Sana (1083_CR27) 2021; 22 EF Pettersen (1083_CR62) 2004; 25 S Mori (1083_CR25) 2019; 10 SS Gholap (1083_CR3) 2016; 110 RD Santo (1083_CR6) 1998; 8 M Frese (1083_CR48) 2014; 6 K Yamanaka (1083_CR35) 2012; 134 DS Gkotsi (1083_CR24) 2019; 11 IS Young (1083_CR13) 2010; 27 C Crowe (1083_CR20) 2021; 50 H Nishide (1083_CR9) 2008; 319 IA Rather (1083_CR10) 2019; 9 PC Dorrestein (1083_CR37) 2005; 102 M-Z Wang (1083_CR5) 2011; 46 D Mondal (1083_CR46) 2021; 12 1083_CR1 TKM Nguyen (1083_CR43) 2019; 103 C Dong (1083_CR50) 2005; 309 AD Mathiyazhagan (1083_CR56) 2019; 17 L Yin (1083_CR51) 2022; 78 V Bhardwaj (1083_CR2) 2015; 5 |
References_xml | – volume: 16 start-page: 471 year: 2019 ident: 1083_CR60 publication-title: Nat. methods doi: 10.1038/s41592-019-0396-9 contributor: fullname: M Schorb – volume: 575 start-page: 93 year: 2016 ident: 1083_CR22 publication-title: Methods Enzymol. doi: 10.1016/bs.mie.2016.03.024 contributor: fullname: JT Payne – volume: 5 start-page: 15233 year: 2015 ident: 1083_CR2 publication-title: RSC Adv. doi: 10.1039/C4RA15710A contributor: fullname: V Bhardwaj – volume: 22 start-page: 2791 year: 2021 ident: 1083_CR27 publication-title: ChemBioChem doi: 10.1002/cbic.202100210 contributor: fullname: B Sana – volume: 117 start-page: 5619 year: 2017 ident: 1083_CR18 publication-title: Chem. Rev. doi: 10.1021/acs.chemrev.6b00571 contributor: fullname: V Agarwal – volume: 55 start-page: 6374 year: 2016 ident: 1083_CR19 publication-title: Angew. Chem. Int. Ed. doi: 10.1002/anie.201509573 contributor: fullname: V Weichold – volume: 63 start-page: 2147 year: 1997 ident: 1083_CR30 publication-title: Appl. Environ. Microbiol. doi: 10.1128/aem.63.6.2147-2154.1997 contributor: fullname: PE Hammer – volume: 46 start-page: 1463 year: 2011 ident: 1083_CR5 publication-title: Eur. J. Med. Chem. doi: 10.1016/j.ejmech.2011.01.031 contributor: fullname: M-Z Wang – volume: 27 start-page: 1801 year: 2010 ident: 1083_CR13 publication-title: Nat. Prod. Rep. doi: 10.1039/c0np00014k contributor: fullname: IS Young – volume: 152 start-page: 36 year: 2005 ident: 1083_CR59 publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2005.07.007 contributor: fullname: DN Mastronarde – volume: 343 start-page: 591 year: 2001 ident: 1083_CR41 publication-title: Adv. Synth. Catal. doi: 10.1002/1615-4169(200108)343:6/7<591::AID-ADSC591>3.0.CO;2-E contributor: fullname: M Hölzer – volume: 319 start-page: 737 year: 2008 ident: 1083_CR9 publication-title: Science doi: 10.1126/science.1151831 contributor: fullname: H Nishide – volume: 118 start-page: 232 year: 2018 ident: 1083_CR17 publication-title: Chem. Rev. doi: 10.1021/acs.chemrev.7b00032 contributor: fullname: J Latham – volume: 43 start-page: 489 year: 2011 ident: 1083_CR14 publication-title: Org. Preparations Proced. Int. doi: 10.1080/00304948.2011.629553 contributor: fullname: H Veisi – volume: 9 start-page: 1992 year: 2008 ident: 1083_CR34 publication-title: ChemBioChem doi: 10.1002/cbic.200800186 contributor: fullname: L Heide – volume: 103 start-page: 2205 year: 2019 ident: 1083_CR43 publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-018-09595-w contributor: fullname: TKM Nguyen – ident: 1083_CR1 doi: 10.1039/D0QO01574A – volume: 391 start-page: 74 year: 2009 ident: 1083_CR53 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2009.06.008 contributor: fullname: X Zhu – volume: 296 start-page: 100068 year: 2021 ident: 1083_CR44 publication-title: J. Biol. Chem. doi: 10.1074/jbc.RA120.016004 contributor: fullname: A