메뉴 건너뛰기




Volumn 33, Issue 7, 2000, Pages 449-455

Hypersensitive radical and the mechanisms of cytochrome P450-catalyzed hydroxylation reactions

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOL; CATION; CYCLOPROPANE DERIVATIVE; CYTOCHROME P450; IRON; OXYGEN; POLYCYCLIC AROMATIC HYDROCARBON DERIVATIVE; RADICAL; CYTOCHROME P450 2B1; FREE RADICAL;

EID: 0033623690     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar960058b     Document Type: Article
Times cited : (257)

References (58)
  • 2
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos, T. L.; Finzel, B. C.; Howard, P. J. High-resolution Crystal Structure of Cytochrome P450cam. J. Mol. Biol. 1987, 195, 687-700.
    • (1987) J. Mol. Biol. , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, P.J.3
  • 3
    • 0030869952 scopus 로고    scopus 로고
    • Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer
    • Schlichting, I.; Jung, C.; Schulze, H. Crystal Structure of Cytochrome P-450cam Complexed with the (1S)-Camphor Enantiomer. FEBS Lett. 1997, 415, 253-257.
    • (1997) FEBS Lett. , vol.415 , pp. 253-257
    • Schlichting, I.1    Jung, C.2    Schulze, H.3
  • 6
    • 33847799949 scopus 로고
    • Aliphatic hydroxylation via oxygen rebound. Oxygen transfer catalyzed by iron
    • Groves, J. T.; McClusky, G. A. Aliphatic Hydroxylation Via Oxygen Rebound. Oxygen Transfer Catalyzed by Iron. J. Am. Chem. Soc. 1976, 98, 859-861.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 859-861
    • Groves, J.T.1    McClusky, G.A.2
  • 7
    • 0017800253 scopus 로고
    • Aliphatic hydroxylation by highly purified liver microsomal cytochrome P-450. Evidence for a carbon radical intermediate
    • Groves, J. T.; McClusky, G. A.; White, R. E.; Coon, M. J. Aliphatic Hydroxylation by Highly Purified Liver Microsomal Cytochrome P-450. Evidence for a Carbon Radical Intermediate. Biochem. Biophys. Res. Commun. 1978, 81, 154-160.
    • (1978) Biochem. Biophys. Res. Commun. , vol.81 , pp. 154-160
    • Groves, J.T.1    McClusky, G.A.2    White, R.E.3    Coon, M.J.4
  • 8
    • 0021754855 scopus 로고
    • Hydroxylation by cytochrome P-450 and metalloporphyrin models. Evidence for allylic rearrangement
    • Groves, J. T.; Subramanian, D. V. Hydroxylation by Cytochrome P-450 and Metalloporphyrin Models. Evidence for Allylic Rearrangement. J. Am. Chem. Soc. 1984, 106, 2177-2181.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 2177-2181
    • Groves, J.T.1    Subramanian, D.V.2
  • 9
    • 0000540460 scopus 로고
    • Timing of the radical recombination step in cytochrome P-450 catalysis with ring-strained probes
    • Ortiz de Montellano, P. R.; Stearns, R. A. Timing of the Radical Recombination Step in Cytochrome P-450 Catalysis with Ring-Strained Probes. J. Am. Chem. Soc. 1987, 109, 3415-3420.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 3415-3420
    • Ortiz De Montellano, P.R.1    Stearns, R.A.2
  • 12
    • 0343881608 scopus 로고
    • Radical kinetics and mechanistic probe studies
    • Coxon, J. M., Ed.; JAI Press: Greenwich, CT
    • Newcomb, M. Radical Kinetics and Mechanistic Probe Studies. In Advances in Detailed Reactions Mechanisms; Coxon, J. M., Ed.; JAI Press: Greenwich, CT, 1991; Vol. 1, pp 1-33.
    • (1991) Advances in Detailed Reactions Mechanisms , vol.1 , pp. 1-33
    • Newcomb, M.1
  • 13
    • 0027538424 scopus 로고
    • Competition methods and scales for alkyl radical reaction kinetics
    • Newcomb, M. Competition Methods and Scales for Alkyl Radical Reaction Kinetics. Tetrahedron 1993, 49, 1151-1176.
