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Volumn 338, Issue 1, 2005, Pages 355-364

Freeze-quenched iron-oxo intermediates in cytochromes P450

Author keywords

Compound I; M ssbauer spectroscopy; Multifrequency EPR; Radicals; Rapid mixing freeze quench; Thiolate heme proteins

Indexed keywords

CHLORIDE PEROXIDASE; CYTOCHROME P450; HEMOPROTEIN; HYDROGEN PEROXIDE; NITRIC OXIDE SYNTHASE; OXYGEN; PORPHYRIN DERIVATIVE; RADICAL; TRYPTOPHAN; TYROSINE;

EID: 27544510321     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.166     Document Type: Review
Times cited : (31)

References (63)
  • 2
    • 0345275779 scopus 로고    scopus 로고
    • A passion for P450s (Remembrance of the early history of research on cytochrome P450)
    • R.W. Estabrook A passion for P450s (Remembrance of the early history of research on cytochrome P450) Drug Metab. Dispos. 31 2003 1461 1473
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 1461-1473
    • Estabrook, R.W.1
  • 3
    • 0001202995 scopus 로고
    • Pigments of rat liver microsomes
    • M. Klingenberg Pigments of rat liver microsomes Arch. Biochem. Biophys. 75 1958 376 386
    • (1958) Arch. Biochem. Biophys. , vol.75 , pp. 376-386
    • Klingenberg, M.1
  • 4
    • 0001718982 scopus 로고
    • Studies on pig liver microsomes. I. Enzymic and pigment composition of different microsomal fractions
    • D. Garfinkel Studies on pig liver microsomes. I. Enzymic and pigment composition of different microsomal fractions Arch. Biochem. Biophys. 77 1958 493 509
    • (1958) Arch. Biochem. Biophys. , vol.77 , pp. 493-509
    • Garfinkel, D.1
  • 5
    • 0001045385 scopus 로고
    • A new cytochrome in liver microsomes
    • T. Omura, and R. Sato A new cytochrome in liver microsomes J. Biol. Chem. 237 1964 PC1375 PC1376
    • (1964) J. Biol. Chem. , vol.237
    • Omura, T.1    Sato, R.2
  • 6
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for hemeprotein nature
    • T. Omura, and R. Sato The carbon monoxide-binding pigment of liver microsomes. I. Evidence for hemeprotein nature J. Biol. Chem. 239 1964 2370 2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 7
    • 42449157733 scopus 로고    scopus 로고
    • Models and mechanisms of cytochrome P450 action
    • P.R. Ortiz de Montellano Kluwer Academic/Plenum New York
    • J.T. Groves Models and mechanisms of cytochrome P450 action P.R. Ortiz de Montellano Cytochrome P450, Structure, Mechanism, and Biochemistry 2005 Kluwer Academic/Plenum New York 1 43
    • (2005) Cytochrome P450, Structure, Mechanism, and Biochemistry , pp. 1-43
    • Groves, J.T.1
  • 8
    • 0036197490 scopus 로고    scopus 로고
    • Electronic structure and reactivity of high-valent oxo iron porphyrins
    • H. Fujii Electronic structure and reactivity of high-valent oxo iron porphyrins Coord. Chem. Rev. 226 2002 51 60
    • (2002) Coord. Chem. Rev. , vol.226 , pp. 51-60
    • Fujii, H.1
  • 9
    • 0242562608 scopus 로고    scopus 로고
    • Intermediates in the reaction of substrate-free cytochrome P450cam with peroxy acetic acid
    • V. Schünemann, C. Jung, A.X. Trautwein, D. Mandon, and R. Weiss Intermediates in the reaction of substrate-free cytochrome P450cam with peroxy acetic acid FEBS Lett. 479 2000 149 154
    • (2000) FEBS Lett. , vol.479 , pp. 149-154
    • Schünemann, V.1    Jung, C.2    Trautwein, A.X.3    Mandon, D.4    Weiss, R.5
  • 11
    • 27544512458 scopus 로고
    • Model systems in studies of the chemistry and the enzymatic activation of oxygen
    • B.B. Brodie J.R. Gillette H.S. Ackermann Springer-Verlag Berlin, New york
    • V. Ullrich, and H.J. Staudinger Model systems in studies of the chemistry and the enzymatic activation of oxygen B.B. Brodie J.R. Gillette H.S. Ackermann Handbuch der Experimentellen Pharmakologie Vol. 28/2 1971 Springer-Verlag Berlin, New york 251 263
