메뉴 건너뛰기




Volumn 2, Issue NOV, 2014, Pages

Insights into enzymatic halogenation from computational studies

Author keywords

Ab initio methods; DFT; Enzymes; Molecular modeling; QM MM; Reaction mechanisms

Indexed keywords


EID: 84986895140     PISSN: None     EISSN: 22962646     Source Type: Journal    
DOI: 10.3389/fchem.2014.00098     Document Type: Review
Times cited : (21)

References (98)
  • 1
    • 33745934456 scopus 로고    scopus 로고
    • Molecular mechanisms of enzyme-catalysed halogenation
    • Anderson, J. L. R., and Chapman, S. K. (2006). Molecular mechanisms of enzyme-catalysed halogenation. Mol. Biosyst. 2, 350-357. doi: 10.1039/b607813c
    • (2006) Mol. Biosyst , vol.2 , pp. 350-357
    • Anderson, J.L.R.1    Chapman, S.K.2
  • 2
    • 9244227570 scopus 로고    scopus 로고
    • Quantum chemical studies of dioxygen activation by mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad
    • Bassan, A., Borowski, T., and Siegbahn, P. E. M. (2004). Quantum chemical studies of dioxygen activation by mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad. Dalton Trans. 3153-3162. doi: 10.1039/b408340g
    • (2004) Dalton Trans , pp. 3153-3162
    • Bassan, A.1    Borowski, T.2    Siegbahn, P.E.M.3
  • 3
    • 61849174140 scopus 로고    scopus 로고
    • Structural perspective on enzymatic halogenation
    • Blasiak, L. C., and Drennan, C. L. (2008). Structural perspective on enzymatic halogenation. Acc. Chem. Res. 42, 147-155. doi: 10.1021/ar800088r
    • (2008) Acc. Chem. Res , vol.42 , pp. 147-155
    • Blasiak, L.C.1    Drennan, C.L.2
  • 4
    • 33645017788 scopus 로고    scopus 로고
    • Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis
    • Blasiak, L. C., Vaillancourt, F. H., Walsh, C. T., and Drennan, C. L. (2006). Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis. Nature 440, 368-371. doi: 10.1038/nature04544
    • (2006) Nature , vol.440 , pp. 368-371
    • Blasiak, L.C.1    Vaillancourt, F.H.2    Walsh, C.T.3    Drennan, C.L.4
  • 5
    • 84898005451 scopus 로고    scopus 로고
    • Quantum chemical studies of mechanisms for metalloenzymes
    • Blomberg, M. R., Borowski, T., Himo, F., Liao, R.-Z., and Siegbahn, P. E. M. (2014). Quantum chemical studies of mechanisms for metalloenzymes. Chem. Rev. 114, 3601-3658. doi: 10.1021/cr400388t
    • (2014) Chem. Rev , vol.114 , pp. 3601-3658
    • Blomberg, M.R.1    Borowski, T.2    Himo, F.3    Liao, R.-Z.4    Siegbahn, P.E.M.5
  • 7
    • 4644341669 scopus 로고    scopus 로고
    • 4-Hydroxyphenylpyruvate dioxygenase: a hybrid density functional study of the catalytic reaction mechanism
    • Borowski, T., Bassan, A., and Siegbahn, P. E. M. (2004a). 4-Hydroxyphenylpyruvate dioxygenase: a hybrid density functional study of the catalytic reaction mechanism. Biochemistry 43, 12331-12342. doi: 10.1021/bi049503y
    • (2004) Biochemistry , vol.43 , pp. 12331-12342
    • Borowski, T.1    Bassan, A.2    Siegbahn, P.E.M.3
  • 8
    • 1542289159 scopus 로고    scopus 로고
    • Mechanism of dioxygen activation in 2-oxoglutarate-dependent enzymes: a hybrid DFT study
    • Borowski, T., Bassan, A., and Siegbahn, P. E. M. (2004b). Mechanism of dioxygen activation in 2-oxoglutarate-dependent enzymes: a hybrid DFT study. Chem. Eur. J. 10, 1031-1041. doi: 10.1002/chem.200305306
    • (2004) Chem. Eur. J , vol.10 , pp. 1031-1041
    • Borowski, T.1    Bassan, A.2    Siegbahn, P.E.M.3
  • 9
    • 77956638724 scopus 로고    scopus 로고
    • Mechanism of selective halogenation by SyrB2: a computational study
    • Borowski, T., Noack, H., Radoñ, M., Zych, K., and Siegbahn, P. E. M. (2010). Mechanism of selective halogenation by SyrB2: a computational study. J. Am. Chem. Soc. 132, 12887-12898. doi: 10.1021/ja101877a
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 12887-12898
    • Borowski, T.1    Noack, H.2    Radoñ, M.3    Zych, K.4    Siegbahn, P.E.M.5
  • 10
    • 58149087852 scopus 로고    scopus 로고
    • Structure and action of the myxobacterial chondrochloren halogenase CndH: a new variant of FAD-dependent halogenases
    • Buedenbender, S., Rachid, S., Müller, R., and Schulz, G. E. (2009). Structure and action of the myxobacterial chondrochloren halogenase CndH: a new variant of FAD-dependent halogenases. J. Mol. Biol. 385, 520-530. doi: 10.1016/j.jmb.2008.10.057
    • (2009) J. Mol. Biol , vol.385 , pp. 520-530
    • Buedenbender, S.1    Rachid, S.2    Müller, R.3    Schulz, G.E.4
  • 11
    • 68949117491 scopus 로고    scopus 로고
    • Mechanistic considerations of halogenating enzymes
    • Butler, A., and Sandy, M. (2009). Mechanistic considerations of halogenating enzymes. Nature 460, 848-854. doi: 10.1038/nature08303
    • (2009) Nature , vol.460 , pp. 848-854
    • Butler, A.1    Sandy, M.2
  • 12
    • 49649112644 scopus 로고    scopus 로고
    • Quantum mechanical/molecular mechanical study on the mechanisms of Compound I formation in the catalytic cycle of chloroperoxidase: an overview on heme enzymes
    • Chen, H., Hirao, H., Derat, E., Schlichting, I., and Shaik, S. (2008). Quantum mechanical/molecular mechanical study on the mechanisms of Compound I formation in the catalytic cycle of chloroperoxidase: an overview on heme enzymes. J. Phys. Chem. B 112, 9490-9500. doi: 10.1021/jp803010f
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9490-9500
    • Chen, H.1    Hirao, H.2    Derat, E.3    Schlichting, I.4    Shaik, S.5
  • 13
    • 77952713408 scopus 로고    scopus 로고
    • Exchange-enhanced H-abstraction reactivity of high-valent nonheme iron(IV)-oxo from coupled cluster and density functional theories
    • Chen, H., Lai, W., and Shaik, S. (2010a). Exchange-enhanced H-abstraction reactivity of high-valent nonheme iron(IV)-oxo from coupled cluster and density functional theories. J. Phys. Chem. Lett. 1, 1533-1540. doi: 10.1038/nchem.943
    • (2010) J. Phys. Chem. Lett , vol.1 , pp. 1533-1540
    • Chen, H.1    Lai, W.2    Shaik, S.3
  • 14
    • 80053972832 scopus 로고    scopus 로고
    • Perferryl FeV-oxo nonheme complexes: do they have high-spin or low-spin ground states?