    • (1993) Tetrahedron , vol.49 , pp. 1151-1176
    • Newcomb, M.1
  • 14
    • 0001478790 scopus 로고
    • N-Hydroxypyridine-2-thione esters as radical precursors in kinetic studies. Measurements of rate constants for hydrogen atom abstraction reactions
    • Newcomb, M.; Park, S.-U. N-Hydroxypyridine-2-thione Esters as Radical Precursors in Kinetic Studies. Measurements of Rate Constants for Hydrogen Atom Abstraction Reactions. J. Am. Chem. Soc. 1986, 108, 4132-4134.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 4132-4134
    • Newcomb, M.1    Park, S.-U.2
  • 15
    • 0000087095 scopus 로고
    • A Convenient method for kinetic studies of fast radical rearrangements rate constants and arrhenius function for the cyclopropylcarbinyl ring opening
    • Newcomb, M.; Glenn, A. G. A Convenient Method for Kinetic Studies of Fast Radical Rearrangements Rate Constants and Arrhenius Function for the Cyclopropylcarbinyl Ring Opening. J. Am. Chem. Soc. 1989, 111, 275-277.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 275-277
    • Newcomb, M.1    Glenn, A.G.2
  • 16
    • 0000327515 scopus 로고
    • Picosecond radical kinetics. Ring openings of phenyl-substituted cyclopropylcarbinyl radicals
    • Newcomb, M.; Johnson, C. C.; Manek, M. B.; Varick, T. R. Picosecond Radical Kinetics. Ring Openings of Phenyl-Substituted Cyclopropylcarbinyl Radicals. J. Am. Chem. Soc. 1992, 114, 10915-10921.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10915-10921
    • Newcomb, M.1    Johnson, C.C.2    Manek, M.B.3    Varick, T.R.4
  • 17
    • 0000261933 scopus 로고
    • Picosecond radical kinetics. Rate constants for reaction of benzeneselenol with primary alkyl radicals and calibration of the 6-cyano-5-hexenyl radical cyclization
    • Newcomb, M.; Varick, T. R.; Ha, C.; Manek, M. B.; Yue, X. Picosecond Radical Kinetics. Rate Constants for Reaction of Benzeneselenol with Primary Alkyl Radicals and Calibration of the 6-Cyano-5-Hexenyl Radical Cyclization. J. Am. Chem. Soc. 1992, 114, 8158-8163.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 8158-8163
    • Newcomb, M.1    Varick, T.R.2    Ha, C.3    Manek, M.B.4    Yue, X.5
  • 18
    • 0000217865 scopus 로고
    • Ring opening and hydrogen atom transfer trapping of the bicyclo[2.1.0]pent-2-yl radical
    • Newcomb, M.; Manek, M. B.; Glenn, A. G. Ring Opening and Hydrogen Atom Transfer Trapping of the Bicyclo[2.1.0]pent-2-yl Radical. J. Am. Chem. Soc. 1991, 113, 949-958.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 949-958
    • Newcomb, M.1    Manek, M.B.2    Glenn, A.G.3
  • 19
    • 0000984234 scopus 로고
    • Picosecond radical kinetics. Bond cleavage of the cubylcarbinyl radical
    • Choi, S.-Y.; Eaton, P. E.; Newcomb, M.; Yip, Y.-C. Picosecond Radical Kinetics. Bond Cleavage of the Cubylcarbinyl Radical. J. Am. Chem. Soc. 1992, 114, 6326-6329.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6326-6329
    • Choi, S.-Y.1    Eaton, P.E.2    Newcomb, M.3    Yip, Y.-C.4
  • 20
    • 0027379622 scopus 로고
    • Ethoxycarbonyl acceleration of cyclopropylcarbinyl radical ring opening
    • Newcomb, M.; Choi, S.-Y. Ethoxycarbonyl Acceleration of Cyclopropylcarbinyl Radical Ring Opening. Tetrahedron Lett. 1993, 34, 6363-6364.
