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Volumn 6, Issue 5, 2002, Pages 556-567

Two-state reactivity mechanisms of hydroxylation and epoxidation by cytochrome P-450 revealed by theory

Author keywords

[No Author keywords available]

Indexed keywords

ALKANE; ALKENE; CYTOCHROME P450; RADICAL;

EID: 0036802621     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(02)00363-0     Document Type: Review
Times cited : (316)

References (68)
  • 4
    • 0002229457 scopus 로고    scopus 로고
    • Cytochrome P-450: Significance, reaction mechanisms and active site analogues
    • Woggon W.-D. Cytochrome P-450: significance, reaction mechanisms and active site analogues. Top Curr Chem. 184:1996;40-96.
    • (1996) Top Curr Chem , vol.184 , pp. 40-96
    • Woggon, W.-D.1
  • 5
    • 0024294403 scopus 로고
    • Probing structure-function relations in heme-containing oxygenases and peroxidases
    • Dawson J.H. Probing structure-function relations in heme-containing oxygenases and peroxidases. Science. 240:1988;433-439.
    • (1988) Science , vol.240 , pp. 433-439
    • Dawson, J.H.1
  • 6
    • 0011697055 scopus 로고
    • Metalloporphyrins as versatile catalysts for oxidation reactions and oxidative DNA cleavage
    • Meunier B. Metalloporphyrins as versatile catalysts for oxidation reactions and oxidative DNA cleavage. Chem Rev. 92:1992;1411-1456.
    • (1992) Chem Rev , vol.92 , pp. 1411-1456
    • Meunier, B.1
  • 8
    • 0024429854 scopus 로고
    • Cytochrome P-450 catalysis: Radical intermediates and dehydrogenation reactions
    • Ortiz de Montellano P.R. Cytochrome P-450 catalysis: radical intermediates and dehydrogenation reactions. Trend Pharmacol Sci. 10:1989;354-359.
    • (1989) Trend Pharmacol Sci. , vol.10 , pp. 354-359
    • Ortiz de Montellano, P.R.1
  • 9
    • 33845282999 scopus 로고
    • Control of the catalytic activity of prosthetic heme by the structure hemoproteins
    • Ortiz de Montellano P.R. Control of the catalytic activity of prosthetic heme by the structure hemoproteins. Acc Chem Res. 20:1987;289-294.
    • (1987) Acc Chem Res , vol.20 , pp. 289-294
    • Ortiz de Montellano, P.R.1
  • 10
    • 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. 81:1978;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
  • 12
    • 0030979251 scopus 로고    scopus 로고
    • A new mechanistic probe for cytochrome P-450: An application of isotope effect profiles
    • Manchester J.I., Dinnocenzo J.P., Higgins L.A., Jones J.P. A new mechanistic probe for cytochrome P-450: An application of isotope effect profiles. J Am Chem Soc. 119:1997;5069-5070.
    • (1997) J Am Chem Soc , vol.119 , pp. 5069-5070
    • Manchester, J.I.1    Dinnocenzo, J.P.2    Higgins, L.A.3    Jones, J.P.4
  • 13
    • 0033623690 scopus 로고    scopus 로고
    • Hypersensitive radical probes and the mechanisms of cytochrome P-450 catalyzed hydroxylation reactions
    • Newcomb M., Toy P.H. Hypersensitive radical probes and the mechanisms of cytochrome P-450 catalyzed hydroxylation reactions. Acc Chem Res. 33:2000;449-455. The paper reviews the two-oxidant hypothesis for C-H hydroxylation by cytochrome P-450. Probe substrates that can distinguish between radical and cationic intermediates are discussed and lifetimes of radicals are quantified.