    • Chen, H., Lai, W., Yao, J., and Shaik, S. (2011). Perferryl FeV-oxo nonheme complexes: do they have high-spin or low-spin ground states? J. Chem. Theory Comput. 7, 3049-3053. doi: 10.1021/ct200614g
    • (2011) J. Chem. Theory Comput , vol.7 , pp. 3049-3053
    • Chen, H.1    Lai, W.2    Yao, J.3    Shaik, S.4
  • 15
    • 77950107585 scopus 로고    scopus 로고
    • Multiple low-lying states for compound I of P450cam and chloroperoxidase revealed from multireference ab initio QM/MM calculations
    • Chen, H., Song, J., Lai, W., Wu, W., and Shaik, S. (2010b). Multiple low-lying states for compound I of P450cam and chloroperoxidase revealed from multireference ab initio QM/MM calculations. J. Chem. Theory Comput. 6, 940-953. doi: 10.1021/ct9006234
    • (2010) J. Chem. Theory Comput , vol.6 , pp. 940-953
    • Chen, H.1    Song, J.2    Lai, W.3    Wu, W.4    Shaik, S.5
  • 16
    • 84857095543 scopus 로고    scopus 로고
    • The ONIOM method: its foundation and applications to metalloenzymes and photobiology
    • Chung, L. W., Hirao, H., Li, X., and Morokuma, K. (2012). The ONIOM method: its foundation and applications to metalloenzymes and photobiology. Wiley Interdiscip. Rev. Comput. Mol. Sci. 2, 327-350. doi: 10.1002/wcms.85
    • (2012) Wiley Interdiscip. Rev. Comput. Mol. Sci , vol.2 , pp. 327-350
    • Chung, L.W.1    Hirao, H.2    Li, X.3    Morokuma, K.4
  • 17
    • 49149103497 scopus 로고    scopus 로고
    • S-Adenosyl-L-methionine:hydroxide adenosyltransferase: a SAM enzyme
    • Deng, H., Botting, C. H., Hamilton, J. T. G., Russell, R. J. M., and O'Hagan, D. (2008a). S-Adenosyl-L-methionine:hydroxide adenosyltransferase: a SAM enzyme. Angew. Chem. Int. Ed. 47, 5357-5361. doi: 10.1002/anie.200800794
    • (2008) Angew. Chem. Int. Ed , vol.47 , pp. 5357-5361
    • Deng, H.1    Botting, C.H.2    Hamilton, J.T.G.3    Russell, R.J.M.4    O'Hagan, D.5
  • 19
    • 57749204574 scopus 로고    scopus 로고
    • In vitro reconstituted biotransformation of 4-fluorothreonine from fluoride ion: application of the fluorinase
    • Deng, H., Cross, S. M., McGlinchey, R. P., Hamilton, J. T. G., and O'Hagan, D. (2008b). In vitro reconstituted biotransformation of 4-fluorothreonine from fluoride ion: application of the fluorinase. Chem. Biol. 15, 1268-1276. doi: 10.1016/j.chembiol.2008.10.012
    • (2008) Chem. Biol , vol.15 , pp. 1268-1276
    • Deng, H.1    Cross, S.M.2    McGlinchey, R.P.3    Hamilton, J.T.G.4    O'Hagan, D.5
  • 20
    • 53849101806 scopus 로고    scopus 로고
    • The fluorinase, the chlorinase and the duf-62 enzymes
    • Deng, H., and O'Hagan, D. (2008). The fluorinase, the chlorinase and the duf-62 enzymes. Curr. Opin. Chem. Biol. 12, 582-592. doi: 10.1016/j.cbpa.2008.06.036
    • (2008) Curr. Opin. Chem. Biol , vol.12 , pp. 582-592
    • Deng, H.1    O'Hagan, D.2
  • 21
    • 33845798811 scopus 로고    scopus 로고
    • Can the peroxosuccinate complex in the catalytic cycle of taurine/a-ketoglutarate dioxygenase (TauD) act as an alternative oxidant?
    • de Visser, S. P. (2007). Can the peroxosuccinate complex in the catalytic cycle of taurine/a-ketoglutarate dioxygenase (TauD) act as an alternative oxidant? Chem. Commun. 171-173. doi: 10.1039/b611273k
    • (2007) Chem. Commun , pp. 171-173
    • de Visser, S.P.1
  • 22
    • 61749086210 scopus 로고    scopus 로고
    • Carbon dioxide: a waste product in the catalytic cycle of α-ketoglutarate dependent halogenases prevents the formation of hydroxylated by-products
    • de Visser, S. P., and Latifi, R. (2009). Carbon dioxide: a waste product in the catalytic cycle of α-ketoglutarate dependent halogenases prevents the formation of hydroxylated by-products. J. Phys. Chem. B 113, 12-14. doi: 10.1021/jp8097632
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12-14
    • de Visser, S.P.1    Latifi, R.2
  • 23
    • 80755126617 scopus 로고    scopus 로고
    • Activation of α-keto acid-dependent dioxygenases: application of an (FeNO)7/(FeO2)8 methodology for characterizing the initial steps of O2 activation
    • Diebold, A. R., Brown-Marshall, C. D., Neidig, M. L., Brownlee, J. M., Moran, G. R., and Solomon, E. I. (2011). Activation of α-keto acid-dependent dioxygenases: application of an (FeNO)7/(FeO2)8 methodology for characterizing the initial steps of O2 activation. J. Am. Chem. Soc. 133, 18148-18160. doi: 10.1021/ja202549q
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 18148-18160
    • Diebold, A.R.1    Brown-Marshall, C.D.2    Neidig, M.L.3    Brownlee, J.M.4    Moran, G.R.5    Solomon, E.I.6
  • 24
    • 1142310932 scopus 로고    scopus 로고
    • Crystal structure and mechanism of a bacterial fluorinating enzyme
    • Dong, C., Huang, F., Deng, H., Schaffrath, C., Spencer, J. B., O'Hagan, D., et al. (2004). Crystal structure and mechanism of a bacterial fluorinating enzyme. Nature 427, 561-565. doi: 10.1038/nature02280
    • (2004) Nature , vol.427 , pp. 561-565
    • Dong, C.1    Huang, F.2    Deng, H.3    Schaffrath, C.4    Spencer, J.B.5    O'Hagan, D.6
  • 25
    • 25844517049 scopus 로고    scopus 로고
    • Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for regioselective chlorination
    • Dong, C. J., Flecks, S., Unversucht, S., Haupt, C., van Pée, K.-H., and Naismith, J. H. (2005). Tryptophan 7-halogenase (PrnA) structure suggests a mechanism for regioselective chlorination. Science 309, 2216-2219. doi: 10.1126/science.1116510
    • (2005) Science , vol.309 , pp. 2216-2219
    • Dong, C.J.1    Flecks, S.2    Unversucht, S.3    Haupt, C.4    van Pée, K.-H.5    Naismith, J.H.6
  • 26
    • 54349111895 scopus 로고    scopus 로고