    • (1993) Tetrahedron Lett. , vol.34 , pp. 6363-6364
    • Newcomb, M.1    Choi, S.-Y.2
  • 21
    • 0028860195 scopus 로고
    • Picosecond radical kinetics. Alkoxycarbonyl accelerated cyclopropylcarbinyl radical ring openings
    • Choi, S.-Y.; Newcomb, M. Picosecond radical kinetics. Alkoxycarbonyl accelerated cyclopropylcarbinyl radical ring openings. Tetrahedron 1995, 51, 657-664.
    • (1995) Tetrahedron , vol.51 , pp. 657-664
    • Choi, S.-Y.1    Newcomb, M.2
  • 23
    • 0001459562 scopus 로고
    • Picosecond radical kinetics. Benzeneselenol as a fast radical trapping agent and rate constants for ring opening of the trans-(2-phenylcyclopropyl)carbinyl radical
    • Newcomb, M.; Manek, M. B. Picosecond Radical Kinetics. Benzeneselenol As a Fast Radical Trapping Agent and Rate Constants for Ring Opening of the trans-(2-Phenylcyclopropyl)Carbinyl Radical. J. Am. Chem. Soc. 1990, 112, 9662-9663.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9662-9663
    • Newcomb, M.1    Manek, M.B.2
  • 24
    • 0001014264 scopus 로고
    • Picosecond radical kinetics. Fast ring openings of constrained, aryl-substituted cyclopropylcarbinyl radicals
    • Martin-Esker, A. A.; Johnson, C. C.; Horner, J. H.; Newcomb, M. Picosecond Radical Kinetics. Fast Ring Openings of Constrained, Aryl-substituted Cyclopropylcarbinyl Radicals. J. Am. Chem. Soc. 1994, 116, 9174-9181.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 9174-9181
    • Martin-Esker, A.A.1    Johnson, C.C.2    Horner, J.H.3    Newcomb, M.4
  • 25
    • 0000557555 scopus 로고    scopus 로고
    • Picosecond radical kinetics. Rate constants for ring openings of (2-alkoxy-3-phenylcyclopropy)methyl radicals
    • Le Tadic-Biadatti, M. H.; Newcomb, M. Picosecond Radical Kinetics. Rate Constants for Ring Openings of (2-Alkoxy-3-phenylcyclopropy)methyl Radicals. J. Chem. Soc., Perkin Trans. 2 1996, 1467-1473.
    • (1996) J. Chem. Soc., Perkin Trans. 2 , vol.2 , pp. 1467-1473
    • Le Tadic-Biadatti, M.H.1    Newcomb, M.2
  • 26
    • 0032514858 scopus 로고    scopus 로고
    • Picosecond radical kinetics. Fast ring openings of secondary and tertiary trans-2-phenylcyclopropylcarbinyl radicals
    • Choi, S. Y.; Toy, P. H.; Newcomb, M. Picosecond Radical Kinetics. Fast Ring Openings of Secondary and Tertiary trans-2-Phenylcyclopropylcarbinyl Radicals. J. Org. Chem. 1998, 63, 8609-8613.
    • (1998) J. Org. Chem. , vol.63 , pp. 8609-8613
    • Choi, S.Y.1    Toy, P.H.2    Newcomb, M.3
  • 27
    • 0033306404 scopus 로고    scopus 로고
    • Picosecond radical kinetics. Rate constants for ring openings of 2-aryl-substituted cyclopropylcarbinyl radicals
    • Newcomb, M.; Choi, S. Y.; Toy, P. H. Picosecond Radical Kinetics. Rate Constants for Ring Openings of 2-Aryl-substituted Cyclopropylcarbinyl Radicals. Can. J. Chem. 1999, 77, 1123-1135.
