메뉴 건너뛰기




Volumn 287, Issue 29, 2012, Pages 24139-24147

Cytochrome P450-type hydroxylation and epoxidation in a tyrosine-liganded hemoprotein, catalase-related allene oxide synthase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ALLENE OXIDE SYNTHASE; ARACHIDONIC ACIDS; COMPOUND I; CYTOCHROME P450; DOUBLE BONDS; HEMOPROTEINS; HYDROXYLASES; IODOSYLBENZENE; MONOOXYGENASES; NATURAL SUBSTRATES; NITRIC-OXIDE SYNTHASE; OXYGEN DONORS; REGIOSPECIFICITY; STEREOSPECIFIC;

EID: 84863799806     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.364216     Document Type: Article
Times cited : (10)

References (44)
  • 1
    • 21844434930 scopus 로고    scopus 로고
    • Structure and chemistry of cytochrome P450
    • DOI 10.1021/cr0307143
    • Denisov, I. G., Makris, T. M., Sligar, S. G., and Schlichting, I. (2005) Structure and chemistry of cytochrome P450. Chem. Rev. 105, 2253-2277 (Pubitemid 40951784)
    • (2005) Chemical Reviews , vol.105 , Issue.6 , pp. 2253-2277
    • Denisov, I.G.1    Makris, T.M.2    Sligar, S.G.3    Schlichting, I.4
  • 2
    • 36048939609 scopus 로고    scopus 로고
    • Mechanisms of cytochrome P450 substrate oxidation: MiniReview
    • Guengerich, F. P. (2007) Mechanisms of cytochrome P450 substrate oxidation: MiniReview. J. Biochem. Mol. Toxicol. 21, 163-168
    • (2007) J. Biochem. Mol. Toxicol. , vol.21 , pp. 163-168
    • Guengerich, F.P.1
  • 3
  • 4
    • 0034635333 scopus 로고    scopus 로고
    • Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism
    • Putnam, C. D., Arvai, A. S., Bourne, Y., and Tainer, J. A. (2000) Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism. J. Mol. Biol. 296, 295-309
    • (2000) J. Mol. Biol. , vol.296 , pp. 295-309
    • Putnam, C.D.1    Arvai, A.S.2    Bourne, Y.3    Tainer, J.A.4
  • 6
    • 0036669865 scopus 로고    scopus 로고
    • Allene oxide synthases and allene oxides
    • DOI 10.1016/S0090-6980(02)00046-1, PII S0090698002000461
    • Tijet, N., and Brash, A. R. (2002) Allene oxide synthases and allene oxides. Prostaglandins Other Lipid Mediat. 68-69, 423-431 (Pubitemid 35247412)
    • (2002) Prostaglandins and Other Lipid Mediators , vol.68-69 , pp. 423-431
    • Tijet, N.1    Brash, A.R.2
  • 7
    • 70350518273 scopus 로고    scopus 로고
    • Mechanistic aspects of CYP74 allene oxide synthases and related cytochrome P450 enzymes
    • Brash, A. R. (2009) Mechanistic aspects of CYP74 allene oxide synthases and related cytochrome P450 enzymes. Phytochemistry 70, 1522-1531
    • (2009) Phytochemistry , vol.70 , pp. 1522-1531
    • Brash, A.R.1
  • 8
    • 0037223865 scopus 로고    scopus 로고
    • Thoughts on thiolate tethering: Tribute and thanks to a teacher
    • Ullrich, V. (2003) Thoughts on thiolate tethering: tribute and thanks to a teacher. Arch. Biochem. Biophys. 409, 45-51
    • (2003) Arch. Biochem. Biophys. , vol.409 , pp. 45-51
    • Ullrich, V.1
  • 9
    • 79951563496 scopus 로고    scopus 로고
    • The reaction mechanism of allene oxide synthase: Interplay of theoretical QM/MM calculations and experimental investigations
    • Cho, K. B., Lai, W., Hamberg, M., Raman, C. S., and Shaik, S. (2011) The reaction mechanism of allene oxide synthase: interplay of theoretical QM/MM calculations and experimental investigations. Arch. Biochem. Biophys. 507, 14-25
    • (2011) Arch. Biochem. Biophys. , vol.507 , pp. 14-25
    • Cho, K.B.1    Lai, W.2    Hamberg, M.3    Raman, C.S.4    Shaik, S.5
  • 11
    • 77349091080 scopus 로고    scopus 로고
    • Hydrocarbon hydroxylation by cytochrome P450 enzymes
    • Ortiz de Montellano, P. R. (2010) Hydrocarbon hydroxylation by cytochrome P450 enzymes. Chem. Rev. 110, 932-948