    • S-Adenosyl-L-methionine hydrolase (adenosine-forming), a conserved bacterial and archaeal protein related to SAM-dependent halogenases
    • Eustáquio, A. S., Härle, J., Noel, J. P., and Moore, B. S. (2008a). S-Adenosyl-L-methionine hydrolase (adenosine-forming), a conserved bacterial and archaeal protein related to SAM-dependent halogenases. ChemBioChem 9, 2215-2219. doi: 10.1002/cbic.200800341
    • (2008) ChemBioChem , vol.9 , pp. 2215-2219
    • Eustáquio, A.S.1    Härle, J.2    Noel, J.P.3    Moore, B.S.4
  • 27
    • 77950455094 scopus 로고    scopus 로고
    • Engineering fluorometabolite production: fluorinase expression in Salinispora tropica yields fluorosalinosporamide
    • Eustáquio, A. S., O'Hagan, D., and Moore, B. S. (2010). Engineering fluorometabolite production: fluorinase expression in Salinispora tropica yields fluorosalinosporamide. J. Nat. Prod. 73, 378-382. doi: 10.1021/np900719u
    • (2010) J. Nat. Prod , vol.73 , pp. 378-382
    • Eustáquio, A.S.1    O'Hagan, D.2    Moore, B.S.3
  • 28
    • 37249024344 scopus 로고    scopus 로고
    • Discovery and characterization of a marine bacterial SAM-dependent chlorinase
    • Eustáquio, A. S., Pojer, F., Noel, J. P., and Moore, B. S. (2008b). Discovery and characterization of a marine bacterial SAM-dependent chlorinase. Nature Chem. Biol. 4, 69-74. doi: 10.1038/nchembio.2007.56
    • (2008) Nature Chem. Biol , vol.4 , pp. 69-74
    • Eustáquio, A.S.1    Pojer, F.2    Noel, J.P.3    Moore, B.S.4
  • 29
    • 84878368825 scopus 로고    scopus 로고
    • Ab initio QM/MM calculations show an intersystem crossing in the hydrogen abstraction step in dealkylation catalyzed by AlkB
    • Fang, D., Lord, R. L., and Cisneros, G. A. (2013). Ab initio QM/MM calculations show an intersystem crossing in the hydrogen abstraction step in dealkylation catalyzed by AlkB. J. Phys. Chem. B 117, 6410-6420. doi: 10.1021/jp403116e
    • (2013) J. Phys. Chem. B , vol.117 , pp. 6410-6420
    • Fang, D.1    Lord, R.L.2    Cisneros, G.A.3
  • 30
    • 84870062977 scopus 로고    scopus 로고
    • Insight into the structure-function relationship of the nonheme iron halogenases involved in the biosynthesis of 4-chlorothreonine-Thr3 from Streptomyces sp. OH-5093 and SyrB2 from Pseudomonas syringae pv. syringae B301DR
    • Fullone, M. R., Paiardini, A., Miele, R., Marsango, S., Gross, D. C., Omura, S., et al. (2012). Insight into the structure-function relationship of the nonheme iron halogenases involved in the biosynthesis of 4-chlorothreonine-Thr3 from Streptomyces sp. OH-5093 and SyrB2 from Pseudomonas syringae pv. syringae B301DR. FEBS J. 279, 4269-4282. doi: 10.1111/febs.12017
    • (2012) FEBS J , vol.279 , pp. 4269-4282
    • Fullone, M.R.1    Paiardini, A.2    Miele, R.3    Marsango, S.4    Gross, D.C.5    Omura, S.6
  • 31
    • 33846379972 scopus 로고    scopus 로고
    • Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3
    • Galonic, D. P., Barr, E. W., Walsh, C. T., Bollinger, J. M. Jr., and Krebs, C. (2007). Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3. Nature Chem. Biol. 3, 113-116. doi: 10.1038/nchembio856
    • (2007) Nature Chem. Biol , vol.3 , pp. 113-116
    • Galonic, D.P.1    Barr, E.W.2    Walsh, C.T.3    Bollinger, J.M.4    Krebs, C.5
  • 32
    • 35348834136 scopus 로고    scopus 로고
    • What's new in enzymatic halogenations
    • Galonic Fujimori, D., and Walsh, C. T. (2007). What's new in enzymatic halogenations. Curr. Opin. Chem. Biol. 11, 553-560. doi: 10.1016/j.cbpa.2007.08.002
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 553-560
    • Galonic Fujimori, D.1    Walsh, C.T.2
  • 33
    • 65249156054 scopus 로고    scopus 로고
    • 51V NMR chemical shifts calculated from QM/MM models of peroxo forms of vanadium haloperoxidases
    • Geethalakshmi, K. R., Waller, M. P., Thiel, W., and Bühl, M. (2009). 51V NMR chemical shifts calculated from QM/MM models of peroxo forms of vanadium haloperoxidases. J. Phys. Chem. B 113, 4456-4465. doi: 10.1021/jp8109308
    • (2009) J. Phys. Chem. B , vol.113 , pp. 4456-4465
    • Geethalakshmi, K.R.1    Waller, M.P.2    Thiel, W.3    Bühl, M.4
  • 34
    • 77955331651 scopus 로고    scopus 로고
    • Analysis of reaction channels for alkane hydroxylation by nonheme iron(IV)-oxo complexes
    • Geng, C., Ye, S., and Neese, F. (2010). Analysis of reaction channels for alkane hydroxylation by nonheme iron(IV)-oxo complexes. Angew. Chem. Int. Ed. 49, 5717-5720. doi: 10.1002/anie.201001850
    • (2010) Angew. Chem. Int. Ed , vol.49 , pp. 5717-5720
    • Geng, C.1    Ye, S.2    Neese, F.3
  • 35
    • 0030358419 scopus 로고    scopus 로고
    • Naturally Occurring Organohalogen Compounds-a Comprehensive Survey
    • Vienna: Springer
    • Gribble, G. W. (1996). Naturally Occurring Organohalogen Compounds-a Comprehensive Survey. Vol. 68. Progress in the Chemistry of Organic Natural Products. Vienna: Springer.
    • (1996) Progress in the Chemistry of Organic Natural Products , vol.68
    • Gribble, G.W.1
  • 36
    • 0001655184 scopus 로고    scopus 로고
    • Naturally occurring organohalogen compounds
    • Gribble, G. W. (1998). Naturally occurring organohalogen compounds. Acc. Chem. Res. 31, 141-152. doi: 10.1021/ar9701777
    • (1998) Acc. Chem. Res , vol.31 , pp. 141-152
    • Gribble, G.W.1
  • 37
    • 0038324086 scopus 로고    scopus 로고
    • The diversity of naturally produced organohalogens
    • Gribble, G. W. (2003). The diversity of naturally produced organohalogens. Chemosphere 52, 289-297. doi: 10.1016/S0045-6535(03)00207-8
    • (2003) Chemosphere , vol.52 , pp. 289-297
    • Gribble, G.W.1
  • 38
    • 4944226169 scopus 로고    scopus 로고
    • Natural organohalogens: a new frontier for medicinal agents?