    • (2000) Acc Chem Res , vol.33 , pp. 449-455
    • Newcomb, M.1    Toy, P.H.2
  • 14
    • 0034728622 scopus 로고    scopus 로고
    • Cytochrome P-450-catalyzed hydroxylation of mechanistic probes that distinguish between radicals and cations. Evidence for cationic but not radical intermediates
    • Newcomb M., Shen R., Choi S.-Y., Toy P.H., Hollenberg P.F., Vaz A.D.N., Coon M.J. Cytochrome P-450-catalyzed hydroxylation of mechanistic probes that distinguish between radicals and cations. Evidence for cationic but not radical intermediates. J Am Chem Soc. 122:2000;2677-2686. Probe substrates that can distinguish between radical- and cationic-type reaction intermediates were used. Cationic rearrangement products were found. Radical lifetimes appear too short.
    • (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
  • 15
    • 0030004087 scopus 로고    scopus 로고
    • Peroxo-iron and xenoid-iron species as alternative oxygenating agents in cytochrome P-450-catalyzed reactions: Switching by threonine-302 to alanine mutagenesis of cytochrome P-450 2B4
    • Vaz A.D.N., Pernecky S.J., Raner G.M., Coon M.J. Peroxo-iron and xenoid-iron species as alternative oxygenating agents in cytochrome P-450-catalyzed reactions: switching by threonine-302 to alanine mutagenesis of cytochrome P-450 2B4. Proc Natl Acad Sci USA. 93:1996;4644-4648.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4644-4648
    • Vaz, A.D.N.1    Pernecky, S.J.2    Raner, G.M.3    Coon, M.J.4
  • 16
    • 0032584090 scopus 로고    scopus 로고
    • Epoxidation of olefins by cytochrome P-450: 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 P-450: evidence from site-specific mutagenesis for hydroperoxo-iron as an electrophilic oxidant. Proc Natl Acad Sci USA. 95:1998;3555-3560.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3555-3560
    • Vaz, A.D.N.1    McGinnity, D.F.2    Coon, M.J.3
  • 17
    • 0030763479 scopus 로고    scopus 로고
    • Reaction profile of the last step in cytochrome P-450 catalysis revealed by studies of model complexes
    • Gross Z., Nimri S., Barzilay C.M., Simkhovich I. Reaction profile of the last step in cytochrome P-450 catalysis revealed by studies of model complexes. J Biol Inorg Chem. 2:1997;492-506.
    • (1997) J Biol Inorg Chem , vol.2 , pp. 492-506
    • Gross, Z.1    Nimri, S.2    Barzilay, C.M.3    Simkhovich, I.4
  • 18
    • 33751158901 scopus 로고
    • Preparation and reactivity of oxoiron(IV) porphyrins
    • Groves J.T., Gross Z., Stern M.K. Preparation and reactivity of oxoiron(IV) porphyrins. Inorg Chem. 33:1994;5065-5072.
    • (1994) Inorg Chem , vol.33 , pp. 5065-5072
    • Groves, J.T.1    Gross, Z.2    Stern, M.K.3
  • 19
    • 0035800399 scopus 로고    scopus 로고
    • How does ethene inactivate cytochrome P-450 en route to its epoxidation? A density functional study
    • de Visser S.P., Ogliaro F., Shaik S. How does ethene inactivate cytochrome P-450 en route to its epoxidation? A density functional study. Angew Chem Int Ed Engl. 40:2001;2871-2874.
    • (2001) Angew Chem Int Ed Engl , vol.40 , pp. 2871-2874
    • De Visser, S.P.1    Ogliaro, F.2    Shaik, S.3
  • 20
    • 0034692380 scopus 로고    scopus 로고
    • A model "rebound" mechanism of hydroxylation by cytochrome P-450: A stepwise and effectively concerted pathways, and their reactivity patterns
    • Ogliaro F., Harris N., Cohen S., Filatov M., de Visser S.P., Shaik S. A model "rebound" mechanism of hydroxylation by cytochrome P-450: a stepwise and effectively concerted pathways, and their reactivity patterns. J Am Chem Soc. 122:2000;8977-8989. The mechanism of alkane hydroxylation by Cpd I was modelled using DFT calculations and found to occur via TSR on closely lying doublet and quartet spin surfaces. The doublet reaction leads to an effectively concerted process. The quartet reaction is truly stepwise. The obtained results were used to resolve the radical lifetime dilemma that has emerged from ultrafast radical clock experiments, and to make predictions of reactivity patterns.