Phintha – volume: 32 start-page: 209 year: 1992 ident: 1083_CR40 publication-title: J. Basic Microbiol. doi: 10.1002/jobm.3620320312 contributor: fullname: P Zhou – volume: 10 year: 2019 ident: 1083_CR25 publication-title: Nat. Commun. doi: 10.1038/s41467-019-09215-9 contributor: fullname: S Mori – volume: 12 start-page: 818 year: 2020 ident: 1083_CR55 publication-title: ChemCatChem doi: 10.1002/cctc.201901827 contributor: fullname: H Minges – volume: 39 start-page: 2300 year: 2000 ident: 1083_CR42 publication-title: Angew. Chem. Int. Ed. doi: 10.1002/1521-3773(20000703)39:13<2300::AID-ANIE2300>3.0.CO;2-I contributor: fullname: S Keller – volume: 28 start-page: 547 year: 2020 ident: 1083_CR7 publication-title: J. Drug Target. doi: 10.1080/1061186X.2019.1703189 contributor: fullname: H Kuznietsova – ident: 1083_CR12 doi: 10.1016/B978-0-08-101033-4.00005-X – volume: 56 start-page: 11841 year: 2017 ident: 1083_CR28 publication-title: Angew. Chem. Int. Ed. doi: 10.1002/anie.201706342 contributor: fullname: BRK Menon – volume: 25 start-page: 1605 year: 2004 ident: 1083_CR62 publication-title: J. computational Chem. doi: 10.1002/jcc.20084 contributor: fullname: EF Pettersen – volume: 10 start-page: 640 year: 2014 ident: 1083_CR33 publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.1564 contributor: fullname: V Agarwal – volume: 28 start-page: 575 year: 1964 ident: 1083_CR38 publication-title: Agric. Biol. Chem. doi: 10.1080/00021369.1964.10858275 contributor: fullname: K Arima – volume: 134 start-page: 12434 year: 2012 ident: 1083_CR35 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja305670f contributor: fullname: K Yamanaka – volume: 8 start-page: 2931 year: 1998 ident: 1083_CR6 publication-title: Bioorg. Med. Chem. Lett. doi: 10.1016/S0960-894X(98)00526-5 contributor: fullname: RD Santo – ident: 1083_CR39 doi: 10.1007/978-3-662-38441-1_32 – volume: 185 start-page: 42 year: 2014 ident: 1083_CR58 publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2013.11.002 contributor: fullname: CR Marr – volume: 7 year: 2016 ident: 1083_CR26 publication-title: Nat. Commun. doi: 10.1038/ncomms11873 contributor: fullname: J Latham – volume: 12 start-page: 1395 year: 2005 ident: 1083_CR4 publication-title: Curr. Med. Chem. doi: 10.2174/0929867054020864 contributor: fullname: JW Huffman – volume: 9 start-page: 38309 year: 2019 ident: 1083_CR10 publication-title: RSC Adv. doi: 10.1039/C9RA07399J contributor: fullname: IA Rather – volume: 9 start-page: 1030 year: 2019 ident: 1083_CR23 publication-title: Catalysts doi: 10.3390/catal9121030 contributor: fullname: J Büchler – volume: 110 start-page: 6595 year: 2010 ident: 1083_CR8 publication-title: Chem. Rev. doi: 10.1021/cr900356p contributor: fullname: A Hagfeldt – volume: 87 start-page: 159 year: 2018 ident: 1083_CR21 publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-062917-012042 contributor: fullname: MC Andorfer – volume: 46 start-page: 1284 year: 2007 ident: 1083_CR49 publication-title: Biochemistry doi: 10.1021/bi0621213 contributor: fullname: E Yeh – volume: 14 start-page: 290 year: 2017 ident: 1083_CR61 publication-title: Nat. methods doi: 10.1038/nmeth.4169 contributor: fullname: A Punjani – volume: 7 start-page: 860 year: 2009 ident: 1083_CR63 publication-title: Org. Biomol. Chem. doi: 10.1039/b822933n contributor: fullname: C Ayats – volume: 12 year: 2021 ident: 1083_CR46 publication-title: Nat. Commun. doi: 10.1038/s41467-021-23503-3 contributor: fullname: D Mondal – volume: 237 start-page: 363 year: 