    • Gribble, G. W. (2004). Natural organohalogens: a new frontier for medicinal agents? J. Chem. Educ. 81, 1441-1449. doi: 10.1021/ed081p1441
    • (2004) J. Chem. Educ , vol.81 , pp. 1441-1449
    • Gribble, G.W.1
  • 39
    • 0002815533 scopus 로고    scopus 로고
    • Naturally Occurring Organohalogen Compounds-a Comprehensive Update
    • Vienna: Springer
    • Gribble, G. W. (2010). Naturally Occurring Organohalogen Compounds-a Comprehensive Update. Vol. 91. Progress in the Chemistry of Organic Natural Products. Vienna: Springer. doi: 10.1007/978-3-211-99323-1
    • (2010) Progress in the Chemistry of Organic Natural Products , vol.91
    • Gribble, G.W.1
  • 40
    • 80051552371 scopus 로고    scopus 로고
    • The coupled-cluster description of electronic structure: perspectives for bioinorganic chemistry
    • Harvey, J. N. (2011). The coupled-cluster description of electronic structure: perspectives for bioinorganic chemistry. J. Biol. Inorg. Chem. 16, 831-839. doi: 10.1007/s00775-011-0786-7
    • (2011) J. Biol. Inorg. Chem , vol.16 , pp. 831-839
    • Harvey, J.N.1
  • 41
    • 84855303488 scopus 로고    scopus 로고
    • The effect of desolvation on nucleophilic halogenase activity
    • Healy, E. F. (2011). The effect of desolvation on nucleophilic halogenase activity. Comput. Theor. Chem. 964, 91-93. doi: 10.1016/j.comptc.2010.12.003
    • (2011) Comput. Theor. Chem , vol.964 , pp. 91-93
    • Healy, E.F.1
  • 42
    • 82955189210 scopus 로고    scopus 로고
    • Perspectives on biotechnological halogenation Part I: halogenated products and enzymatic halogenation
    • Herrera-Rodriguez, L. N., Khan, F., Robins, K. T., and Meyer, H.-P. (2011a). Perspectives on biotechnological halogenation Part I: halogenated products and enzymatic halogenation. Chim. Oggi (Chemistry Today) 29, 31-33.
    • (2011) Chim. Oggi (Chemistry Today) , vol.29 , pp. 31-33
    • Herrera-Rodriguez, L.N.1    Khan, F.2    Robins, K.T.3    Meyer, H.-P.4
  • 43
    • 84856171107 scopus 로고    scopus 로고
    • Perspectives on biotechnological halogenation Part II: prospecting for future biohalogenases
    • Herrera-Rodriguez, L. N., Meyer, H. P., Robins, K. T., and Khan, F. (2011b). Perspectives on biotechnological halogenation Part II: prospecting for future biohalogenases. Chim. Oggi (Chemistry Today) 29, 47-49.
    • (2011) Chim. Oggi (Chemistry Today) , vol.29 , pp. 47-49
    • Herrera-Rodriguez, L.N.1    Meyer, H.P.2    Robins, K.T.3    Khan, F.4
  • 44
    • 77951678517 scopus 로고    scopus 로고
    • The fundamental role of exchange-enhanced reactivity in C-H activation by S = 2 oxo iron(IV) complexes
    • Janardanan, D., Wang, Y., Schyman, P., Que, L. Jr., and Shaik, S. (2010). The fundamental role of exchange-enhanced reactivity in C-H activation by S = 2 oxo iron(IV) complexes. Angew. Chem. Int. Ed. 49, 3342-3345. doi: 10.1002/anie.201000004
    • (2010) Angew. Chem. Int. Ed , vol.49 , pp. 3342-3345
    • Janardanan, D.1    Wang, Y.2    Schyman, P.3    Que, L.4    Shaik, S.5
  • 45
    • 79951565073 scopus 로고    scopus 로고
    • Spectroscopic characterization of cytochrome P450 Compound I
    • Jung, C., de Vries, S., and Schünemann, V. (2011). Spectroscopic characterization of cytochrome P450 Compound I. Arch. Biochem. Biophys. 507, 44-55. doi: 10.1016/j.abb.2010.12.029
    • (2011) Arch. Biochem. Biophys , vol.507 , pp. 44-55
    • Jung, C.1    de Vries, S.2    Schünemann, V.3
  • 46
    • 67651030413 scopus 로고    scopus 로고
    • The catalytic mechanism of fluoroacetate dehalogenase: a computational exploration of biological dehalogenation
    • Kamachi, T., Nakayama, T., Shitamichi, O., Jitsumori, K., Kurihara, T., Esaki, N., et al. (2009). The catalytic mechanism of fluoroacetate dehalogenase: a computational exploration of biological dehalogenation. Chem. Eur. J. 15, 7394-7403. doi: 10.1002/chem.200801813
    • (2009) Chem. Eur. J , vol.15 , pp. 7394-7403
    • Kamachi, T.1    Nakayama, T.2    Shitamichi, O.3    Jitsumori, K.4    Kurihara, T.5    Esaki, N.6
  • 47
    • 77956289715 scopus 로고    scopus 로고
    • Conformational switch triggered by α-ketoglutarate in a halogenase of curacin A biosynthesis
    • Khare, D., Wang, B., Gu, L., Razelun, J., Sherman, D. H., Gerwick, W. H., et al. (2010). Conformational switch triggered by α-ketoglutarate in a halogenase of curacin A biosynthesis. Proc. Natl. Acad. Sci. U.S.A. 107, 14099-14104. doi: 10.1073/pnas.1006738107
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 14099-14104
    • Khare, D.1    Wang, B.2    Gu, L.3    Razelun, J.4    Sherman, D.H.5    Gerwick, W.H.6
  • 48
    • 33646139119 scopus 로고    scopus 로고
    • Quantum mechanics/molecular mechanics calculations of the vanadium dependent chloroperoxidase
    • Kravitz, J. Y., Pecoraro, V. L., and Carlson, H. A. (2005). Quantum mechanics/molecular mechanics calculations of the vanadium dependent chloroperoxidase. J. Chem. Theory Comput. 1, 1265-1274. doi: 10.1021/ct050132o
    • (2005) J. Chem. Theory Comput , vol.1 , pp. 1265-1274
    • Kravitz, J.Y.1    Pecoraro, V.L.2    Carlson, H.A.3
  • 49
    • 70349932987 scopus 로고    scopus 로고
    • First-principles study of non-heme Fe(II) halogenase SyrB2 reactivity
    • Kulik, H. J., Blasiak, L. C., Marzari, N., and Drennan, C. L. (2009). First-principles study of non-heme Fe(II) halogenase SyrB2 reactivity. J. Am. Chem. Soc. 131, 14426-14433. doi: 10.1021/ja905206k
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 14426-14433
    • Kulik, H.J.1    Blasiak, L.C.2    Marzari, N.3    Drennan, C.L.4
  • 50