    • (2000) J Am Chem Soc , vol.122 , pp. 8977-8989
    • Ogliaro, F.1    Harris, N.2    Cohen, S.3    Filatov, M.4    De Visser, S.P.5    Shaik, S.6
  • 21
    • 0034823190 scopus 로고    scopus 로고
    • Multi-state epoxidation of ethene by cytochrome P-450: A quantum chemical study
    • de Visser S.P., Ogliaro F., Harris N., Shaik S. Multi-state epoxidation of ethene by cytochrome P-450: a quantum chemical study. J Am Chem Soc. 123:2001;3037-3047. The mechanism of ethene epoxidation by Cpd I was modelled using DFT calculations. The reaction occurs via TSR with LS (doublet) or HS (quartet) spin surfaces and with species in which the iron has oxidation states Fe-III and Fe-IV. The LS process is effectively concerted. Experimental trends were discussed in the light of the results.
    • (2001) J Am Chem Soc , vol.123 , pp. 3037-3047
    • De Visser, S.P.1    Ogliaro, F.2    Harris, N.3    Shaik, S.4
  • 22
    • 0035929953 scopus 로고    scopus 로고
    • Stereospecific oxidation by Compound I of cytochrome P-450 does not proceed in a concerted synchronous manner
    • de Visser SP, Ogliaro F, Shaik S: Stereospecific oxidation by Compound I of cytochrome P-450 does not proceed in a concerted synchronous manner. Chem Commun 2001:2322-2323.
    • (2001) Chem Commun , pp. 2322-2323
    • De Visser, S.P.1    Ogliaro, F.2    Shaik, S.3
  • 23
    • 0034352128 scopus 로고    scopus 로고
    • Kinetic isotope effects in a C-H bond dissociation by the iron-oxo species of cytochrome P-450
    • Yoshizawa K., Kawaga Y., Shiota Y. Kinetic isotope effects in a C-H bond dissociation by the iron-oxo species of cytochrome P-450. J Phys Chem B. 104:2000;12365-12370.
    • (2000) J Phys Chem B , vol.104 , pp. 12365-12370
    • Yoshizawa, K.1    Kawaga, Y.2    Shiota, Y.3
  • 24
    • 0035840983 scopus 로고    scopus 로고
    • A theoretical study of the dynamic behavior of alkane hydroxylation by a Compound I model of cytochrome P-450
    • Yoshizawa K., Kamachi T., Shiota Y. A theoretical study of the dynamic behavior of alkane hydroxylation by a Compound I model of cytochrome P-450. J Am Chem Soc. 123:2001;9806-9816. The hydroxylation reaction of ethane by a Cpd I model was studied using DFT and molecular dynamics calculations. TSR was found. Trajectory calculations showed that the rebound step takes place in about 200 fs.
    • (2001) J Am Chem Soc , vol.123 , pp. 9806-9816
    • Yoshizawa, K.1    Kamachi, T.2    Shiota, Y.3
  • 25
    • 0025971479 scopus 로고
    • Chemistry of excited electronic states
    • Armentrout P.B. Chemistry of excited electronic states. Science. 251:1991;175-179.
    • (1991) Science , vol.251 , pp. 175-179
    • Armentrout, P.B.1
  • 27
    • 12044249154 scopus 로고
    • Electronic structures and gas-phase reactivities of cationic late transition-metal oxides
    • Fiedler A., Schröder D., Shaik S., Schwarz H. Electronic structures and gas-phase reactivities of cationic late transition-metal oxides. J Am Chem Soc. 116:1994;10734-10741.
    • (1994) J Am Chem Soc , vol.116 , pp. 10734-10741
    • Fiedler, A.1    Schröder, D.2    Shaik, S.3    Schwarz, H.4
  • 30
    • 0030936842 scopus 로고    scopus 로고
    • +. Selection rules and reactivity effects
    • +. Selection rules and reactivity effects. J Am Chem Soc. 119:1997;1773-1786.