    • (1971) Handbuch der Experimentellen Pharmakologie , vol.28 , Issue.2 , pp. 251-263
    • Ullrich, V.1    Staudinger, H.J.2
  • 14
    • 0021766658 scopus 로고
    • Chloroperoxidase compound I: Electron paramagnetic resonance and Mössbauer studies
    • R. Rutter, L.P. Hager, H. Dhonau, M. Hendrich, M. Valentine, and P. Debrunner Chloroperoxidase compound I: electron paramagnetic resonance and Mössbauer studies Biochemistry 23 1984 6809 6816
    • (1984) Biochemistry , vol.23 , pp. 6809-6816
    • Rutter, R.1    Hager, L.P.2    Dhonau, H.3    Hendrich, M.4    Valentine, M.5    Debrunner, P.6
  • 16
    • 0036194077 scopus 로고    scopus 로고
    • Resonance Raman spectra and biological significance of high-valent iron(IV,V) porphyrins
    • K. Nakamoto Resonance Raman spectra and biological significance of high-valent iron(IV,V) porphyrins Coord. Chem. Rev. 226 2002 153 165
    • (2002) Coord. Chem. Rev. , vol.226 , pp. 153-165
    • Nakamoto, K.1
  • 17
    • 2942679678 scopus 로고    scopus 로고
    • Oxoiron(IV) in chloroperoxidase compound II is basic: Implication for P450 chemistry
    • M.T. Green, J.H. Dawson, and H.B. Gray Oxoiron(IV) in chloroperoxidase compound II is basic: implication for P450 chemistry Science 304 2004 1653 1656
    • (2004) Science , vol.304 , pp. 1653-1656
    • Green, M.T.1    Dawson, J.H.2    Gray, H.B.3
  • 18
    • 0028144935 scopus 로고
    • Evidence for Compound I formation in the reaction of cytochrome P450cam with m-chloroperbenzoic acid
    • T. Egawa, H. Shimada, and Y. Ishimura Evidence for Compound I formation in the reaction of cytochrome P450cam with m-chloroperbenzoic acid Biochem. Biophys. Res. Commun. 201 1994 1464 1469
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 1464-1469
    • Egawa, T.1    Shimada, H.2    Ishimura, Y.3
  • 19
    • 0037155911 scopus 로고    scopus 로고
    • Kinetic characterization of compound I formation in the thermostable cytochrome P450 CYP119
    • D.G. Kellner, S.-C. Hung, K.E. Weiss, and S.G. Sligar Kinetic characterization of compound I formation in the thermostable cytochrome P450 CYP119 J. Biol. Chem. 277 2002 9641 9644
    • (2002) J. Biol. Chem. , vol.277 , pp. 9641-9644
    • Kellner, D.G.1    Hung, S.-C.2    Weiss, K.E.3    Sligar, S.G.4
  • 21
    • 0021102305 scopus 로고
    • Absorption spectra of cytochrome P450cam in the reaction with peroxy acids
    • G.C. Wagner, M.M. Palcic, and H.B. Dunford Absorption spectra of cytochrome P450cam in the reaction with peroxy acids FEBS Lett. 156 1983 244 248
    • (1983) FEBS Lett. , vol.156 , pp. 244-248
    • Wagner, G.C.1    Palcic, M.M.2    Dunford, H.B.3
  • 22
    • 1642477668 scopus 로고
    • Oxygen reactions of the P450 heme protein
    • V. Ullrich I. Roots A. Hildebrandt R.W. Estabrook Pergamon Oxford
    • S.G. Sligar, B.S. Shastry, and I.C. Gunsalus Oxygen reactions of the P450 heme protein V. Ullrich I. Roots A. Hildebrandt R.W. Estabrook Microsomes and Drug Oxidations 1977 Pergamon Oxford 202 209
    • (1977) Microsomes and Drug Oxidations , pp. 202-209
    • Sligar, S.G.1    Shastry, B.S.2    Gunsalus, I.C.3
  • 23
    • 0345743593 scopus 로고    scopus 로고
    • Substrate modulate compound I formation in peroxide shunt pathway of Pseudomonas putida cytochrome P450cam
    • S. Prasad, and S. Mitra Substrate modulate compound I formation in peroxide shunt pathway of Pseudomonas putida cytochrome P450cam Biochem. Biophys. Res. Commun. 314 2004 610 614
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 610-614
    • Prasad, S.1    Mitra, S.2
  • 24
    • 20144385036 scopus 로고    scopus 로고
    • Reaction of ferric cytochrome P450cam with peracids: Kinetic characterization of intermediates on the reaction pathway