    • (1999) Can. J. Chem. , vol.77 , pp. 1123-1135
    • Newcomb, M.1    Choi, S.Y.2    Toy, P.H.3
  • 28
    • 0001437849 scopus 로고
    • Calibration of a new horology of fast radical clocks. Ring-opening rates for Ring-alkyl-substituted and α-alkyl-substituted cyclopropylcarbinyl radicals and for the bicyclo[2.1.0]pent-2-yl radical
    • Bowry, V. W.; Lusztyk, J.; Ingold, K. U. Calibration of a New Horology of Fast Radical Clocks. Ring-Opening Rates for Ring-Alkyl-Substituted and α-Alkyl-Substituted Cyclopropylcarbinyl Radicals and for the Bicyclo[2.1.0]pent-2-yl Radical. J. Am. Chem. Soc. 1991, 113, 5687-5698.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5687-5698
    • Bowry, V.W.1    Lusztyk, J.2    Ingold, K.U.3
  • 29
    • 0027852254 scopus 로고
    • Cytochrome P450 hydroxylation of hydrocarbons: Variation in the rate of oxygen rebound using cyclopropyl radical clocks including two new ultrafast probes
    • Atkinson, J. K.; Ingold, K. U. Cytochrome P450 Hydroxylation of Hydrocarbons: Variation in the Rate of Oxygen Rebound Using Cyclopropyl Radical Clocks Including Two New Ultrafast Probes. Biochemistry 1993, 32, 9209-9214.
    • (1993) Biochemistry , vol.32 , pp. 9209-9214
    • Atkinson, J.K.1    Ingold, K.U.2
  • 30
    • 0028085491 scopus 로고
    • Cytochrome P450-catalyzed hydroxylation of hydrocarbons: Kinetic deuterium isotope effects for the hydroxylation of an ultrafast radical clock
    • Atkinson, J. K.; Hollenberg, P. F.; Ingold, K. U.; Johnson, C. C.; Le Tadic, M.-H.; Newcomb, M.; Putt, D. A. Cytochrome P450-Catalyzed Hydroxylation of Hydrocarbons: Kinetic Deuterium Isotope Effects for the Hydroxylation of an Ultrafast Radical Clock. Biochemistry 1994, 33, 10630-10637.
    • (1994) Biochemistry , vol.33 , pp. 10630-10637
    • Atkinson, J.K.1    Hollenberg, P.F.2    Ingold, K.U.3    Johnson, C.C.4    Le Tadic, M.-H.5    Newcomb, M.6    Putt, D.A.7
  • 31
    • 0029140873 scopus 로고
    • An incredibly fast apparent oxygen rebound rate constant for hydrocarbon hydroxylation by cytochrome P-450 enzymes
    • Newcomb, M.; Le Tadic, M. H.; Putt, D. A.; Hollenberg, P. F. An Incredibly Fast Apparent Oxygen Rebound Rate Constant for Hydrocarbon Hydroxylation by Cytochrome P-450 Enzymes. J. Am. Chem. Soc. 1995, 117, 3312-3313.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 3312-3313
    • Newcomb, M.1    Le Tadic, M.H.2    Putt, D.A.3    Hollenberg, P.F.4
  • 32
    • 0000456008 scopus 로고    scopus 로고
    • A substituted hypersensitive radical probe for enzyme-catalyzed hydroxylations. Synthesis of racemic and enantiomerically enriched forms and application in a cytochrome P450-catalyzed oxidation
    • Toy, P. H.; Dhanabalasingam, B.; Newcomb, M.; Hanna, I. H.; Hollenberg, P. F. A Substituted Hypersensitive Radical Probe for Enzyme-Catalyzed Hydroxylations. Synthesis of Racemic and Enantiomerically Enriched Forms and Application in a Cytochrome P450-Catalyzed Oxidation. J. Org. Chem. 1997, 62, 9114-9122.
    • (1997) J. Org. Chem. , vol.62 , pp. 9114-9122
    • Toy, P.H.1    Dhanabalasingam, B.2    Newcomb, M.3    Hanna, I.H.4    Hollenberg, P.F.5
  • 33
    • 0032511425 scopus 로고    scopus 로고
    • Hypersensitive mechanistic probe studies of cytochrome P450-catalyzed hydroxylation reactions. Implications for the cationic pathway
    • Toy, P. H.; Newcomb, M.; Hollenberg, P. F. Hypersensitive Mechanistic Probe Studies of Cytochrome P450-Catalyzed Hydroxylation Reactions. Implications for the Cationic Pathway. J. Am. Chem. Soc. 1998, 120, 7719-7729.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 7719-7729
    • Toy, P.H.1    Newcomb, M.2    Hollenberg, P.F.3
  • 34
    • 0033578349 scopus 로고    scopus 로고
    • Deuterium magic angle spinning studies of substrates bound to cytochrome P450
    • Lee, H.; Ortiz de Montellano, P. R.; McDermott, A. E. Deuterium Magic Angle Spinning Studies of Substrates Bound to Cytochrome P450. Biochemistry 1999, 38, 10808-10813.
