메뉴 건너뛰기




Volumn 338, Issue 1, 2005, Pages 346-354

Thirty years of microbial P450 monooxygenase research: Peroxo-heme intermediates - The central bus station in heme oxygenase catalysis

Author keywords

Cytochrome P450; Heme peroxo intermediate; Oxygenase catalysis

Indexed keywords

CHLORIDE PEROXIDASE; CYTOCHROME P450; HEME OXYGENASE; HEMOPROTEIN; HORSERADISH PEROXIDASE; UNSPECIFIC MONOOXYGENASE;

EID: 27544483600     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.094     Document Type: Review
Times cited : (76)

References (51)
  • 4
    • 13844322067 scopus 로고    scopus 로고
    • Cytochrome P450: Nature's most versatile biological catalyst
    • M.J. Coon Cytochrome P450: nature's most versatile biological catalyst Annu. Rev. Pharmacol. Toxicol. 45 2005 1 25
    • (2005) Annu. Rev. Pharmacol. Toxicol. , vol.45 , pp. 1-25
    • Coon, M.J.1
  • 6
    • 0015116798 scopus 로고
    • A specific role of reduced adrenodoxin in adrenal mitochondrial steroid hydroxylases
    • J.J. Huang, and T. Kimura A specific role of reduced adrenodoxin in adrenal mitochondrial steroid hydroxylases Biochem. Biophys. Res. Commun. 44 1971 1065 1070
    • (1971) Biochem. Biophys. Res. Commun. , vol.44 , pp. 1065-1070
    • Huang, J.J.1    Kimura, T.2
  • 7
    • 0017170343 scopus 로고
    • Coupling of spin, substrate, and redox equilibria in cytochrome P450
    • S.G. Sligar Coupling of spin, substrate, and redox equilibria in cytochrome P450 Biochemistry 15 1976 5399 5406
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 9
    • 0015311103 scopus 로고
    • Pseudomonas putida cytochrome P-450. Characterization of an oxygenated form of the hemoprotein
    • J.A. Peterson, Y. Ishimura, and B.W. Griffin Pseudomonas putida cytochrome P-450. Characterization of an oxygenated form of the hemoprotein Arch. Biochem. Biophys. 149 1972 197 208
    • (1972) Arch. Biochem. Biophys. , vol.149 , pp. 197-208
    • Peterson, J.A.1    Ishimura, Y.2    Griffin, B.W.3
  • 10
  • 12
    • 0017696533 scopus 로고
    • On the mechanism of compound I formation from peroxidases and catalases
    • P. Jones, and H.B. Dunford On the mechanism of compound I formation from peroxidases and catalases J. Theor. Biol. 69 1977 457 470
    • (1977) J. Theor. Biol. , vol.69 , pp. 457-470
    • Jones, P.1    Dunford, H.B.2
  • 13
    • 0017823468 scopus 로고
    • Electron capture at the iron-oxygen centre in single crystals of oxymyoglobin studied by electron spin resonance spectroscopy
    • M.C.R. Symons, and R.L. Petersen Electron capture at the iron-oxygen centre in single crystals of oxymyoglobin studied by electron spin resonance spectroscopy Biochim. Biophys. Acta 535 1978 241 247
    • (1978) Biochim. Biophys. Acta , vol.535 , pp. 241-247
    • Symons, M.C.R.1    Petersen, R.L.2
  • 14
    • 0018662450 scopus 로고
    • Intermediate spin-states in one-electron reduction of oxygen-hemoprotein complexes at low temperature
    • Z. Gasyna Intermediate spin-states in one-electron reduction of oxygen-hemoprotein complexes at low temperature FEBS Lett. 106 1979 213 218
    • (1979) FEBS Lett. , vol.106 , pp. 213-218
    • Gasyna, Z.1
  • 15
    • 21844448228 scopus 로고
    • ESR spectroscopy of unstable intermediates of the reduction of oxygen complexes of cytochrome P450 and other hemoproteins
    • R.M. Davydov, and S.V. Khangulov ESR spectroscopy of unstable intermediates of the reduction of oxygen complexes of cytochrome P450 and other hemoproteins Stud. Biophys. 95 1983 97 106
    • (1983) Stud. Biophys. , vol.95 , pp. 97-106
    • Davydov, R.M.1    Khangulov, S.V.2
  • 19