    • T. Spolitak, J.H. Dawson, and D.P. Ballou Reaction of ferric cytochrome P450cam with peracids: Kinetic characterization of intermediates on the reaction pathway J. Biol. Chem. 280 2005 20300 20309
    • (2005) J. Biol. Chem. , vol.280 , pp. 20300-20309
    • Spolitak, T.1    Dawson, J.H.2    Ballou, D.P.3
  • 25
    • 0037145077 scopus 로고    scopus 로고
    • Spectroscopic studies of peroxyacetic acid reaction intermediate of cytochrome P450cam and chloroperoxidase
    • V. Schünemann, C. Jung, J. Terner, A.X. Trautwein, and R. Weiss Spectroscopic studies of peroxyacetic acid reaction intermediate of cytochrome P450cam and chloroperoxidase J. Inorg. Biochem. 91 2002 586 596
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 586-596
    • Schünemann, V.1    Jung, C.2    Terner, J.3    Trautwein, A.X.4    Weiss, R.5
  • 28
    • 1642483708 scopus 로고    scopus 로고
    • Tyrosine radical formation in the reaction of wild type and mutant cytochrome P450cam with peroxy acids: A multifrequency EPR study of intermediates on the millisecond time scale
    • V. Schünemann, F. Lendzian, C. Jung, J. Contzen, A.-L. Barra, S.G. Sligar, and A.X. Trautwein Tyrosine radical formation in the reaction of wild type and mutant cytochrome P450cam with peroxy acids: a multifrequency EPR study of intermediates on the millisecond time scale J. Biol. Chem. 279 2004 10919 10930
    • (2004) J. Biol. Chem. , vol.279 , pp. 10919-10930
    • Schünemann, V.1    Lendzian, F.2    Jung, C.3    Contzen, J.4    Barra, A.-L.5    Sligar, S.G.6    Trautwein, A.X.7
  • 29
    • 0011267032 scopus 로고
    • Cytochrome P450: Structure and states
    • H.B. Dunford Reidel Dordrecht
    • G.C. Wagner, and I.C. Gunsalus Cytochrome P450: Structure and states H.B. Dunford The Biological Chemistry of Iron 1982 Reidel Dordrecht 405 412
    • (1982) The Biological Chemistry of Iron , pp. 405-412
    • Wagner, G.C.1    Gunsalus, I.C.2
  • 31
    • 0242414727 scopus 로고    scopus 로고
    • Protein-based radicals in the catalase-peroxidase of synechocystis PCC6803: A multifrequency EPR investigation of wild-type and variants on the environment of the heme active site
    • A. Ivancich, C. Jakopitsch, M. Auer, S. Un, and C. Obinger Protein-based radicals in the catalase-peroxidase of synechocystis PCC6803: a multifrequency EPR investigation of wild-type and variants on the environment of the heme active site J. Am. Chem. Soc. 125 2003 14093 14102
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14093-14102
    • Ivancich, A.1    Jakopitsch, C.2    Auer, M.3    Un, S.4    Obinger, C.5
  • 32
    • 13844298688 scopus 로고    scopus 로고
    • Structure and interactions of amino acid radicals in class I ribonucleotide reductase studied by ENDOR and high-field EPR spectroscopy
    • F. Lendzian Structure and interactions of amino acid radicals in class I ribonucleotide reductase studied by ENDOR and high-field EPR spectroscopy Biochim. Biophys. Acta 1707 2005 67 90
    • (2005) Biochim. Biophys. Acta , vol.1707 , pp. 67-90
    • Lendzian, F.1
  • 33
    • 0035849509 scopus 로고    scopus 로고
    • Comparative electron paramagnetic resonance study of radical intermediates in turnip peroxidase isozymes
    • A. Ivancich, G. Mazza, and A. Desbois Comparative electron paramagnetic resonance study of radical intermediates in turnip peroxidase isozymes Biochemistry 40 2001 6860 6866
    • (2001) Biochemistry , vol.40 , pp. 6860-6866
    • Ivancich, A.1    Mazza, G.2    Desbois, A.3
  • 34
    • 0033597610 scopus 로고    scopus 로고
    • Effect of protein microenvironment on tyrosyl radicals. a high-field (285-GHz) EPR, resonance Raman, and hybrid density functional study
    • A. Ivancich, T.A. Mattioli, and S. Un Effect of protein microenvironment on tyrosyl radicals. A high-field (285-GHz) EPR, resonance Raman, and hybrid density functional study J. Am. Chem. Soc. 121 1999 5743 5753
