메뉴 건너뛰기




Volumn 316, Issue 4, 2004, Pages 1081-1087

Aromatic N-hydroxyguanidines as new reduction cosubstrates for dopamine β-hydroxylase

Author keywords

Copper centers; Dopamine hydroxylase; N Hydroxyguanidines; Nitrosoimine; Reduction

Indexed keywords

4 METHOXYACETOPHENONE OXIME; 4 METHOXYBENZAMIDOXIME; DOPAMINE BETA MONOOXYGENASE; GUANIDINE DERIVATIVE; IMINE; N (4 METHOXYPHENYL) N' HYDROXYGUANIDINE; N (4 METHOXYPHENYL) N' METHOXYGUANIDINE; N (4 METHOXYPHENYL)ACETAMIDOXIME; NITROSOIMINE; OXIME DERIVATIVE; UNCLASSIFIED DRUG;

EID: 1642373115     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.02.163     Document Type: Article
Times cited : (5)

References (32)
  • 1
    • 0017403459 scopus 로고
    • Bovine adrenal tyrosine hydroxylase: Purification and properties
    • Hoeldtke R., Kaufman S. Bovine adrenal tyrosine hydroxylase: purification and properties. J. Biol. Chem. 252:1977;3160-3169.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3160-3169
    • Hoeldtke, R.1    Kaufman, S.2
  • 2
    • 7744231498 scopus 로고    scopus 로고
    • Mechanisms whereby mononuclear proteins functionalize organic substrates
    • Klinman J.P. Mechanisms whereby mononuclear proteins functionalize organic substrates. Chem. Rev. 96:1996;2541-2562.
    • (1996) Chem. Rev. , vol.96 , pp. 2541-2562
    • Klinman, J.P.1
  • 3
    • 0036179406 scopus 로고    scopus 로고
    • Copper-containing monooxygenases: Enzymatic and biomimetic studies of the O-atom transfer catalysis
    • Blain I., Slama P., Giorgi M., Tron T., Réglier M. Copper-containing monooxygenases: enzymatic and biomimetic studies of the O-atom transfer catalysis. Rev. Mol. Biotech. 90:2002;95-112.
    • (2002) Rev. Mol. Biotech. , vol.90 , pp. 95-112
    • Blain, I.1    Slama, P.2    Giorgi, M.3    Tron, T.4    Réglier, M.5
  • 4
    • 0023076449 scopus 로고
    • Dopamine β-monooxygenase from bovine adrenal medulla
    • Ljones T. Dopamine β-monooxygenase from bovine adrenal medulla. Methods Enzymol. 142:1987;596-602.
    • (1987) Methods Enzymol. , vol.142 , pp. 596-602
    • Ljones, T.1
  • 5
    • 0006015756 scopus 로고
    • 3,4-Dihydroxyphenylethylamine β-hydroxylase: A copper protein
    • Friedman S., Kaufman S. 3,4-Dihydroxyphenylethylamine β-hydroxylase: a copper protein. J. Biol. Chem. 240:1965;552-554.
    • (1965) J. Biol. Chem. , vol.240 , pp. 552-554
    • Friedman, S.1    Kaufman, S.2
  • 6
    • 0018965590 scopus 로고
    • Direct spectrophotometric detection of ascorbate free radical formed by dopamine beta-monooxygenase and by ascorbate oxidase
    • Skotland T., Ljones T. Direct spectrophotometric detection of ascorbate free radical formed by dopamine beta-monooxygenase and by ascorbate oxidase. Biochim. Biophys. Acta. 630:1980;30-35.
    • (1980) Biochim. Biophys. Acta , vol.630 , pp. 30-35
    • Skotland, T.1    Ljones, T.2
  • 7
    • 0023748630 scopus 로고
    • The copper site of dopamine β-hydroxylase: An X-ray absorption spectroscopic study
    • Scott R.A., Sullivan R.J., DeWolf W.E. Jr., Dolle R.E., Kruse L.I. The copper site of dopamine β-hydroxylase: an X-ray absorption spectroscopic study. Biochemistry. 27:1988;5411-5417.
    • (1988) Biochemistry , vol.27 , pp. 5411-5417
    • Scott, R.A.1    Sullivan, R.J.2    Dewolf, W.E.Jr.3    Dolle, R.E.4    Kruse, L.I.5
  • 8
    • 0028768981 scopus 로고
    • A. Identification of a sulfur ligand at the dioxygen binding site by EXAFS and FTIR spectroscopy