    • (1997) J Am Chem Soc , vol.119 , pp. 1773-1786
    • Danovich, D.1    Shaik, S.2
  • 33
    • 0001753248 scopus 로고    scopus 로고
    • +: Addition-elimination, 'rebound' and oxene-insertion mechanisms
    • +: addition-elimination, 'rebound' and oxene-insertion mechanisms. J Phys Chem A. 102:1998;3835-3846.
    • (1998) J Phys Chem A , vol.102 , pp. 3835-3846
    • Filatov, M.1    Shaik, S.2
  • 35
    • 0037742151 scopus 로고    scopus 로고
    • Two-state reactivity as a new concept in organometallic chemistry
    • Schröder D., Shaik S., Schwarz H. Two-state reactivity as a new concept in organometallic chemistry. Acc Chem Res. 33:2000;139-145. The TSR phenomenon is defined in this paper and its effects and applicability are discussed for a variety of reactions. TSR is proposed as a new general paradigm in organometallic chemistry.
    • (2000) Acc Chem Res , vol.33 , pp. 139-145
    • Schröder, D.1    Shaik, S.2    Schwarz, H.3
  • 36
    • 0031979212 scopus 로고    scopus 로고
    • Electronic structure makes a difference: Cytochrome mediated hydroxylations of hydrocarbons as a two-state reactivity paradigm
    • Shaik S., Filatov M., Schröder D., Schwarz H. Electronic structure makes a difference: cytochrome mediated hydroxylations of hydrocarbons as a two-state reactivity paradigm. Chem Eur J. 4:1998;193-199.
    • (1998) Chem Eur J , vol.4 , pp. 193-199
    • Shaik, S.1    Filatov, M.2    Schröder, D.3    Schwarz, H.4
  • 37
    • 0034595865 scopus 로고    scopus 로고
    • Two-state reactivity in the rebound step of alkane hydroxylation by cytochrome P-450: Origins of free radicals with finite lifetime
    • Harris N., Cohen S., Filatov M., Ogliaro F., Shaik S. Two-state reactivity in the rebound step of alkane hydroxylation by cytochrome P-450: origins of free radicals with finite lifetime. Angew Chem Int Ed Engl. 39:2000;2003-2007. DFT calculations on the rebound step of the methane hydroxylation by Cpd I show a HS process with a significant barrier and a LS process that is virtually barrierless.
    • (2000) Angew Chem Int Ed Engl , vol.39 , pp. 2003-2007
    • Harris, N.1    Cohen, S.2    Filatov, M.3    Ogliaro, F.4    Shaik, S.5
  • 38
    • 0000767074 scopus 로고    scopus 로고
    • Role of the heme active site and protein environment in structure, spectra and function of the cytochrome P-450s
    • Loew G.H., Harris D.L. Role of the heme active site and protein environment in structure, spectra and function of the cytochrome P-450s. Chem Rev. 100:2000;407-419.
    • (2000) Chem Rev , vol.100 , pp. 407-419
    • Loew, G.H.1    Harris, D.L.2
  • 40
    • 0035606245 scopus 로고    scopus 로고
    • High-valent intermediates of heme proteins and model compounds
    • Harris D.L. High-valent intermediates of heme proteins and model compounds. Curr Opin Chem Biol. 5:2001;724-735. This review discusses the latest theoretical developments in understanding Cpd I, the oxo-iron porphyrin active species of heme protein enzymes and its reactivity.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 724-735
    • Harris, D.L.1
  • 41
    • 0034602030 scopus 로고    scopus 로고
    • The high-valent compound of Cytochrome P-450: The nature of the Fe-S bond and the role of the thiolate ligand as an internal electron donor
    • Ogliaro F., Cohen S., Filatov M., Harris N., Shaik S. The high-valent compound of Cytochrome P-450: the nature of the Fe-S bond and the role of the thiolate ligand as an internal electron donor. Angew Chem Int Ed Engl. 39:2000;3851-3855.