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5743-5753
    • Ivancich, A.1    Mattioli, T.A.2    Un, S.3
  • 35
    • 0029904196 scopus 로고    scopus 로고
    • Electron magnetic resonance of the tyrosyl radical in ribonucleotide reductase from Escherichia coli
    • C.W. Hoganson, M. Sahlin, B.-M. Sjöberg, and G.T. Babcock Electron magnetic resonance of the tyrosyl radical in ribonucleotide reductase from Escherichia coli J. Am. Chem. Soc. 118 1996 4672 4679
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 4672-4679
    • Hoganson, C.W.1    Sahlin, M.2    Sjöberg, B.-M.3    Babcock, G.T.4
  • 36
    • 0343035716 scopus 로고    scopus 로고
    • Density functional calculations on model tyrosyl radicals
    • F. Himo, A. Gräslund, and L.A. Eriksson Density functional calculations on model tyrosyl radicals Biophys. J. 72 1997 1556 1567
    • (1997) Biophys. J. , vol.72 , pp. 1556-1567
    • Himo, F.1    Gräslund, A.2    Eriksson, L.A.3
  • 38
    • 0001877970 scopus 로고
    • Iron-containing proteins and related analogs-complementary Mössbauer, EPR and magnetic susceptibility studies
    • A.X. Trautwein, E. Bill, E.L. Bominaar, and H. Winkler Iron-containing proteins and related analogs-complementary Mössbauer, EPR and magnetic susceptibility studies Struct. Bond. 78 1991 1 95
    • (1991) Struct. Bond. , vol.78 , pp. 1-95
    • Trautwein, A.X.1    Bill, E.2    Bominaar, E.L.3    Winkler, H.4
  • 39
    • 1842637859 scopus 로고    scopus 로고
    • Cytochrome P450: An investigation of the Mössbauer spectra of a reaction intermediate and an Fe(IV)O model system
    • Y. Zhang, and E. Oldfield Cytochrome P450: an investigation of the Mössbauer spectra of a reaction intermediate and an Fe(IV)O model system J. Am. Chem. Soc. 126 2004 4470 4471
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4470-4471
    • Zhang, Y.1    Oldfield, E.2
  • 40
    • 0342617660 scopus 로고    scopus 로고
    • Mobility of norbornane-type substrates and water accessibility in cytochrome P-450cam
    • H. Schulze, G. Hui Bon Hoa, and C. Jung Mobility of norbornane-type substrates and water accessibility in cytochrome P-450cam Biochim. Biophys. Acta 1338 1997 77 92
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 77-92
    • Schulze, H.1    Hui Bon Hoa, G.2    Jung, C.3
  • 41
  • 42
    • 0030014679 scopus 로고    scopus 로고
    • The flavoprotein domain of P450BM-3: Expression, purification, and properties of the flavin adenine dinucleotide- and flavin mononucleotide-binding subdomains
    • I.F. Sevrioukova, G. Truan, and J.A. Peterson The flavoprotein domain of P450BM-3: expression, purification, and properties of the flavin adenine dinucleotide- and flavin mononucleotide-binding subdomains Biochemistry 35 1996 7528 7535
    • (1996) Biochemistry , vol.35 , pp. 7528-7535
    • Sevrioukova, I.F.1    Truan, G.2    Peterson, J.A.3
  • 43
    • 0031569880 scopus 로고    scopus 로고
    • Reconstitution of the fatty acid hydroxylase activity of cytochrome P450BM-3 utilizing its functional domains
    • I.F. Sevrioukova, G. Truan, and J.A. Peterson Reconstitution of the fatty acid hydroxylase activity of cytochrome P450BM-3 utilizing its functional domains Arch. Biochem. Biophys. 340 1997 231 238
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 231-238
    • Sevrioukova, I.F.1    Truan, G.2    Peterson, J.A.3
  • 44
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • K. Alderton, C.E. Cooper, and R.G. Knowles Nitric oxide synthases: structure, function and inhibition Biochem. J. 357 2001 593 615
    • (2001) Biochem. J. , vol.357 , pp. 593-615
    • Alderton, K.1    Cooper, C.E.2    Knowles, R.G.3
  • 46
    • 0018992114 scopus 로고