    • (1999) Biochemistry , vol.38 , pp. 10808-10813
    • Lee, H.1    Ortiz De Montellano, P.R.2    McDermott, A.E.3
  • 35
    • 0001067880 scopus 로고
    • A hypersensitive mechanistic probe for distinguishing between radical and carbocation intermediates
    • Newcomb, M.; Chestney, D. L. A Hypersensitive Mechanistic Probe for Distinguishing Between Radical and Carbocation Intermediates. J. Am. Chem. Soc. 1994, 116, 9753-9754.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 9753-9754
    • Newcomb, M.1    Chestney, D.L.2
  • 37
    • 0034728622 scopus 로고    scopus 로고
    • Cytochrome P450-catalyzed hydroxylation of mechanistic probes that distinguish between radicals and cations. Evidence for cationic but not for radical intermediates
    • Newcomb, M.; Shen, R.; Choi, S.-Y.; Toy, P. H.; Hollenberg, P. F.; Vaz, A. D. N.; Coon, M. J. Cytochrome P450-Catalyzed Hydroxylation of Mechanistic Probes that Distinguish Between Radicals and Cations. Evidence for Cationic but Not for Radical Intermediates. J. Am. Chem. Soc. 2000, 122, 2677-2686
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2677-2686
    • Newcomb, M.1    Shen, R.2    Choi, S.-Y.3    Toy, P.H.4    Hollenberg, P.F.5    Vaz, A.D.N.6    Coon, M.J.7
  • 38
    • 0033582676 scopus 로고    scopus 로고
    • Adjusting the top end of the alkyl radical kinetic scale. Laser flash photolysis calibrations of fast radical clocks and rate constants for reactions of benzeneselenol
    • Newcomb, M.; Choi, S.-Y.; Horner, J. H. Adjusting the Top End of the Alkyl Radical Kinetic Scale. Laser Flash Photolysis Calibrations of Fast Radical Clocks and Rate Constants for Reactions of Benzeneselenol. J. Org. Chem. 1999, 64, 1225-1231.
    • (1999) J. Org. Chem. , vol.64 , pp. 1225-1231
    • Newcomb, M.1    Choi, S.-Y.2    Horner, J.H.3
  • 40
    • 0031979212 scopus 로고    scopus 로고
    • Electronic structure makes a difference: Cytochrome P-450 mediated hydroxylations of hydrocarbons as a two-state reactivity paradigm
    • Shaik, S.; Filatov, M.; Schröder, D.; Schwarz, H. Electronic Structure Makes a Difference: Cytochrome P-450 Mediated Hydroxylations of Hydrocarbons as a Two-State Reactivity Paradigm. Chem. Eur. J. 1998, 4, 193-199.