    • A. Identification of a sulfur ligand at the dioxygen binding site by EXAFS and FTIR spectroscopy. J. Am. Chem. Soc. 116:1994;1924-1931.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 1924-1931
    • Reedy, B.J.1    Blackburn, N.J.2
  • 9
    • 0023684024 scopus 로고
    • Active site of dopamine β-hydroxylase. Comparison of enzyme derivatives containing four and eight copper atoms per tetramer using potentiometry and EPR spectroscopy
    • Blackburn N.J., Concannon M., Shahiyan S.K., Mabbs F.E., Collison D. Active site of dopamine β-hydroxylase. Comparison of enzyme derivatives containing four and eight copper atoms per tetramer using potentiometry and EPR spectroscopy. Biochemistry. 27:1988;6001-6008.
    • (1988) Biochemistry , vol.27 , pp. 6001-6008
    • Blackburn, N.J.1    Concannon, M.2    Shahiyan, S.K.3    Mabbs, F.E.4    Collison, D.5
  • 10
    • 0000623742 scopus 로고    scopus 로고
    • Copper-dioxygen and copper-oxo species relevant to copper oxygenases and oxidases
    • Blackman A.G., Tolman W.B. Copper-dioxygen and copper-oxo species relevant to copper oxygenases and oxidases. Struct. Bond. 97:2000;179-212.
    • (2000) Struct. Bond. , vol.97 , pp. 179-212
    • Blackman, A.G.1    Tolman, W.B.2
  • 11
    • 0030699146 scopus 로고    scopus 로고
    • Amidation of bioactive peptides: The structure of peptidylglycine α-amidating monooxygenase
    • Prigge S.T., Kolhekar A.S., Eipper B.A., Mains R.E., Amzel L.M. Amidation of bioactive peptides: the structure of peptidylglycine α-amidating monooxygenase. Science. 278:1997;1300-1305.
    • (1997) Science , vol.278 , pp. 1300-1305
    • Prigge, S.T.1    Kolhekar, A.S.2    Eipper, B.A.3    Mains, R.E.4    Amzel, L.M.5
  • 12
    • 0016204091 scopus 로고
    • Dopamine β-hydroxylase: Evidence against a ping-pong mechanism
    • Ljones T., Flatmark T. Dopamine β-hydroxylase: evidence against a ping-pong mechanism. FEBS Lett. 49:1974;49-52.
    • (1974) FEBS Lett. , vol.49 , pp. 49-52
    • Ljones, T.1    Flatmark, T.2
  • 13
    • 0025784684 scopus 로고
    • Continuous spectrophotometric assays for dopamine β-monooxygenase based on two novel electron donors: N , N -dimethyl-1,4-phenylenediamine and 2-aminoascorbic acid
    • Wimalasena K., Wimalasena D.S. Continuous spectrophotometric assays for dopamine β-monooxygenase based on two novel electron donors: N, N -dimethyl-1,4-phenylenediamine and 2-aminoascorbic acid Anal. Biochem. 197:1991;353-361.
    • (1991) Anal. Biochem. , vol.197 , pp. 353-361
    • Wimalasena, K.1    Wimalasena, D.S.2
  • 14
    • 0029909758 scopus 로고    scopus 로고
    • Reduction of dopamine β-monooxygenase. A unified model for apparent negative cooperativity and fumarate activation
    • Wimalasena K., Dharmasena S., Wimalasena D.S., Hughbanks-Wheaton D.K. Reduction of dopamine β-monooxygenase. A unified model for apparent negative cooperativity and fumarate activation. J. Biol. Chem. 271:1996;26032-26043.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26032-26043
    • Wimalasena, K.1    Dharmasena, S.2    Wimalasena, D.S.3    Hughbanks-Wheaton, D.K.4
  • 15
    • 0026512737 scopus 로고
    • Chemical oxidation of N -hydroxyguanidine compounds. Release of nitric oxide, nitroxyl and possible relationship to the mechanism of biological nitric oxide generation