    • (2000) Angew Chem Int Ed Engl , vol.39 , pp. 3851-3855
    • Ogliaro, F.1    Cohen, S.2    Filatov, M.3    Harris, N.4    Shaik, S.5
  • 42
    • 0034723020 scopus 로고    scopus 로고
    • Medium polarization and hydrogen bonding effects on Compound I of cytochrome P-450: What kind of radical is it really?
    • Ogliaro F., Cohen S., de Visser S.P., Shaik S. Medium polarization and hydrogen bonding effects on Compound I of cytochrome P-450: what kind of radical is it really? J Am Chem Soc. 122:2000;12892-12893.
    • (2000) J Am Chem Soc , vol.122 , pp. 12892-12893
    • Ogliaro, F.1    Cohen, S.2    De Visser, S.P.3    Shaik, S.4
  • 43
    • 0037014038 scopus 로고    scopus 로고
    • Hydrogen bonding modulates the selectivity of enzymatic oxidation by P-450: A chameleon oxidant behavior by Compound I
    • de Visser S.P., Ogliaro F., Sharma P.K., Shaik S. Hydrogen bonding modulates the selectivity of enzymatic oxidation by P-450: a chameleon oxidant behavior by Compound I. Angew Chem Int Ed Engl. 41:2002;1947-1951.
    • (2002) Angew Chem Int Ed Engl , vol.41 , pp. 1947-1951
    • De Visser, S.P.1    Ogliaro, F.2    Sharma, P.K.3    Shaik, S.4
  • 44
    • 0033669428 scopus 로고    scopus 로고
    • Alkane hydroxylation by Cytochrome P-450: Is kinetic isotope effect a reliable probe of a transition state structure
    • Ogliaro F, Filatov M, Shaik S: Alkane hydroxylation by Cytochrome P-450: is kinetic isotope effect a reliable probe of a transition state structure. Eur J Inorg Chem 2000:2455-2458. KIE studies on the hydrogen abstraction step in the hydroxylation reaction of methane were performed and gave good agreement with experimental values for similar hydrogen abstraction reactions. The mechanistic implications vis-à-vis KIE effects on rearrangement of Newcomb's probe substrates was discussed.
    • (2000) Eur J Inorg Chem , pp. 2455-2458
    • Ogliaro, F.1    Filatov, M.2    Shaik, S.3
  • 45
    • 0001349992 scopus 로고
    • Intramolecular kinetic isotope effects in alkane hydroxylation catalyzed by manganese and iron porphyrin complexes
    • Sorokin A., Robert A., Meunier B. Intramolecular kinetic isotope effects in alkane hydroxylation catalyzed by manganese and iron porphyrin complexes. J Am Chem Soc. 115:1993;7293-7299.
    • (1993) J Am Chem Soc , vol.115 , pp. 7293-7299
    • Sorokin, A.1    Robert, A.2    Meunier, B.3
  • 48
    • 0000850713 scopus 로고
    • Mechanism of alkene epoxidation by iron, chromium, and manganese higher valent oxo-metalloporphyrins
    • Ostovic D., Bruice T.C. Mechanism of alkene epoxidation by iron, chromium, and manganese higher valent oxo-metalloporphyrins. Acc Chem Res. 25:1992;314-320.
    • (1992) Acc Chem Res , vol.25 , pp. 314-320
    • Ostovic, D.1    Bruice, T.C.2
  • 49
    • 0037009994 scopus 로고    scopus 로고
    • What factors affect the regioselectivity of oxidation by cytochrome P450? A DFT study of allylic hydroxylation and double bond epoxidation in a model reaction
    • in press
    • de Visser SP, Ogliaro F, Sharma PK, Shaik S: What factors affect the regioselectivity of oxidation by cytochrome P450? A DFT study of allylic hydroxylation and double bond epoxidation in a model reaction. J Am Chem Soc 2002, 124:in press.
    • (2002) J Am Chem Soc , pp. 124
    • De Visser, S.P.1    Ogliaro, F.2    Sharma, P.K.3    Shaik, S.4
  • 50
    • 0033521186 scopus 로고    scopus 로고
    • On the "rebound" mechanism of alkane hydroxylation by cytochrome P-450: 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 P-450: electronic structure of the intermediate and the electron transfer character in the rebound step. Angew Chem Int Ed Engl. 38:1999;3510-3512.