    • (1998) Chem. Eur. J. , vol.4 , pp. 193-199
    • Shaik, S.1    Filatov, M.2    Schröder, D.3    Schwarz, H.4
  • 41
    • 0030004087 scopus 로고    scopus 로고
    • Peroxo-iron and oxenoid-iron species as alternative oxygenating agents in cytochrome P450-catalyzed reactions: Switching by threonine-302 to alanine mutagenesis of cytochrome P450 2B4
    • Vaz, A. D. N.; Pernecky, S. J.; Raner, G. M.; Coon, M. J. Peroxo-Iron and Oxenoid-Iron Species as Alternative Oxygenating Agents in Cytochrome P450-Catalyzed Reactions: Switching by Threonine-302 to Alanine Mutagenesis of Cytochrome P450 2B4. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 4644-4648.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 4644-4648
    • Vaz, A.D.N.1    Pernecky, S.J.2    Raner, G.M.3    Coon, M.J.4
  • 42
    • 0032584090 scopus 로고    scopus 로고
    • Epoxidation of olefins by cytochrome P450: Evidence from site-specific mutagenesis for hydroperoxo-iron as an electrophilic oxidant
    • Vaz, A. D. N.; McGinnity, D. F.; Coon, M. J. Epoxidation of Olefins by Cytochrome P450: Evidence from Site-Specific Mutagenesis for Hydroperoxo-Iron as an Electrophilic Oxidant. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 3555-3560.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3555-3560
    • Vaz, A.D.N.1    McGinnity, D.F.2    Coon, M.J.3
  • 43
    • 0032561001 scopus 로고    scopus 로고
    • Two distinct electrophilic oxidants effect hydroxylation in cytochrome P-450-catalyzed reactions
    • Toy, P. H.; Newcomb, M.; Coon, M. J.; Vaz, A. D. N. Two Distinct Electrophilic Oxidants Effect Hydroxylation in Cytochrome P-450-Catalyzed Reactions. J. Am. Chem. Soc. 1998, 120, 9718-9719.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9718-9719
    • Toy, P.H.1    Newcomb, M.2    Coon, M.J.3    Vaz, A.D.N.4
  • 45
    • 0542422859 scopus 로고    scopus 로고
    • Heme oxygenase mechanism: Evidence for an electrophilic, ferric peroxide species
    • Ortiz de Montellano, P. R. Heme Oxygenase Mechanism: Evidence for an Electrophilic, Ferric Peroxide Species. Acc. Chem. Res. 1998, 31, 543-549.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 543-549
    • Ortiz De OMontellano, P.R.1
  • 46
    • 0028855317 scopus 로고
    • Chloroperoxidase-catalyzed asymmetric oxidations: Substrate specificity and mechanistic study
    • Zaks, A.; Dodds, D. R. Chloroperoxidase-Catalyzed Asymmetric Oxidations: Substrate Specificity and Mechanistic Study. J. Am. Chem. Soc. 1995, 117, 10419-10424.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10419-10424
    • Zaks, A.1    Dodds, D.R.2
  • 47
    • 0031823396 scopus 로고    scopus 로고
    • Hypersensitive radical probe studies of chloroperoxidase-catalyzed hydroxylation reactions
    • Toy, P. H.; Newcomb, M.; Hager, L. P. Hypersensitive Radical Probe Studies of Chloroperoxidase-Catalyzed Hydroxylation Reactions. Chem. Res. Toxicol. 1998, 11, 816-823.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 816-823
    • Toy, P.H.1    Newcomb, M.2    Hager, L.P.3
  • 48
    • 0000353336 scopus 로고
    • Radical clock substrate probes and kinetic isotope effect studies of the hydroxylation of hydrocarbons by methane monooxygenase
    • Liu, K. E.; Johnson, C. C.; Newcomb, M.; Lippard, S. J. Radical Clock Substrate Probes and Kinetic Isotope Effect Studies of the Hydroxylation of Hydrocarbons by Methane Monooxygenase. J. Am. Chem. Soc. 1993, 115, 939-947.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 939-947
    • Liu, K.E.1    Johnson, C.C.2    Newcomb, M.3    Lippard, S.J.4
  • 49
    • 0033574674 scopus 로고    scopus 로고
    • Oxidation of ultrafast radical clock substrate probes by the soluble methane monooxygenase from Methylococcus capsulatus (Bath)
    • Valentine, A. M.; Le Tadic-Biadatti, M. H.; Toy, P. H.; Newcomb, M.; Lippard, S. J. Oxidation of Ultrafast Radical Clock Substrate Probes by the Soluble Methane Monooxygenase from Methylococcus capsulatus (Bath). J. Biol. Chem. 1999, 274, 10771-10776.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10771-10776