    • (2010) Chem. Rev. , vol.110 , pp. 932-948
    • Ortiz De Montellano, P.R.1
  • 12
    • 0023657122 scopus 로고
    • Thromboxane synthase catalyses hydroxylations of prostaglandin H2 analogs in the presence of iodosylbenzene
    • Hecker, M., Baader, W. J., Weber, P., and Ullrich, V. (1987) Thromboxane synthase catalyses hydroxylations of prostaglandin H2 analogs in the presence of iodosylbenzene. Eur. J. Biochem. 169, 563-569
    • (1987) Eur. J. Biochem. , vol.169 , pp. 563-569
    • Hecker, M.1    Baader, W.J.2    Weber, P.3    Ullrich, V.4
  • 14
    • 0033584952 scopus 로고    scopus 로고
    • Purification and catalytic activities of the two domains of the allene oxide synthase-lipoxygenase fusion protein of the coral Plexaura homomalla
    • Boutaud, O., and Brash, A. R. (1999) Purification and catalytic activities of the two domains of the allene oxide synthase-lipoxygenase fusion protein of the coral Plexaura homomalla. J. Biol. Chem. 274, 33764-33770 (Pubitemid 129511693)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.47 , pp. 33764-33770
    • Boutaud, O.1    Brash, A.R.2
  • 15
    • 0020510516 scopus 로고
    • Controlled synthesis of monohydroperoxides by α-tocopherol inhibited autoxidation of polyunsaturated lipids
    • DOI 10.1016/0009-3084(83)90069-5
    • Peers, K. E., and Coxon, D. T. (1983) Controlled synthesis of monohydroperoxides by α-tocopherol inhibited autoxidation of polyunsaturated lipids. Chem. Phys. Lipids 32, 49-56 (Pubitemid 13127517)
    • (1983) Chemistry and Physics of Lipids , vol.32 , Issue.1 , pp. 49-56
    • Peers, K.E.1    Coxon, D.T.2
  • 16
    • 0034548008 scopus 로고    scopus 로고
    • Enantiomeric separation of hydroxy eicosanoids by chiral column chromatography: Effect of the alcohol modifier
    • Schneider, C., Boeglin, W. E., and Brash, A. R. (2000) Enantiomeric separation of hydroxy eicosanoids by chiral column chromatography: effect of the alcohol modifier. Anal. Biochem. 287, 186-189
    • (2000) Anal. Biochem. , vol.287 , pp. 186-189
    • Schneider, C.1    Boeglin, W.E.2    Brash, A.R.3
  • 19
    • 1042297292 scopus 로고
    • Behavior of long chain allylic hydroperoxides in the presence of certain transition metal complexes. II. Structure of epoxy alcohols formed from the hydroperoxides of cis and trans octadec- 9-enoate methyl esters in the presence of vanadyl acetylacetonate (translated from the French)
    • Mercier, J., and Agoh, B. (1974) Behavior of long chain allylic hydroperoxides in the presence of certain transition metal complexes. II. Structure of epoxy alcohols formed from the hydroperoxides of cis and trans octadec- 9-enoate methyl esters in the presence of vanadyl acetylacetonate (translated from the French). Chem. Phys. Lipids 12, 239-248
    • (1974) Chem. Phys. Lipids , vol.12 , pp. 239-248
    • Mercier, J.1    Agoh, B.2
  • 20
    • 0028093915 scopus 로고
    • Eicosanoids from the tropical red alga Murrayella periclados
    • DOI 10.1016/S0031-9422(00)89643-0
    • Bernart, M. W., and Gerwick, W. H. (1994) Eicosanoids from the tropical red alga Murrayella periclados. Phytochemistry 36, 1233-1240 (Pubitemid 2118482)
    • (1994) Phytochemistry , vol.36 , Issue.5 , pp. 1233-1240
    • Bernart, M.W.1    Gerwick, W.H.2
  • 21
    • 46149131094 scopus 로고
    • Stereochemistry of two epoxy alcohols from Saprolegnia parasitica
    • Hamberg, M., Herman, R. P., and Jacobsson, U. (1986) Stereochemistry of two epoxy alcohols from Saprolegnia parasitica. Biochim. Biophys. Acta 879, 410-418
    • (1986) Biochim. Biophys. Acta , vol.879 , pp. 410-418