    • (1999) Angew Chem Int Ed Engl , vol.38 , pp. 3510-3512
    • Filatov, M.1    Harris, N.2    Shaik, S.3
  • 51
    • 0028085491 scopus 로고
    • Cytochrome P-450-catalyzed hydroxylation of hydrocarbones: 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 P-450-catalyzed hydroxylation of hydrocarbones: kinetic deuterium isotope effects for the hydroxylation of an ultrafast radical clock. Biochemistry. 33:1994;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
  • 55
    • 0001851317 scopus 로고    scopus 로고
    • The role of the proximal ligand in heme enzymes
    • Poulos T.L. The role of the proximal ligand in heme enzymes. J Biol Inorg Chem. 1:1996;356-359.
    • (1996) J Biol Inorg Chem , vol.1 , pp. 356-359
    • Poulos, T.L.1
  • 56
    • 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. 120:1998;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
  • 58
    • 33845375582 scopus 로고
    • Oxygen transfer from iron oxo porphyrins to ethylene. A semiempirical MO/VB approach
    • Sevin A., Fontecave F. Oxygen transfer from iron oxo porphyrins to ethylene. A semiempirical MO/VB approach. J Am Chem Soc. 108:1986;3266-3272.
    • (1986) J Am Chem Soc , vol.108 , pp. 3266-3272
    • Sevin, A.1    Fontecave, F.2
  • 59
    • 0030866328 scopus 로고    scopus 로고
    • Oxene vs non-oxene reactive intermediates in iron(III) porphyrin catalyzed oxidation reactions: Organometallic compounds as diagnostic probes
    • Kamaraj K., Bandyopadhyay D. Oxene vs non-oxene reactive intermediates in iron(III) porphyrin catalyzed oxidation reactions: Organometallic compounds as diagnostic probes. J Am Chem Soc. 119:1997;8099-8100.
    • (1997) J Am Chem Soc , vol.119 , pp. 8099-8100
    • Kamaraj, K.1    Bandyopadhyay, D.2
  • 60
    • 0037139511 scopus 로고    scopus 로고
    • Searching for the second oxidant in the catalytic cycle of cytochrome P-450: A theoretical investigation of the iron(III)-hydroperoxo species and its epoxidation pathways
    • Ogliaro F., de Visser S.P., Cohen S., Sharma P.K., Shaik S. Searching for the second oxidant in the catalytic cycle of cytochrome P-450: a theoretical investigation of the iron(III)-hydroperoxo species and its epoxidation pathways. J Am Chem Soc. 124:2002;2806-2817.
    • (2002) J Am Chem Soc , vol.124 , pp. 2806-2817
    • Ogliaro, F.1    De Visser, S.P.2    Cohen, S.3    Sharma, P.K.4    Shaik, S.5
  • 61
    • 0037140738 scopus 로고    scopus 로고
    • Revisiting the mechanism of P-450 enzymes using the radical clocks norcarane and spiro[2,5]octane
    • Auclaire K., Hu Z., Little D.M., Ortiz de Montellano P.R., Groves J.T. Revisiting the mechanism of P-450 enzymes using the radical clocks norcarane and spiro[2,5]octane. J Am Chem Soc. 124:2002;6020-6027. Hydroxylation reactions of norcarane and spiro[2.5]octane were studied with different P-450 isozymes. The amount of radical intermediates behaves according to the prediction of the TSR scenario. Alternative cationic intermediates were only observed in trace amounts with norcarane.