    • 0000498078 scopus 로고    scopus 로고
    • Coming to grips with reactive intermediates
    • A.J. Downs, and T.M. Greene Coming to grips with reactive intermediates Adv. Inorg. Chem. 46 1998 101 171
    • (1998) Adv. Inorg. Chem. , vol.46 , pp. 101-171
    • Downs, A.J.1    Greene, T.M.2
  • 20
    • 0016340781 scopus 로고
    • Studies on the conformational changes of metalloproteins induced by electrons in water-ethylene glycol solutions at low temperatures. Haemoglobin
    • L.A. Blumenfeld, R.M. Davydov, S.M. Magonov, and R.O. Vilu Studies on the conformational changes of metalloproteins induced by electrons in water-ethylene glycol solutions at low temperatures. Haemoglobin FEBS Lett. 49 1974 246 248
    • (1974) FEBS Lett. , vol.49 , pp. 246-248
    • Blumenfeld, L.A.1    Davydov, R.M.2    Magonov, S.M.3    Vilu, R.O.4
  • 21
    • 0033579110 scopus 로고    scopus 로고
    • EPR and ENDOR of catalytic intermediates in cryoreduced native and mutant oxy-cytochromes P450cam: Mutation-induced changes in the proton delivery system
    • R. Davydov, I.D.G. Macdonald, T.M. Makris, S.G. Sligar, and B.M. Hoffman EPR and ENDOR of catalytic intermediates in cryoreduced native and mutant oxy-cytochromes P450cam: mutation-induced changes in the proton delivery system J. Am. Chem. Soc. 121 1999 10654 10655
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10654-10655
    • Davydov, R.1    MacDonald, I.D.G.2    Makris, T.M.3    Sligar, S.G.4    Hoffman, B.M.5
  • 22
    • 0035853766 scopus 로고    scopus 로고
    • Cryotrapped reaction intermediates of cytochrome P450 studied by radiolytic reduction with phosphorus-32
    • I.G. Denisov, T.M. Makris, and S.G. Sligar Cryotrapped reaction intermediates of cytochrome P450 studied by radiolytic reduction with phosphorus-32 J. Biol. Chem. 276 2001 11648 11652
    • (2001) J. Biol. Chem. , vol.276 , pp. 11648-11652
    • Denisov, I.G.1    Makris, T.M.2    Sligar, S.G.3
  • 23
    • 0035925164 scopus 로고    scopus 로고
    • Hydroxylation of camphor by reduced oxy-cytochrome P450cam: Mechanistic implications of EPR and ENDOR studies of catalytic intermediates in native and mutant enzymes
    • R. Davydov, T.M. Makris, V. Kofman, D.E. Werst, S.G. Sligar, and B.M. Hoffman Hydroxylation of camphor by reduced oxy-cytochrome P450cam: mechanistic implications of EPR and ENDOR studies of catalytic intermediates in native and mutant enzymes J. Am. Chem. Soc. 123 2001 1403 1415
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1403-1415
    • Davydov, R.1    Makris, T.M.2    Kofman, V.3    Werst, D.E.4    Sligar, S.G.5    Hoffman, B.M.6
  • 24
    • 0036029799 scopus 로고    scopus 로고
    • Cryoradiolysis for the study of P450 reaction intermediates
    • I.G. Denisov, T.M. Makris, and S.G. Sligar Cryoradiolysis for the study of P450 reaction intermediates Meth. Enzymol. 357 2002 103 115
    • (2002) Meth. Enzymol. , vol.357 , pp. 103-115
    • Denisov, I.G.1    Makris, T.M.2    Sligar, S.G.3
  • 26
    • 18744374132 scopus 로고    scopus 로고
    • Cryogenic absorption spectra of hydroperoxo-ferric heme oxygenase, the active intermediate of enzymatic heme oxygenation
    • I.G. Denisov, M. Ikeda-Saito, T. Yoshida, and S.G. Sligar Cryogenic absorption spectra of hydroperoxo-ferric heme oxygenase, the active intermediate of enzymatic heme oxygenation FEBS Lett. 532 2002 203 206
    • (2002) FEBS Lett. , vol.532 , pp. 203-206
    • Denisov, I.G.1    Ikeda-Saito, M.2    Yoshida, T.3    Sligar, S.G.4
  • 27
    • 0037044754 scopus 로고    scopus 로고
    • Formation and decay of hydroperoxo-ferric heme complex in horseradish peroxidase studied by cryoradiolysis