    • Hamberg, M.1    Herman, R.P.2    Jacobsson, U.3
  • 22
    • 49249151283 scopus 로고
    • Stereoselective epoxidation of acyclic allylic alcohols. A correction of our previous work
    • Rossiter, B. E., Verhoeven, T. R., and Sharpless, K. B. (1979) Stereoselective epoxidation of acyclic allylic alcohols. A correction of our previous work. Tetrahedron Lett. 20, 4733-4736
    • (1979) Tetrahedron Lett. , vol.20 , pp. 4733-4736
    • Rossiter, B.E.1    Verhoeven, T.R.2    Sharpless, K.B.3
  • 23
    • 0027995192 scopus 로고
    • Prostacyclin and thromboxane synthase: New aspects of hemethiolate catalysis
    • Ullrich, V., and Brugger, R. (1994) Prostacyclin and thromboxane synthase: new aspects of hemethiolate catalysis. Angew. Chem. Int. Ed. Engl. 33, 1911-1919
    • (1994) Angew. Chem. Int. Ed. Engl. , vol.33 , pp. 1911-1919
    • Ullrich, V.1    Brugger, R.2
  • 24
    • 0029122098 scopus 로고
    • Molecular cloning, expression, and characterization of an endogenous human cytochrome P450 arachidonic acid epoxygenase isoform
    • Zeldin, D. C., DuBois, R. N., Falck, J. R., and Capdevila, J. H. (1995) Molecular cloning, expression, and characterization of an endogenous human cytochrome P450 arachidonic acid epoxygenase isoform. Arch. Biochem. Biophys. 322, 76-86
    • (1995) Arch. Biochem. Biophys. , vol.322 , pp. 76-86
    • Zeldin, D.C.1    DuBois, R.N.2    Falck, J.R.3    Capdevila, J.H.4
  • 25
    • 0031951506 scopus 로고    scopus 로고
    • Cytochromes P450 with bisallylic hydroxylation activity on arachidonic and linoleic acids studied with human recombinant enzymes and with human and rat liver microsomes
    • Bylund, J., Kunz, T., Valmsen, K., and Oliw, E. H. (1998) Cytochromes P450 with bis-allylic hydroxylation activity on arachidonic and linoleic acids studied with human recombinant enzymes and with human and rat liver microsomes. J. Pharmacol. Exp. Ther. 284, 51-60 (Pubitemid 28109528)
    • (1998) Journal of Pharmacology and Experimental Therapeutics , vol.284 , Issue.1 , pp. 51-60
    • Bylund, J.1    Kunz, T.2    Valmsen, K.3    Oliw, E.H.4
  • 26
    • 0027216936 scopus 로고
    • Bis-allylic hydroxylation of polyunsaturated fatty acids by hepatic monooxygenases and its relation to the enzymatic and nonenzymatic formation of conjugated hydroxy fatty acids
    • DOI 10.1006/abbi.1993.1059
    • Oliw, E. H., Brodowsky, I. D., Hörnsten, L., and Hamberg, M. (1993) Bisallylic hydroxylation of polyunsaturated fatty acids by hepatic monooxygenases and its relation to the enzymatic and nonenzymatic formation of conjugated hydroxy fatty acids. Arch. Biochem. Biophys. 300, 434-439 (Pubitemid 23225768)
    • (1993) Archives of Biochemistry and Biophysics , vol.300 , Issue.1 , pp. 434-439
    • Oliw, E.H.1    Brodowsky, I.D.2    Hornsten, L.3    Hamberg, M.4
  • 27
    • 0029102061 scopus 로고
    • 7-HETE, 10-HETE, and 13-HETE are major products of NADPH-dependent arachidonic acid metabolism in rat liver microsomes: Analysis of their stereochemistry, and the stereochemistry of their acid-catalyzed rearrangement
    • Brash, A. R., Boeglin, W. E., Capdevila, J. H., Yeola, S., and Blair, I. A. (1995) 7-HETE, 10-HETE, and 13-HETE are major products of NADPH-dependent arachidonic acid metabolism in rat liver microsomes: analysis of their stereochemistry, and the stereochemistry of their acid-catalyzed rearrangement. Arch. Biochem. Biophys. 321, 485-492
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 485-492
    • Brash, A.R.1    Boeglin, W.E.2    Capdevila, J.H.3    Yeola, S.4    Blair, I.A.5
  • 28
    • 0029039791 scopus 로고