    • (2002) J Am Chem Soc , vol.124 , pp. 6020-6027
    • Auclaire, K.1    Hu, Z.2    Little, D.M.3    Ortiz de Montellano, P.R.4    Groves, J.T.5
  • 63
    • 0035984571 scopus 로고    scopus 로고
    • Oxidizing species in the mechanism of Cytochrome P-450
    • Ortiz de Montellano P.R., De Vos J.J. Oxidizing species in the mechanism of Cytochrome P-450. Nat Prod Rep. 19:2002;1-18. The review discusses the mechanism of oxygen activation by P-450, the catalytic roles of the various iron-oxygen species formed in the catalytic cycle of the enzyme, and the progress achieved in understanding of the mechanisms of the various monooxygenation reactions. Data for alkane hydroxylation and alkene epoxidation are discussed also in terms of TSR.
    • (2002) Nat Prod Rep , vol.19 , pp. 1-18
    • Ortiz de Montellano, P.R.1    De Vos, J.J.2
  • 64
    • 0037055032 scopus 로고    scopus 로고
    • The elusive oxidant species of cytochrome P-450 enzymes: Characterization by combined quantum mechanical/molecular mechanical (QM/MM) calculations
    • Schöneboom J.C., Lin H., Reuter N., Thiel W., Cohen S., Ogliaro F., Shaik S. The elusive oxidant species of cytochrome P-450 enzymes: characterization by combined quantum mechanical/molecular mechanical (QM/MM) calculations. J Am Chem Soc. 124:2002;8142-8151.
    • (2002) J Am Chem Soc , vol.124 , pp. 8142-8151
    • Schöneboom, J.C.1    Lin, H.2    Reuter, N.3    Thiel, W.4    Cohen, S.5    Ogliaro, F.6    Shaik, S.7
  • 65
    • 0034739018 scopus 로고    scopus 로고
    • Roles of the axial push effect in cytochrome P-450cam studied with the site-directed mutagenesis at the heme proximal site
    • Yoshioka S., Takahashi S., Ishimori K., Morishima I. Roles of the axial push effect in cytochrome P-450cam studied with the site-directed mutagenesis at the heme proximal site. J Inorg Biochem. 81:2000;141-151.
    • (2000) J Inorg Biochem , vol.81 , pp. 141-151
    • Yoshioka, S.1    Takahashi, S.2    Ishimori, K.3    Morishima, I.4
  • 66
    • 0037151588 scopus 로고    scopus 로고
    • Evidence for two different active oxygen species in cytochrome P-450 BM3 mediated sulfoxidation and N-dealkylation reactions
    • in press
    • Volz TJ, Rock DA, Jones JP: Evidence for two different active oxygen species in cytochrome P-450 BM3 mediated sulfoxidation and N-dealkylation reactions. J Am Chem Soc 2002, 124:in press.
    • (2002) J Am Chem Soc , vol.124
    • Volz, T.J.1    Rock, D.A.2    Jones, J.P.3
  • 67
    • 0035925164 scopus 로고    scopus 로고
    • Hydroxylation of camphor by reduced oxy-cytochrome P-450cam: Mechanistic implications of EPR and ENDOR studies of catalytic intermediates in native and mutant enzymes
    • Davydov R., Markis T.M., Kofman V., Werst D.E., Sligar S.G., Hoffman B.M. Hydroxylation of camphor by reduced oxy-cytochrome P-450cam: mechanistic implications of EPR and ENDOR studies of catalytic intermediates in native and mutant enzymes. J Am Chem Soc. 123:2001;1413-1415.
    • (2001) J Am Chem Soc , vol.123 , pp. 1413-1415
    • Davydov, R.1    Markis, T.M.2    Kofman, V.3    Werst, D.E.4    Sligar, S.G.5    Hoffman, B.M.6
  • 68
    • 0037013634 scopus 로고    scopus 로고
    • Experimental evidence for multiple oxidation pathways in the (salen) Mn-catalyzed epoxidation of alkenes
    • Linde C., Kolinï N., Norbby P.-O., Åkermark B. Experimental evidence for multiple oxidation pathways in the (salen) Mn-catalyzed epoxidation of alkenes. Chem Eur J. 8:2002;2568-2573.
    • (2002) Chem Eur J , vol.8 , pp. 2568-2573
    • Linde, C.1    Kolinï, N.2    Norbby, P.-O.3    Åkermark, B.4


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