    • Differences in the mechanism of NADPH- and cumene hydroperoxide-supported reactions of cytochrome P-450
    • J. Capdevila, R.W. Estabrook, and R.A. Prough Differences in the mechanism of NADPH- and cumene hydroperoxide-supported reactions of cytochrome P-450 Arch. Biochem. Biophys. 200 1980 186 195
    • (1980) Arch. Biochem. Biophys. , vol.200 , pp. 186-195
    • Capdevila, J.1    Estabrook, R.W.2    Prough, R.A.3
  • 47
    • 0020484831 scopus 로고
    • Destruction of cytochrome P-450 by vinyl fluoride, fluroxene, and acetyl. Evidence for a radical intermediate in olefin oxidation
    • P.R. Ortiz de Montellano, K.L. Kunze, H.S. Beilan, and C. Wheeler Destruction of cytochrome P-450 by vinyl fluoride, fluroxene, and acetyl. Evidence for a radical intermediate in olefin oxidation Biochemistry 21 1982 1331 1339
    • (1982) Biochemistry , vol.21 , pp. 1331-1339
    • Ortiz De Montellano, P.R.1    Kunze, K.L.2    Beilan, H.S.3    Wheeler, C.4
  • 48
    • 0025179693 scopus 로고
    • On the nature of the cytochrome P450scc "ultimative oxidant": Characterization of a productive radical intermediate
    • C. Larroque, R. Lange, L. Maurin, A. Bienvenue, and J.E. van Lier On the nature of the cytochrome P450scc "ultimative oxidant": characterization of a productive radical intermediate Arch. Biochem. Biophys. 282 1990 198 201
    • (1990) Arch. Biochem. Biophys. , vol.282 , pp. 198-201
    • Larroque, C.1    Lange, R.2    Maurin, L.3    Bienvenue, A.4    Van Lier, J.E.5
  • 49
    • 0024473758 scopus 로고
    • Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES
    • M. Sivaraja, D.B. Goodin, M. Smith, and B.M. Hoffman Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES Science 245 1989 738 740
    • (1989) Science , vol.245 , pp. 738-740
    • Sivaraja, M.1    Goodin, D.B.2    Smith, M.3    Hoffman, B.M.4
  • 50
    • 3042853026 scopus 로고    scopus 로고
    • Electrostatic control of the tryptophan radical in cytochrome c peroxidase
    • T.P. Barrows, B. Bhaskar, and T.L. Poulos Electrostatic control of the tryptophan radical in cytochrome c peroxidase Biochemistry 43 2004 8826 8834
    • (2004) Biochemistry , vol.43 , pp. 8826-8834
    • Barrows, T.P.1    Bhaskar, B.2    Poulos, T.L.3
  • 52
    • 0030455403 scopus 로고    scopus 로고
    • EPR evidence for a tyrosyl radical intermediate in bovine liver catalase
    • A. Ivancich, H.M. Joue, and J. Gaillard EPR evidence for a tyrosyl radical intermediate in bovine liver catalase J. Am. Chem. Soc. 118 1996 12852 12853
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12852-12853
    • Ivancich, A.1    Joue, H.M.2    Gaillard, J.3
  • 53
    • 0030835382 scopus 로고    scopus 로고
    • EPR investigation of compound I in Proteus mirabilis and bovine liver catalases: Formation of porphyrin and tyrosyl radical intermediates
    • A. Ivancich, H.M. Joue, B. Sartor, and J. Gaillard EPR investigation of compound I in Proteus mirabilis and bovine liver catalases: formation of porphyrin and tyrosyl radical intermediates Biochemistry 36 1997 9356 9364
    • (1997) Biochemistry , vol.36 , pp. 9356-9364
    • Ivancich, A.1    Joue, H.M.2    Sartor, B.3    Gaillard, J.4
  • 54
    • 0023839665 scopus 로고
    • Higher oxidation states of prostaglandin H synthase. EPR study of a transient tyrosyl radical in the enzyme during the peroxidase reaction
    • R. Karthein, R. Dietz, W. Nastainzyk, and H.H. Ruf Higher oxidation states of prostaglandin H synthase. EPR study of a transient tyrosyl radical in the enzyme during the peroxidase reaction Eur. J. Biochem. 171 1988 313 320
    • (1988) Eur. J. Biochem. , vol.171 , pp. 313-320
    • Karthein, R.1    Dietz, R.2    Nastainzyk, W.3    Ruf, H.H.4
  • 55
    • 0017133108 scopus 로고
    • Mossbauer spectroscopic study of compound ES of cytochrome c peroxidase