    • I.G. Denisov, T.M. Makris, and S.G. Sligar Formation and decay of hydroperoxo-ferric heme complex in horseradish peroxidase studied by cryoradiolysis J. Biol. Chem. 277 2002 42706 42710
    • (2002) J. Biol. Chem. , vol.277 , pp. 42706-42710
    • Denisov, I.G.1    Makris, T.M.2    Sligar, S.G.3
  • 28
    • 0242490629 scopus 로고    scopus 로고
    • Resonance Raman spectroscopic studies of hydroperoxo-myoglobin at cryogenic temperatures
    • M. Ibrahim, I.G. Denisov, T.M. Makris, J.R. Kincaid, and S.G. Sligar Resonance Raman spectroscopic studies of hydroperoxo-myoglobin at cryogenic temperatures J. Am. Chem. Soc. 125 2003 13714 13718
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13714-13718
    • Ibrahim, M.1    Denisov, I.G.2    Makris, T.M.3    Kincaid, J.R.4    Sligar, S.G.5
  • 29
    • 0011120835 scopus 로고
    • Systematic trends in the spectroscopic properties of low-spin ferric ligand adducts of cytochrome P-450 and chloroperoxidase: The transition from normal to hyper spectra
    • J.H. Dawson, L.A. Andersson, M. Sono, and L.P. Hager Systematic trends in the spectroscopic properties of low-spin ferric ligand adducts of cytochrome P-450 and chloroperoxidase: the transition from normal to hyper spectra New J. Chem. 16 1992 577 582
    • (1992) New J. Chem. , vol.16 , pp. 577-582
    • Dawson, J.H.1    Andersson, L.A.2    Sono, M.3    Hager, L.P.4
  • 30
    • 0038506974 scopus 로고    scopus 로고
    • ENDOR of metalloenzymes
    • B.M. Hoffman ENDOR of metalloenzymes Acc. Chem. Res. 36 2003 522 529
    • (2003) Acc. Chem. Res. , vol.36 , pp. 522-529
    • Hoffman, B.M.1
  • 31
    • 1542378704 scopus 로고    scopus 로고
    • Dioxygen activation at mononuclear nonheme iron active sites: Enzymes, models, and intermediates
    • M. Costas, M.P. Mehn, M.P. Jensen, and L. Que Jr. Dioxygen activation at mononuclear nonheme iron active sites: enzymes, models, and intermediates Chem. Rev. 104 2004 939 986
    • (2004) Chem. Rev. , vol.104 , pp. 939-986
    • Costas, M.1    Mehn, M.P.2    Jensen, M.P.3    Que Jr., L.4
  • 32
    • 0033797723 scopus 로고    scopus 로고
    • Electronic structures of active sites in electron transfer metalloproteins: Contributions to reactivity
    • E.I. Solomon, D.W. Randall, and T. Glaser Electronic structures of active sites in electron transfer metalloproteins: contributions to reactivity Coord. Chem. Rev. 200-202 2000 595 632
    • (2000) Coord. Chem. Rev. , vol.200-202 , pp. 595-632
    • Solomon, E.I.1    Randall, D.W.2    Glaser, T.3
  • 35
    • 0020491094 scopus 로고
    • Endogenous cysteine ligation in ferric and ferrous cytochrome P-450. Direct evidence from x-ray absorption spectroscopy
    • J.E. Hahn, K.O. Hodgson, L.A. Andersson, and J.H. Dawson Endogenous cysteine ligation in ferric and ferrous cytochrome P-450. Direct evidence from x-ray absorption spectroscopy J. Biol. Chem. 257 1982 10934 10941
    • (1982) J. Biol. Chem. , vol.257 , pp. 10934-10941
    • Hahn, J.E.1    Hodgson, K.O.2    Andersson, L.A.3    Dawson, J.H.4
  • 36
    • 0001625955 scopus 로고
    • Oxygenated cytochrome P-450-CAM and chloroperoxidase: Direct evidence for sulfur donor ligation trans to dioxygen and structural characterization using EXAFS spectroscopy
    • J.H. Dawson, L.S. Kau, J.E. Penner-Hahn, M. Sono, K.S. Eble, G.S. Bruce, L.P. Hager, and K.O. Hodgson Oxygenated cytochrome P-450-CAM and chloroperoxidase: direct evidence for sulfur donor ligation trans to dioxygen and structural characterization using EXAFS spectroscopy J. Am. Chem. Soc. 108 1986 8114 8116