    • 33748334301 scopus 로고    scopus 로고
    • Density functional theory in transition-metal chemistry: a self-consistent Hubbard U approach
    • Kulik, H. J., Cococcioni, M., Scherlis, D. A., and Marzari, N. (2006). Density functional theory in transition-metal chemistry: a self-consistent Hubbard U approach. Phys. Rev. Lett. 97:103001. doi: 10.1103/PhysRevLett.97.103001
    • (2006) Phys. Rev. Lett , vol.97
    • Kulik, H.J.1    Cococcioni, M.2    Scherlis, D.A.3    Marzari, N.4
  • 51
    • 84876537991 scopus 로고    scopus 로고
    • Substrate placement influences reactivity in non-heme Fe(II) halogenases and hydroxylases
    • Kulik, H. J., and Drennan, C. L. (2013). Substrate placement influences reactivity in non-heme Fe(II) halogenases and hydroxylases. J. Biol. Chem. 288, 11233-11241. doi: 10.1074/jbc.M112.415570
    • (2013) J. Biol. Chem , vol.288 , pp. 11233-11241
    • Kulik, H.J.1    Drennan, C.L.2
  • 53
    • 70350776835 scopus 로고    scopus 로고
    • Effects of substrate, protein environment, and proximal ligand mutation on compound I and compound 0 of chloroperoxidase
    • Lai, W., Chen, H., Cho, K.-B., and Shaik, S. (2009a). Effects of substrate, protein environment, and proximal ligand mutation on compound I and compound 0 of chloroperoxidase. J. Phys. Chem. A 113, 11763-11771. doi: 10.1021/jp902898s
    • (2009) J. Phys. Chem. A , vol.113 , pp. 11763-11771
    • Lai, W.1    Chen, H.2    Cho, K.-B.3    Shaik, S.4
  • 54
    • 66549089347 scopus 로고    scopus 로고
    • What kinds of ferryl species exist for compound II of chloroperoxidase? A dialog of theory with experiment
    • Lai, W., Chen, H., and Shaik, S. (2009b). What kinds of ferryl species exist for compound II of chloroperoxidase? A dialog of theory with experiment. J. Phys. Chem. B 113, 7912-7917. doi: 10.1021/jp902288q
    • (2009) J. Phys. Chem. B , vol.113 , pp. 7912-7917
    • Lai, W.1    Chen, H.2    Shaik, S.3
  • 55
    • 84885119375 scopus 로고    scopus 로고
    • Catalysis by desolvation: the catalytic prowess of SAM-dependent halide-alkylating enzymes
    • Lohman, D. C., Edwards, D. R., and Wolfenden, R. (2013). Catalysis by desolvation: the catalytic prowess of SAM-dependent halide-alkylating enzymes. J. Am. Chem. Soc. 135, 14473-14475. doi: 10.1021/ja406381b
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 14473-14475
    • Lohman, D.C.1    Edwards, D.R.2    Wolfenden, R.3
  • 56
    • 84870390560 scopus 로고    scopus 로고
    • Oxoferryl species in mononuclear non-heme iron enzymes: biosynthesis, properties and reactivity from a theoretical perspective
    • Lundberg, M., and Borowski, T. (2013). Oxoferryl species in mononuclear non-heme iron enzymes: biosynthesis, properties and reactivity from a theoretical perspective. Coord. Chem. Rev. 257, 277-289. doi: 10.1016/j.ccr.2012.03.047
    • (2013) Coord. Chem. Rev , vol.257 , pp. 277-289
    • Lundberg, M.1    Borowski, T.2
  • 57
    • 65249103153 scopus 로고    scopus 로고
    • Substrate-triggered formation and remarkable stability of the C-H bond-cleaving chloroferryl intermediate in the aliphatic halogenase, SyrB2
    • Matthews, M. L., Krest, C. M., Barr, E. W., Vaillancourt, F. H., Walsh, C. T., Green, M. T., et al. (2009a). Substrate-triggered formation and remarkable stability of the C-H bond-cleaving chloroferryl intermediate in the aliphatic halogenase, SyrB2. Biochemistry 48, 4331-4343. doi: 10.1021/bi900109z
    • (2009) Biochemistry , vol.48 , pp. 4331-4343
    • Matthews, M.L.1    Krest, C.M.2    Barr, E.W.3    Vaillancourt, F.H.4    Walsh, C.T.5    Green, M.T.6
  • 58
    • 70449564335 scopus 로고    scopus 로고
    • Substrate positioning controls the partition between halogenation and hydroxylation in the aliphatic halogenase, SyrB2
    • Matthews, M. L., Neumann, C. S., Miles, L. A., Grove, T. L., Booker, S. J., Krebs, C., et al. (2009b). Substrate positioning controls the partition between halogenation and hydroxylation in the aliphatic halogenase, SyrB2. Proc. Natl. Acad. Sci. U.S.A. 106, 17723-17728. doi: 10.1073/pnas.0909649106
    • (2009) Proc. Natl. Acad. Sci. U.S.A , vol.106 , pp. 17723-17728
    • Matthews, M.L.1    Neumann, C.S.2    Miles, L.A.3    Grove, T.L.4    Booker, S.J.5    Krebs, C.6
  • 59
    • 80051548928 scopus 로고    scopus 로고
    • Correlated wavefunction methods in bioinorganic chemistry
    • Neese, F., Liakos, D. G., and Ye, S. F. (2011). Correlated wavefunction methods in bioinorganic chemistry. J. Biol. Inorg. Chem. 16, 821-829. doi: 10.1007/s00775-011-0787-6
    • (2011) J. Biol. Inorg. Chem , vol.16 , pp. 821-829
    • Neese, F.1    Liakos, D.G.2    Ye, S.F.3
  • 60
    • 39149099787 scopus 로고    scopus 로고
    • Halogenation strategies in natural product biosynthesis
    • Neumann, C. S., Galonic Fujimori, D., and Walsh, C. T. (2008). Halogenation strategies in natural product biosynthesis. Chem. Biol. 15, 99-109. doi: 10.1016/j.chembiol.2008.01.006
    • (2008) Chem. Biol , vol.15 , pp. 99-109
    • Neumann, C.S.1    Galonic Fujimori, D.2    Walsh, C.T.3
  • 61
    • 77952381293 scopus 로고    scopus 로고
    • Active site, catalytic cycle, and iodination reactions of vanadium iodoperoxidase: a computational study
    • Pacios, L. F., and Gálvez, O. (2010). Active site, catalytic cycle, and iodination reactions of vanadium iodoperoxidase: a computational study. J. Chem. Theory Comput. 6, 1738-1752. doi: 10.1021/ct100041x
    • (2010) J. Chem. Theory Comput , vol.6 , pp. 1738-1752
    • Pacios, L.F.1    Gálvez, O.2
  • 62
    • 68149144337 scopus 로고    scopus 로고