    • G. Lang, K. Spartalian, and T. Yonetani Mossbauer spectroscopic study of compound ES of cytochrome c peroxidase Biochim. Biophys. Acta 451 1976 250 258
    • (1976) Biochim. Biophys. Acta , vol.451 , pp. 250-258
    • Lang, G.1    Spartalian, K.2    Yonetani, T.3
  • 56
    • 4644324308 scopus 로고    scopus 로고
    • Tyrosine 167: The origin of the radical species observed in the reaction of cytochrome c oxidase with hydrogen peroxide in Paracoccus denitrificans
    • K. Budiman, A. Kannt, S. Lyubenova, O.M.H. Richter, B. Ludwig, H. Michel, and F. MacMillan Tyrosine 167: the origin of the radical species observed in the reaction of cytochrome c oxidase with hydrogen peroxide in Paracoccus denitrificans Biochemistry 43 2004 11709 11716
    • (2004) Biochemistry , vol.43 , pp. 11709-11716
    • Budiman, K.1    Kannt, A.2    Lyubenova, S.3    Richter, O.M.H.4    Ludwig, B.5    Michel, H.6    MacMillan, F.7
  • 57
    • 0025891116 scopus 로고
    • Compound I radical in site-directed mutants of cytochrome c peroxidase as probed by electron paramagnetic resonance and electron-nuclear double resonance
    • L.A. Fishel, M.F. Farnum, J.M. Mauro, M.A. Miller, and J. Kraut Compound I radical in site-directed mutants of cytochrome c peroxidase as probed by electron paramagnetic resonance and electron-nuclear double resonance Biochemistry 30 1991 1986 1996
    • (1991) Biochemistry , vol.30 , pp. 1986-1996
    • Fishel, L.A.1    Farnum, M.F.2    Mauro, J.M.3    Miller, M.A.4    Kraut, J.5
  • 59
    • 0033199376 scopus 로고    scopus 로고
    • Evidence for sulfur-based radicals in thiolate compound I intermediates
    • M.T. Green Evidence for sulfur-based radicals in thiolate compound I intermediates J. Am. Chem. Soc. 121 1999 7939 7940
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 7939-7940
    • Green, M.T.1
  • 60
    • 0037223865 scopus 로고    scopus 로고
    • Thoughts on thiolate tethering. Tribute and thanks to a teacher
    • V. Ullrich Thoughts on thiolate tethering. Tribute and thanks to a teacher Arch. Biochem. Biophys. 409 2003 45 51
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 45-51
    • Ullrich, V.1
  • 61
    • 84892226337 scopus 로고    scopus 로고
    • Computational approaches to cytochrome P450 function
    • P.R. Ortiz de Montellano Kluwer Academic/Plenum New York
    • S. Shaik, and S.P. De Visser Computational approaches to cytochrome P450 function P.R. Ortiz de Montellano Cytochrome P450, Structure, Mechanism, and Biochemistry 2005 Kluwer Academic/Plenum New York 45 85
    • (2005) Cytochrome P450, Structure, Mechanism, and Biochemistry , pp. 45-85
    • Shaik, S.1    De Visser, S.P.2
  • 62
    • 0035951308 scopus 로고    scopus 로고
    • Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171: Implications for the reaction mechanism
    • W. Blodig, A.T. Smith, W.A. Doyle, and K.J. Piontek Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171: Implications for the reaction mechanism Mol. Biol. 305 2001 851 861
    • (2001) Mol. Biol. , vol.305 , pp. 851-861
    • Blodig, W.1    Smith, A.T.2    Doyle, W.A.3    Piontek, K.J.4
  • 63
    • 0001273387 scopus 로고    scopus 로고
    • A tyrosyl radical in an irradiated single crystal of N-acetyl-l-tyrosine studied by X-band cw-EPR, high-frequency EPR, and ENDOR spectroscopies
    • A. Mezzetti, A.L. Maniero, M. Brustolon, G. Giacometti, and L.C. Brunel A tyrosyl radical in an irradiated single crystal of N-acetyl-l-tyrosine studied by X-band cw-EPR, high-frequency EPR, and ENDOR spectroscopies J. Phys. Chem. A 103 1999 9636 9643
    • (1999) J. Phys. Chem. a , vol.103 , pp. 9636-9643
    • Mezzetti, A.1    Maniero, A.L.2    Brustolon, M.3    Giacometti, G.4    Brunel, L.C.5


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