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 8114-8116
    • Dawson, J.H.1    Kau, L.S.2    Penner-Hahn, J.E.3    Sono, M.4    Eble, K.S.5    Bruce, G.S.6    Hager, L.P.7    Hodgson, K.O.8
  • 37
    • 0000767074 scopus 로고    scopus 로고
    • Role of the heme active site and protein environment in structure, spectra, and function of the cytochrome P450s
    • G.H. Loew, and D.L. Harris Role of the heme active site and protein environment in structure, spectra, and function of the cytochrome P450s Chem. Rev. 100 2000 407 419
    • (2000) Chem. Rev. , vol.100 , pp. 407-419
    • Loew, G.H.1    Harris, D.L.2
  • 38
    • 0037139511 scopus 로고    scopus 로고
    • Searching for the second oxidant in the catalytic cycle of cytochrome P450: A theoretical investigation of the iron(III)-hydroperoxo species and its epoxidation pathways
    • F. Ogliaro, S.P. de Visser, S. Cohen, P.K. Sharma, and S. Shaik Searching for the second oxidant in the catalytic cycle of cytochrome P450: 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
  • 40
    • 0037063569 scopus 로고    scopus 로고
    • Electronic structure and reactivity of low-spin Fe(III)-hydroperoxo complexes: Comparison to activated bleomycin
    • N. Lehnert, F. Neese, R.Y.N. Ho, L. Que Jr., and E.I. Solomon Electronic structure and reactivity of low-spin Fe(III)-hydroperoxo complexes: comparison to activated bleomycin J. Am. Chem. Soc. 124 2002 10810 10822
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10810-10822
    • Lehnert, N.1    Neese, F.2    Ho, R.Y.N.3    Que Jr., L.4    Solomon, E.I.5
  • 43
    • 0022271371 scopus 로고
    • P450cam gene cloning and expression in Pseudomonas putida and Escherichia coli
    • H. Koga, B. Rauchfuss, and I.C. Gunsalus P450cam gene cloning and expression in Pseudomonas putida and Escherichia coli Biochem. Biophys. Res. Commun. 130 1985 412 417
    • (1985) Biochem. Biophys. Res. Commun. , vol.130 , pp. 412-417
    • Koga, H.1    Rauchfuss, B.2    Gunsalus, I.C.3
  • 44
    • 0026352457 scopus 로고
    • Crystal structure of the cytochrome P-450cam active site mutant Thr252Ala
    • R. Raag, S.A. Martinis, S.G. Sligar, and T.L. Poulos Crystal structure of the cytochrome P-450cam active site mutant Thr252Ala Biochemistry 30 1991 11420 11429
    • (1991) Biochemistry , vol.30 , pp. 11420-11429
    • Raag, R.1    Martinis, S.A.2    Sligar, S.G.3    Poulos, T.L.4
  • 46
    • 0028986232 scopus 로고
    • Role of Thr-252 in cytochrome P450cam-a study with unnatural amino-acid mutagenesis
    • Y. Kimata, H. Shimada, T. Hirose, and Y. Ishimura Role of Thr-252 in cytochrome P450cam-a study with unnatural amino-acid mutagenesis Biochem. Biophys. Res. Commun. 208 1995 96 102
    • (1995) Biochem. Biophys. Res. Commun. , vol.208 , pp. 96-102
    • Kimata, Y.1    Shimada, H.2    Hirose, T.3    Ishimura, Y.4
  • 47
    • 0027994378 scopus 로고
    • A role for Asp-251 in cytochrome P-450cam oxygen activation
    • N.C. Gerber, and S.G. Sligar A role for Asp-251 in cytochrome P-450cam oxygen activation J. Biol. Chem. 269 1994 4260 4266
    • (1994) J. Biol. Chem. , vol.269 , pp. 4260-4266
    • Gerber, N.C.1    Sligar, S.G.2
  • 51
    • 0021138883 scopus 로고
    • On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P-450. Products of oxygen reduction
    • L.D. Gorsky, D.R. Koop, and M.J. Coon On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P-450. Products of oxygen reduction J. Biol. Chem. 259 1984 6812 6817
    • (1984) J. Biol. Chem. , vol.259 , pp. 6812-6817
    • Gorsky, L.D.1    Koop, D.R.2    Coon, M.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.