    • Valentine, A.M.1    Le Tadic-Biadatti, M.H.2    Toy, P.H.3    Newcomb, M.4    Lippard, S.J.5
  • 50
    • 0033616098 scopus 로고    scopus 로고
    • Cationic species can be produced in soluble methane monooxygenase-catalyzed hydroxylation reactions; radical intermediates are not formed
    • Choi, S.-Y.; Eaton, P. E.; Kopp, D. A.; Lippard, S. J.; Newcomb, M.; Shen, R. Cationic Species Can Be Produced in Soluble Methane Monooxygenase-Catalyzed Hydroxylation Reactions; Radical Intermediates Are Not Formed. J. Am. Chem. Soc. 1999, 121, 12198-12199.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 12198-12199
    • Choi, S.-Y.1    Eaton, P.E.2    Kopp, D.A.3    Lippard, S.J.4    Newcomb, M.5    Shen, R.6
  • 51
    • 0001115527 scopus 로고
    • Pseudomonas oleovorans monooxygenase catalyzed asymmetric epoxidation of allyl alcohol derivatives and hydroxylation of a hypersensitive radical probe with the radical ring opening rate exceeding the oxygen rebound rate
    • Fu, H.; Newcomb, M.; Wong, C.-H. Pseudomonas oleovorans Monooxygenase Catalyzed Asymmetric Epoxidation of Allyl Alcohol Derivatives and Hydroxylation of a Hypersensitive Radical Probe with the Radical Ring Opening Rate Exceeding the Oxygen Rebound Rate. J. Am. Chem. Soc. 1991, 113, 5878-5880.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5878-5880
    • Fu, H.1    Newcomb, M.2    Wong, C.-H.3
  • 52
    • 0033530861 scopus 로고    scopus 로고
    • Probing the radical mechanism of galactose oxidase using an ultrafast radical probe
    • Turner, B. E.; Branchaud, B. P. Probing the Radical Mechanism of Galactose Oxidase Using an Ultrafast Radical Probe. Bioorg. Med. Chem. Lett. 1999, 9, 3341-3346.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 3341-3346
    • Turner, B.E.1    Branchaud, B.P.2
  • 53
    • 0032487882 scopus 로고    scopus 로고
    • Dimethyldioxirane hydroxylation of a hypersensitive radical probe: Supporting evidence for an oxene insertion pathway
    • Simakov, P. A.; Choi, S. Y.; Newcomb, M. Dimethyldioxirane Hydroxylation of a Hypersensitive Radical Probe: Supporting Evidence for an Oxene Insertion Pathway. Tetrahedron Lett. 1998, 39, 8187-8190.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 8187-8190
    • Simakov, P.A.1    Choi, S.Y.2    Newcomb, M.3
  • 54
    • 0030043907 scopus 로고    scopus 로고
    • Hypersensitive radical probe studies of gif oxidations
    • Newcomb, M.; Simakov, P. A.; Park, S. U. Hypersensitive Radical Probe Studies of Gif Oxidations. Tetrahedron Lett. 1996, 37, 819-822.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 819-822
    • Newcomb, M.1    Simakov, P.A.2    Park, S.U.3
  • 56
    • 0000146962 scopus 로고
    • Mechanistic study of a synthetically useful monooxygenase model using the hypersensitive probe trans-2-phenyl-1-vinylcy-clopropane
    • Fu, H.; Look, G. C.; Zhang, W.; Jacobsen, E. N.; Wong, C.-H. Mechanistic Study of a Synthetically Useful Monooxygenase Model Using the Hypersensitive Probe trans-2-Phenyl-1-vinylcy-clopropane. J. Org. Chem. 1991, 56, 6497-6500.
    • (1991) J. Org. Chem. , vol.56 , pp. 6497-6500
    • Fu, H.1    Look, G.C.2    Zhang, W.3    Jacobsen, E.N.4    Wong, C.-H.5
  • 58
    • 0033521186 scopus 로고    scopus 로고
    • On the "Rebound" mechanism of alkane hydroxylation by cytochrome P450: Electronic structure of the intermediate and the electron-transfer character in the rebound step
    • Filatov, M.; Harris, N.; Shaik, S. On the "Rebound" Mechanism of Alkane Hydroxylation by Cytochrome P450: Electronic Structure of the Intermediate and the Electron-Transfer Character in the Rebound Step. Angew. Chem., Int. Ed. Engl. 1999, 38, 3510-3512.
    • (1999) Angew. Chem., Int. Ed. Engl. , vol.38 , pp. 3510-3512
    • Filatov, M.1    Harris, N.2    Shaik, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.