    • Arachidonic acid metabolism by human cytochrome P450s 2C8, 2C9, 2E1, and 1A2: Regioselective oxygenation and evidence for a role for CYP2C enzymes in arachidonic acid epoxygenation in human liver microsomes
    • Rifkind, A. B., Lee, C., Chang, T. K., and Waxman, D. J. (1995) Arachidonic acid metabolism by human cytochrome P450s 2C8, 2C9, 2E1, and 1A2: regioselective oxygenation and evidence for a role for CYP2C enzymes in arachidonic acid epoxygenation in human liver microsomes. Arch. Biochem. Biophys. 320, 380-389
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 380-389
    • Rifkind, A.B.1    Lee, C.2    Chang, T.K.3    Waxman, D.J.4
  • 29
    • 0032167962 scopus 로고    scopus 로고
    • Cloning and expression of murine CYP2Cs and their ability to metabolize arachidonic acid
    • DOI 10.1006/abbi.1998.0806
    • Luo, G., Zeldin, D. C., Blaisdell, J. A., Hodgson, E., and Goldstein, J. A. (1998) Cloning and expression of murine CYP2Cs and their ability to metabolize arachidonic acid. Arch. Biochem. Biophys. 357, 45-57 (Pubitemid 28402584)
    • (1998) Archives of Biochemistry and Biophysics , vol.357 , Issue.1 , pp. 45-57
    • Luo, G.1    Zeldin, D.C.2    Blaisdell, J.A.3    Hodgson, E.4    Goldstein, J.A.5
  • 31
    • 0018426059 scopus 로고
    • Iodosylbenzene derivatives as oxygen donors in cytochrome P-450 catalyzed steroid hydroxylations
    • DOI 10.1021/bi00572a020
    • Gustafsson, J. A., Rondahl, L., and Bergman, J. (1979) Iodosylbenzene derivatives as oxygen donors in cytochrome P-450 catalyzed steroid hydroxylations. Biochemistry 18, 865-870 (Pubitemid 9152367)
    • (1979) Biochemistry , vol.18 , Issue.5 , pp. 865-870
    • Gustafsson, J.A.1    Rondahl, L.2    Bergman, J.3
  • 32
    • 0029047732 scopus 로고
    • Roles of divalent metal ions in oxidations catalyzed by recombinant cytochrome P450 3A4 and replacement of NADPH-cytochrome P450 reductase with other flavoproteins, ferredoxin, and oxygen surrogates
    • Yamazaki, H., Ueng, Y. F., Shimada, T., and Guengerich, F. P. (1995) Roles of divalent metal ions in oxidations catalyzed by recombinant cytochrome P450 3A4 and replacement of NADPH-cytochrome P450 reductase with other flavoproteins, ferredoxin, and oxygen surrogates. Biochemistry 34, 8380-8389
    • (1995) Biochemistry , vol.34 , pp. 8380-8389
    • Yamazaki, H.1    Ueng, Y.F.2    Shimada, T.3    Guengerich, F.P.4
  • 33
    • 0037388114 scopus 로고    scopus 로고
    • The bioinorganic chemistry of iron in oxygenases and supramolecular assemblies
    • Groves, J. T. (2003) The bioinorganic chemistry of iron in oxygenases and supramolecular assemblies. Proc. Natl. Acad. Sci. U.S.A. 100, 3569-3574
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3569-3574
    • Groves, J.T.1
  • 34
    • 0032584090 scopus 로고    scopus 로고
    • Epoxidation of olefins by cytochrome P450: Evidence from site-specific mutagenesis for hydroperoxo-iron as an electrophilic oxidant
    • DOI 10.1073/pnas.95.7.3555
    • Vaz, A. D., McGinnity, D. F., and Coon, M. J. (1998) 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. 95, 3555-3560 (Pubitemid 28173166)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.7 , pp. 3555-3560
    • Vaz, A.D.N.1    McGinnity, D.F.2    Coon, M.J.3
  • 35
    • 48149083506 scopus 로고    scopus 로고
    • Which oxidant is really responsible for P450 model oxygenation reactions? A kinetic approach
    • Franke, A., Fertinger, C., and van Eldik, R. (2008) Which oxidant is really responsible for P450 model oxygenation reactions? A kinetic approach. Angew. Chem. Int. Ed. Engl. 47, 5238-5242
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 5238-5242