    • Why does the enzyme SyrB2 chlorinate, but does not hydroxylate, saturated hydrocarbons? A density functional theory (DFT) study
    • Pandian, S., Vincent, M. A., Hillier, I. H., and Burton, N. A. (2009). Why does the enzyme SyrB2 chlorinate, but does not hydroxylate, saturated hydrocarbons? A density functional theory (DFT) study. Dalton Trans. 6201-6207. doi: 10.1039/b906866j
    • (2009) Dalton Trans , pp. 6201-6207
    • Pandian, S.1    Vincent, M.A.2    Hillier, I.H.3    Burton, N.A.4
  • 63
    • 84877258549 scopus 로고    scopus 로고
    • Regioselective arene halogenation using the FAD-dependent halogenase RebH
    • Payne, J. T., Andorfer, M. C., and Lewis, J. C. (2013). Regioselective arene halogenation using the FAD-dependent halogenase RebH. Angew. Chem. Int. Ed. 52, 5271-5274. doi: 10.1002/anie.201300762
    • (2013) Angew. Chem. Int. Ed , vol.52 , pp. 5271-5274
    • Payne, J.T.1    Andorfer, M.C.2    Lewis, J.C.3
  • 64
    • 77249101987 scopus 로고    scopus 로고
    • Chloramphenicol biosynthesis: the structure of CmlS, a flavin-dependent halogenase showing a covalent flavin-aspartate bond
    • Podzelinska, K., Latimer, R., Bhattacharya, A., Vining, L. C., Zechel, D. L., and Jia, Z. (2010). Chloramphenicol biosynthesis: the structure of CmlS, a flavin-dependent halogenase showing a covalent flavin-aspartate bond. J. Mol. Biol. 397, 316-331. doi: 10.1016/j.jmb.2010.01.020
    • (2010) J. Mol. Biol , vol.397 , pp. 316-331
    • Podzelinska, K.1    Latimer, R.2    Bhattacharya, A.3    Vining, L.C.4    Zechel, D.L.5    Jia, Z.6
  • 65
    • 84895930955 scopus 로고    scopus 로고
    • Quantum mechanics/molecular mechanics study on the oxygen binding and substrate hydroxylation step in AlkB repair enzymes
    • Quesne, M. G., Latifi, R., Gonzalez-Ovalle, L. E., Kumar, D., and de Visser, S. P. (2014). Quantum mechanics/molecular mechanics study on the oxygen binding and substrate hydroxylation step in AlkB repair enzymes. Chem. Eur. J. 20, 435-446. doi: 10.1002/chem.201303282
    • (2014) Chem. Eur. J , vol.20 , pp. 435-446
    • Quesne, M.G.1    Latifi, R.2    Gonzalez-Ovalle, L.E.3    Kumar, D.4    de Visser, S.P.5
  • 66
    • 33644893629 scopus 로고    scopus 로고
    • Structure and function of vanadium haloperoxidases
    • Raugei, S., and Carloni, P. (2006). Structure and function of vanadium haloperoxidases. J. Phys. Chem. B 110, 3747-3758. doi: 10.1021/jp054901b
    • (2006) J. Phys. Chem. B , vol.110 , pp. 3747-3758
    • Raugei, S.1    Carloni, P.2
  • 67
    • 78549294465 scopus 로고    scopus 로고
    • Integrating carbon-halogen bond formation into medicinal plant metabolism
    • Runguphan, W., Qu, X., and O'Connor, S. E. (2010). Integrating carbon-halogen bond formation into medicinal plant metabolism. Nature 468, 461-464. doi: 10.1038/nature09524
    • (2010) Nature , vol.468 , pp. 461-464
    • Runguphan, W.1    Qu, X.2    O'Connor, S.E.3
  • 68
    • 0345825809 scopus 로고    scopus 로고
    • Comparison between the geometric and electronic structures and reactivities of (FeNO)7 and (FeO2)8 complexes: a density functional theory study
    • Schenk, G., Pau, M. Y. M., and Solomon, E. I. (2004). Comparison between the geometric and electronic structures and reactivities of (FeNO)7 and (FeO2)8 complexes: a density functional theory study. J. Am. Chem. Soc. 126, 505-515. doi: 10.1021/ja036715u
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 505-515
    • Schenk, G.1    Pau, M.Y.M.2    Solomon, E.I.3
  • 69
    • 77952335014 scopus 로고    scopus 로고
    • Halomethane biosynthesis: structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana
    • Schmidberger, J. W., James, A. B., Edwards, R., Naismith, J. H., and O'Hagan, D. (2010). Halomethane biosynthesis: structure of a SAM-dependent halide methyltransferase from Arabidopsis thaliana. Angew. Chem. Int. Ed. 49, 3646-3648. doi: 10.1002/anie.201000119
    • (2010) Angew. Chem. Int. Ed , vol.49 , pp. 3646-3648
    • Schmidberger, J.W.1    James, A.B.2    Edwards, R.3    Naismith, J.H.4    O'Hagan, D.5
  • 70
    • 70350660770 scopus 로고    scopus 로고
    • Finite-temperature effects in enzymatic reactions-Insights from QM/MM free-energy simulations
    • Senn, H. M., Kästner, J., Breidung, J., and Thiel, W. (2009). Finite-temperature effects in enzymatic reactions-Insights from QM/MM free-energy simulations. Can. J. Chem. 87, 1322-1337. doi: 10.1139/V09-092
    • (2009) Can. J. Chem , vol.87 , pp. 1322-1337
    • Senn, H.M.1    Kästner, J.2    Breidung, J.3    Thiel, W.4
  • 71
    • 25844511268 scopus 로고    scopus 로고
    • Insight into enzymatic C-F bond formation from QM and QM/MM calculations
    • Senn, H. M., O'Hagan, D., and Thiel, W. (2005). Insight into enzymatic C-F bond formation from QM and QM/MM calculations. J. Am. Chem. Soc. 127, 13643-13655. doi: 10.1021/ja053875s
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 13643-13655
    • Senn, H.M.1    O'Hagan, D.2    Thiel, W.3
  • 73
    • 34047191046 scopus 로고    scopus 로고
    • QM/MM studies of enzymes
    • Senn, H. M., and Thiel, W. (2007b). QM/MM studies of enzymes. Curr. Opin. Chem. Biol. 11, 182-187. doi: 10.1016/j.cbpa.2007.01.684
    • (2007) Curr. Opin. Chem. Biol , vol.11 , pp. 182-187
    • Senn, H.M.1    Thiel, W.2
  • 74
    • 60349127442 scopus 로고    scopus 로고
    • QM/MM methods for biomolecular systems
    • Senn, H. M., and Thiel, W. (2009). QM/MM methods for biomolecular systems. Angew. Chem. Int. Ed. 48, 1198-1229. doi: 10.1002/anie.200802019
    • (2009) Angew. Chem. Int. Ed , vol.48 , pp. 1198-1229
    • Senn, H.M.1    Thiel, W.2
  • 75