2004 ident: 1083_CR29 publication-title: FEMS Microbiol. Lett. contributor: fullname: I Wynands – volume: 5 start-page: 10298 year: 2020 ident: 1083_CR57 publication-title: ChemistrySelect doi: 10.1002/slct.202001344 contributor: fullname: K Kumar – volume: 78 start-page: 270 year: 2022 ident: 1083_CR51 publication-title: Acta Crystallogr. Sect. F doi: 10.1107/S2053230X22006586 contributor: fullname: L Yin – volume: 64 start-page: 1730 year: 2021 ident: 1083_CR45 publication-title: Sci. China Chem. doi: 10.1007/s11426-021-1018-0 contributor: fullname: Y Zhang – volume: 7 start-page: 1897 year: 2017 ident: 1083_CR31 publication-title: ACS Catal. doi: 10.1021/acscatal.6b02707 contributor: fullname: MC Andorfer – volume: 43 start-page: 119 year: 2018 ident: 1083_CR16 publication-title: Curr. Opin. Chem. Biol. doi: 10.1016/j.cbpa.2018.01.002 contributor: fullname: DS Gkotsi – volume: 91 start-page: 1 year: 2022 ident: 1083_CR52 publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev-biochem-032620-110705 contributor: fullname: EYD Chua – volume: 5 start-page: 534 year: 2022 ident: 1083_CR47 publication-title: Nat. Catal. doi: 10.1038/s41929-022-00800-8 contributor: fullname: K Prakinee – volume: 17 start-page: 6735 year: 2019 ident: 1083_CR56 publication-title: Org. Biomol. Chem. doi: 10.1039/C9OB00847K contributor: fullname: AD Mathiyazhagan – volume: 11 start-page: 1091 year: 2019 ident: 1083_CR24 publication-title: Nat. Chem. doi: 10.1038/s41557-019-0349-z contributor: fullname: DS Gkotsi – volume: 6 start-page: 1270 year: 2014 ident: 1083_CR48 publication-title: ChemCatChem doi: 10.1002/cctc.201301090 contributor: fullname: M Frese – volume: 5 start-page: 1844 year: 2019 ident: 1083_CR32 publication-title: ACS Cent. Sci. doi: 10.1021/acscentsci.9b00835 contributor: fullname: BF Fisher – volume: 102 start-page: 13843 year: 2005 ident: 1083_CR37 publication-title: Proc. Natl Acad. Sci. USA doi: 10.1073/pnas.0506964102 contributor: fullname: PC Dorrestein – volume: 50 start-page: 9443 year: 2021 ident: 1083_CR20 publication-title: Chem. Soc. Rev. doi: 10.1039/D0CS01551B contributor: fullname: C Crowe – volume: 75 start-page: 518 year: 2019 ident: 1083_CR11 publication-title: Tetrahedron doi: 10.1016/j.tet.2018.12.016 contributor: fullname: SS Eliseenko – volume: 309 start-page: 2216 year: 2005 ident: 1083_CR50 publication-title: Science doi: 10.1126/science.1116510 contributor: fullname: C Dong – volume: 137 start-page: 11546 year: 2015 ident: 1083_CR36 publication-title: J. Am. Chem. Soc. doi: 10.1021/jacs.5b04525 contributor: fullname: MJ Jaremko – volume: 294 start-page: 2529 year: 2019 ident: 1083_CR54 publication-title: J. Biol. Chem. doi: 10.1074/jbc.RA118.005393 contributor: fullname: A-C Moritzer – ident: 1083_CR15 – volume: 110 start-page: 13 year: 2016 ident: 1083_CR3 publication-title: Eur. J. Med. Chem. doi: 10.1016/j.ejmech.2015.12.017 contributor: fullname: SS Gholap |
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Snippet | Halogenation of pyrrole requires strong electrophilic reagents and often leads to undesired polyhalogenated products. Biocatalytic halogenation is a highly... Abstract Halogenation of pyrrole requires strong electrophilic reagents and often leads to undesired polyhalogenated products. Biocatalytic halogenation is a... |
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Title | Site-selective chlorination of pyrrolic heterocycles by flavin dependent enzyme PrnC |
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