    • Franke, A.1    Fertinger, C.2    Van Eldik, R.3
  • 36
    • 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. (2010) P450 enzymes: their structure, reactivity, and selectivity - modeled by QM/MM calculations. Chem. Rev. 110, 949-1017
    • (2010) 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
  • 37
    • 4644317084 scopus 로고    scopus 로고
    • Hydroperoxoferric heme intermediate as a second electrophilic oxidant in cytochrome P450-catalyzed reactions
    • DOI 10.1007/s00775-004-0575-7
    • Jin, S., Bryson, T. A., and Dawson, J. H. (2004) Hydroperoxoferric heme intermediate as a second electrophilic oxidant in cytochrome P450-catalyzed reactions. J. Biol. Inorg. Chem. 9, 644-653 (Pubitemid 39279243)
    • (2004) Journal of Biological Inorganic Chemistry , vol.9 , Issue.6 , pp. 644-653
    • Jin, S.1    Bryson, T.A.2    Dawson, J.H.3
  • 38
    • 0031213744 scopus 로고    scopus 로고
    • Myoglobin-catalyzed bis-allylic hydroxylation and epoxidation of linoleic acid
    • Hamberg, M. (1997) Myoglobin-catalyzed bis-allylic hydroxylation and epoxidation of linoleic acid. Arch. Biochem. Biophys. 344, 194-199
    • (1997) Arch. Biochem. Biophys. , vol.344 , pp. 194-199
    • Hamberg, M.1
  • 39
    • 34547759977 scopus 로고    scopus 로고
    • Reactivities of oxo and peroxo intermediates studied by hemoprotein mutants
    • Watanabe, Y., Nakajima, H., and Ueno, T. (2007) Reactivities of oxo and peroxo intermediates studied by hemoprotein mutants. Acc. Chem. Res. 40, 554-562
    • (2007) Acc. Chem. Res. , vol.40 , pp. 554-562
    • Watanabe, Y.1    Nakajima, H.2    Ueno, T.3
  • 40
    • 0027505784 scopus 로고
    • Roles of proximal ligand in heme proteins: Replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase
    • DOI 10.1021/bi00052a031
    • Adachi, S., Nagano, S., Ishimori, K., Watanabe, Y., Morishima, I., Egawa, T., Kitagawa, T., and Makino, R. (1993) Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase. Biochemistry 32, 241-252 (Pubitemid 23033342)
    • (1993) Biochemistry , vol.32 , Issue.1 , pp. 241-252
    • Adachi, S.-I.1    Nagano, S.2    Ishimori, K.3    Watanabe, Y.4    Morishima, I.5    Egawa, T.6    Kitagawa, T.7    Makino, R.8
  • 43
    • 69249109193 scopus 로고    scopus 로고
    • Evidence for an ionic intermediate in the transformation of fatty acid hydroperoxide by a catalase-related allene oxide synthase from the Cyanobacterium Acaryochloris marina
    • Gao, B., Boeglin, W. E., Zheng, Y., Schneider, C., and Brash, A. R. (2009) Evidence for an ionic intermediate in the transformation of fatty acid hydroperoxide by a catalase-related allene oxide synthase from the Cyanobacterium Acaryochloris marina. J. Biol. Chem. 284, 22087-22098
    • (2009) J. Biol. Chem. , vol.284 , pp. 22087-22098
    • Gao, B.1    Boeglin, W.E.2    Zheng, Y.3    Schneider, C.4    Brash, A.R.5
  • 44
    • 37649021487 scopus 로고    scopus 로고
    • Enzymatic synthesis of a bicyclobutane fatty acid by a hemoprotein lipoxygenase fusion protein from the cyanobacterium Anabaena PCC 7120
    • Schneider, C., Niisuke, K., Boeglin, W. E., Voehler, M., Stec, D. F., Porter, N. A., and Brash, A. R. (2007) Enzymatic synthesis of a bicyclobutane fatty acid by a hemoprotein lipoxygenase fusion protein from the cyanobacterium Anabaena PCC 7120. Proc. Natl. Acad. Sci. U.S.A. 104, 18941-18945
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 18941-18945
    • Schneider, C.1    Niisuke, K.2    Boeglin, W.E.3    Voehler, M.4    Stec, D.F.5    Porter, N.A.6    Brash, A.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.