    • 77349115125 scopus 로고    scopus 로고
    • P450 enzymes: their structure, reactivity, and selectivity-modeled by QM/MM calculations
    • Shaik, S., Cohen, S., Wang, Y., Chen, H., Kumar, D., and Thiel, W. (2009). P450 enzymes: their structure, reactivity, and selectivity-modeled by QM/MM calculations. Chem. Rev. 110, 949-1017. doi: 10.1021/cr900121s
    • (2009) Chem. Rev , vol.110 , pp. 949-1017
    • Shaik, S.1    Cohen, S.2    Wang, Y.3    Chen, H.4    Kumar, D.5    Thiel, W.6
  • 76
    • 21944432511 scopus 로고    scopus 로고
    • Theoretical perspective on the structure and mechanism of cytochrome P450 enzymes
    • Shaik, S., Kumar, D., de Visser, S. P., Altun, A., and Thiel, W. (2005). Theoretical perspective on the structure and mechanism of cytochrome P450 enzymes. Chem. Rev. 105, 2279-2328. doi: 10.1021/cr030722j
    • (2005) Chem. Rev , vol.105 , pp. 2279-2328
    • Shaik, S.1    Kumar, D.2    de Visser, S.P.3    Altun, A.4    Thiel, W.5
  • 77
    • 79961242697 scopus 로고    scopus 로고
    • The quantum chemical cluster approach for modeling enzyme reactions
    • Siegbahn, P. E. M., and Himo, F. (2011). The quantum chemical cluster approach for modeling enzyme reactions. Wiley Interdiscip. Rev. Comput. Mol. Sci. 1, 323-336. doi: 10.1002/wcms.13
    • (2011) Wiley Interdiscip. Rev. Comput. Mol. Sci , vol.1 , pp. 323-336
    • Siegbahn, P.E.M.1    Himo, F.2
  • 78
    • 84876741871 scopus 로고    scopus 로고
    • Scope and potential of halogenases in biosynthetic applications
    • Smith, D. R., Grüschow, S., and Goss, R. J. (2013). Scope and potential of halogenases in biosynthetic applications. Curr. Opin. Chem. Biol. 17, 276-283. doi: 10.1016/j.cbpa.2013.01.018
    • (2013) Curr. Opin. Chem. Biol , vol.17 , pp. 276-283
    • Smith, D.R.1    Grüschow, S.2    Goss, R.J.3
  • 79
    • 84858637274 scopus 로고    scopus 로고
    • Explicitly correlated electronic structure theory from R12/F12 ansätze
    • Ten-No, S., and Noga, J. (2012). Explicitly correlated electronic structure theory from R12/F12 ansätze. Wiley Interdiscip. Rev. Comput. Mol. Sci. 2, 114-125. doi: 10.1002/wcms.68
    • (2012) Wiley Interdiscip. Rev. Comput. Mol. Sci , vol.2 , pp. 114-125
    • Ten-No, S.1    Noga, J.2
  • 80
    • 33645799730 scopus 로고    scopus 로고
    • Quantum chemical modeling of reaction mechanism for 2-oxoglutarate dependent enzymes: effect of substitution of iron by nickel and cobalt
    • Topol, I. A., Nemukhin, A. V., Salnikow, K., Cachau, R. E., Abashkin, Y. G., Kasprzak, K. S., et al. (2006). Quantum chemical modeling of reaction mechanism for 2-oxoglutarate dependent enzymes: effect of substitution of iron by nickel and cobalt. J. Phys. Chem. A 110, 4223-4228. doi: 10.1021/jp055633k
    • (2006) J. Phys. Chem. A , vol.110 , pp. 4223-4228
    • Topol, I.A.1    Nemukhin, A.V.2    Salnikow, K.3    Cachau, R.E.4    Abashkin, Y.G.5    Kasprzak, K.S.6
  • 81
    • 33748588122 scopus 로고    scopus 로고
    • Nature's inventory of halogenation catalysts: oxidative strategies predominate
    • Vaillancourt, F. H., Yeh, E., Vosburg, D. A., Garneau-Tsodikova, S., and Walsh, C. T. (2006). Nature's inventory of halogenation catalysts: oxidative strategies predominate. Chem. Rev. 106, 3364-3378. doi: 10.1021/cr050313i
    • (2006) Chem. Rev , vol.106 , pp. 3364-3378
    • Vaillancourt, F.H.1    Yeh, E.2    Vosburg, D.A.3    Garneau-Tsodikova, S.4    Walsh, C.T.5
  • 82
    • 77950166505 scopus 로고    scopus 로고
    • Performance of CASPT2 and DFT for relative spin-state energetics of heme models
    • Vancoillie, S., Zhao, H. L., Radoñ, M., and Pierloot, K. (2010). Performance of CASPT2 and DFT for relative spin-state energetics of heme models. J. Chem. Theory Comput. 6, 576-582. doi: 10.1021/ct900567c
    • (2010) J. Chem. Theory Comput , vol.6 , pp. 576-582
    • Vancoillie, S.1    Zhao, H.L.2    Radoñ, M.3    Pierloot, K.4
  • 83
    • 84872580413 scopus 로고    scopus 로고
    • Halogenating enzymes for selective halogenation reactions
    • van Pée, K. H. (2012). Halogenating enzymes for selective halogenation reactions. Curr. Org. Chem. 16, 2583-2597. doi: 10.2174/138527212804004607
    • (2012) Curr. Org. Chem , vol.16 , pp. 2583-2597
    • van Pée, K.H.1
  • 85
    • 65349170600 scopus 로고    scopus 로고
    • Biohalogenation: nature's way to synthesize halogenated metabolites
    • Wagner, C., El Omari, M., and König, G. M. (2009). Biohalogenation: nature's way to synthesize halogenated metabolites. J. Nat. Prod. 72, 540-553. doi: 10.1021/np800651m
    • (2009) J. Nat. Prod , vol.72 , pp. 540-553
    • Wagner, C.1    El Omari, M.2    König, G.M.3
  • 86
    • 34250308062 scopus 로고    scopus 로고
    • 51V NMR chemical shifts calculated from QM/MM models of vanadium chloroperoxidase
    • Waller, M. P., Bühl, M., Geethalakshmi, K. R., Wang, D., and Thiel, W. (2007). 51V NMR chemical shifts calculated from QM/MM models of vanadium chloroperoxidase. Chem. Eur. J. 13, 4723-4732. doi: 10.1002/chem.200700295
    • (2007) Chem. Eur. J , vol.13 , pp. 4723-4732
    • Waller, M.P.1    Bühl, M.2    Geethalakshmi, K.R.3    Wang, D.4    Thiel, W.5
  • 87
    • 43949110999 scopus 로고    scopus 로고
    • 51V NMR chemical shifts from quantum-mechanical/molecular-mechanical models of vanadium bromoperoxidase
    • Waller, M. P., Geethalakshmi, K. R., and Bühl, M. (2008). 51V NMR chemical shifts from quantum-mechanical/molecular-mechanical models of vanadium bromoperoxidase. J. Phys. Chem. B 112, 5813-5823. doi: 10.1021/jp800580n
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5813-5823
    • Waller, M.P.1    Geethalakshmi, K.R.2    Bühl, M.3
  • 88
    • 84860269412 scopus 로고    scopus 로고
    • Mixed quantum mechanics and molecular mechanics methods: looking inside proteins
    • Wallrapp, F. H., and Guallar, V. (2011). Mixed quantum mechanics and molecular mechanics methods: looking inside proteins. Wiley Interdiscip. Rev. Comput. Mol. Sci. 1, 315-322. doi: 10.1002/wcms.27
    • (2011) Wiley Interdiscip. Rev. Comput. Mol. Sci , vol.1 , pp. 315-322
    • Wallrapp, F.H.1    Guallar, V.2
  • 89
    • 0017100947 scopus 로고
    • Theoretical studies of enzymatic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • Warshel, A., and Levitt, M. (1976). Theoretical studies of enzymatic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. J. Mol. Biol. 103, 227-249. doi: 10.1016/0022-2836(76)90311-9
    • (1976) J. Mol. Biol , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2
  • 90
    • 67949109444 scopus 로고    scopus 로고
    • Structural analysis of an open active site conformation of nonheme iron halogenase CytC3
    • Wong, C., Fujimori, D. G., Walsh, C. T., and Drennan, C. L. (2009). Structural analysis of an open active site conformation of nonheme iron halogenase CytC3. J. Am. Chem. Soc. 131, 4872-4879. doi: 10.1021/ja8097355
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 4872-4879
    • Wong, C.1    Fujimori, D.G.2    Walsh, C.T.3    Drennan, C.L.4
  • 91
    • 84880420011 scopus 로고    scopus 로고
    • Elucidation of the Fe(IV)=O intermediate in the catalytic cycle of the halogenase SyrB2
    • Wong, S. D., Srnec, M., Matthews, M. L., Liu, L. V., Kwak, Y., Park, K., et al. (2013). Elucidation of the Fe(IV)=O intermediate in the catalytic cycle of the halogenase SyrB2. Nature 499, 320-323. doi: 10.1038/nature12304
    • (2013) Nature , vol.499 , pp. 320-323
    • Wong, S.D.1    Srnec, M.2    Matthews, M.L.3    Liu, L.V.4    Kwak, Y.5    Park, K.6
  • 92
    • 79952150252 scopus 로고    scopus 로고
    • Nonheme oxo-iron(IV) intermediates form an oxyl radical upon approaching the C-H bond activation transition state
    • Ye, S., and Neese, F. (2011). Nonheme oxo-iron(IV) intermediates form an oxyl radical upon approaching the C-H bond activation transition state. Proc. Natl. Acad. Sci. U.S.A. 108, 1228-1233. doi: 10.1073/pnas.1008411108
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 1228-1233
    • Ye, S.1    Neese, F.2
  • 93
    • 77950798000 scopus 로고    scopus 로고
    • Cryoreduction of the NO-adduct of taurine:a-ketoglutarate dioxygenase (TauD) yields an elusive (FeNO)8 species
    • Ye, S., Price, J. C., Barr, E. W., Green, M. T., Bollinger, J. M. Jr., Krebs, C., et al. (2010). Cryoreduction of the NO-adduct of taurine:a-ketoglutarate dioxygenase (TauD) yields an elusive (FeNO)8 species. J. Am. Chem. Soc. 132, 4739-4751. doi: 10.1021/ja909715g
    • (2010) J. Am. Chem. Soc , vol.132 , pp. 4739-4751
    • Ye, S.1    Price, J.C.2    Barr, E.W.3    Green, M.T.4    Bollinger, J.M.5    Krebs, C.6
  • 94
    • 84861165004 scopus 로고    scopus 로고
    • Electronic structure analysis of the oxygen-activation mechanism by FeII-and α-ketoglutarate (aKG)-dependent dioxygenases
    • Ye, S., Riplinger, C., Hansen, A., Krebs, C., Bollinger, J. M. Jr., and Neese, F. (2012). Electronic structure analysis of the oxygen-activation mechanism by FeII-and α-ketoglutarate (aKG)-dependent dioxygenases. Chem. Eur. J. 18, 6555-6567. doi: 10.1002/chem.201102829
    • (2012) Chem. Eur. J , vol.18 , pp. 6555-6567
    • Ye, S.1    Riplinger, C.2    Hansen, A.3    Krebs, C.4    Bollinger, J.M.5    Neese, F.6
  • 95
    • 33846842522 scopus 로고    scopus 로고
    • Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenases
    • Yeh, E., Blasiak, L. C., Koglin, A., Drennan, C. L., and Walsh, C. T. (2007). Chlorination by a long-lived intermediate in the mechanism of flavin-dependent halogenases. Biochemistry 46, 1284-1292. doi: 10.1021/bi0621213
    • (2007) Biochemistry , vol.46 , pp. 1284-1292
    • Yeh, E.1    Blasiak, L.C.2    Koglin, A.3    Drennan, C.L.4    Walsh, C.T.5
  • 96
    • 47049118079 scopus 로고    scopus 로고
    • QM/MM investigation of structure and spectroscopic properties of a vanadium-containing peroxidase
    • Zhang, Y., and Gascón, J. A. (2008). QM/MM investigation of structure and spectroscopic properties of a vanadium-containing peroxidase. J. Inorg. Biochem. 102, 1684-1690. doi: 10.1016/j.jinorgbio.2008.04.006
    • (2008) J. Inorg. Biochem , vol.102 , pp. 1684-1690
    • Zhang, Y.1    Gascón, J.A.2
  • 97
    • 67651121669 scopus 로고    scopus 로고
    • Structural insights into regioselectivity in the enzymatic chlorination of tryptophan
    • Zhu, X., De Laurentis, W., Leang, K., Herrmann, J., Ihlefeld, K., van Pée, K. H., et al. (2009). Structural insights into regioselectivity in the enzymatic chlorination of tryptophan. J. Mol. Biol. 391, 74-85. doi: 10.1016/j.jmb.2009.06.008
    • (2009) J. Mol. Biol , vol.391 , pp. 74-85
    • Zhu, X.1    De Laurentis, W.2    Leang, K.3    Herrmann, J.4    Ihlefeld, K.5    van Pée, K.H.6
  • 98
    • 36749093357 scopus 로고    scopus 로고
    • Mechanism of enzymatic fluorination in Streptomyces cattleya
    • Zhu, X., Robinson, D. A., McEwan, A. R., O'Hagan, D., and Naismith, J. H. (2007). Mechanism of enzymatic fluorination in Streptomyces cattleya. J. Am. Chem. Soc. 129, 14597-14604. doi: 10.1021/ja0731569
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 14597-14604
    • Zhu, X.1    Robinson, D.A.2    McEwan, A.R.3    O'Hagan, D.4    Naismith, J.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.