    • Fukuto J.M., Wallace G.C., Hszieh R., Chaudhuri G. Chemical oxidation of. N -hydroxyguanidine compounds. Release of nitric oxide, nitroxyl and possible relationship to the mechanism of biological nitric oxide generation Biochem. Pharmacol. 43:1992;607-613.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 607-613
    • Fukuto, J.M.1    Wallace, G.C.2    Hszieh, R.3    Chaudhuri, G.4
  • 17
    • 0037217551 scopus 로고    scopus 로고
    • Microperoxidase-8 catalysed nitrogen oxide formation from oxidation of N -hydroxyguanidines by hydrogen peroxide
    • Ricoux R., Boucher J.-L., Mandon D., Frapart Y.-M., Henry Y., Mansuy D., Mahy J.-P. Microperoxidase-8 catalysed nitrogen oxide formation from oxidation of. N -hydroxyguanidines by hydrogen peroxide Eur. J. Biochem. 270:2003;47-55.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 47-55
    • Ricoux, R.1    Boucher, J.-L.2    Mandon, D.3    Frapart, Y.-M.4    Henry, Y.5    Mansuy, D.6    Mahy, J.-P.7
  • 18
    • 0029915133 scopus 로고    scopus 로고
    • Oxidation of arylamidoximes by hydrogen peroxide and horseradish peroxidase in water: Easy preparation and first X-ray structure of O-(arylimidoyl)arylamidoximes
    • Boucher J.-L., Vadon S., Tomas A., Viossat A., Mansuy D. Oxidation of arylamidoximes by hydrogen peroxide and horseradish peroxidase in water: easy preparation and first X-ray structure of O-(arylimidoyl)arylamidoximes. Tetrahedron Lett. 37:1996;3113-3116.
    • (1996) Tetrahedron Lett. , vol.37 , pp. 3113-3116
    • Boucher, J.-L.1    Vadon, S.2    Tomas, A.3    Viossat, A.4    Mansuy, D.5
  • 19
    • 0024834566 scopus 로고
    • 1-(4-Chlorophenyl)-3-hydroxyguanidine and O-acyl-derivatives
    • Schantl J.G., Türk W. 1-(4-Chlorophenyl)-3-hydroxyguanidine and O-acyl-derivatives. Sci. Pharm. 57:1989;375-380.
    • (1989) Sci. Pharm. , vol.57 , pp. 375-380
    • Schantl, J.G.1    Türk, W.2
  • 20
    • 0025773013 scopus 로고
    • ω -hydroxyarginine: A possible intermediate in the biosynthesis of nitric oxide from arginine
    • ω -hydroxyarginine: a possible intermediate in the biosynthesis of nitric oxide from arginine J. Med. Chem. 34:1991;1746-1748.
    • (1991) J. Med. Chem. , vol.34 , pp. 1746-1748
    • Wallace, G.C.1    Fukuto, J.M.2
  • 21
    • 0000656689 scopus 로고
    • Syntheses and stereochemistry of amidoximes
    • Bushey D.F., Hoover F.C. Syntheses and stereochemistry of amidoximes. J. Org. Chem. 45:1980;4198-4206.
    • (1980) J. Org. Chem. , vol.45 , pp. 4198-4206
    • Bushey, D.F.1    Hoover, F.C.2
  • 23
    • 33947478356 scopus 로고
    • The chemistry of amidoximes and related compounds
    • Eloy F., Lenaers R. The chemistry of amidoximes and related compounds. Chem. Rev. 62:1962;155-183.
    • (1962) Chem. Rev. , vol.62 , pp. 155-183
    • Eloy, F.1    Lenaers, R.2
  • 24
    • 0035928820 scopus 로고    scopus 로고
    • N -Hydroxyguanidines as new heme ligands: UV-Visible, EPR, and resonance Raman studies of the interaction of various compounds bearing a C=NOH function with microperoxidase-8
    • Lefèvre-Groboillot D., Dijols S., Boucher J.-L., Mahy J.-P., Ricoux R., Desbois A., Zimmermann J.-L., Mansuy D. N -Hydroxyguanidines as new heme ligands: UV-Visible, EPR, and resonance Raman studies of the interaction of various compounds bearing a C=NOH function with microperoxidase-8 Biochemistry. 40:2001;9909-9917.
    • (2001) Biochemistry , vol.40 , pp. 9909-9917
    • Lefèvre-Groboillot, D.1    Dijols, S.2    Boucher, J.-L.3    Mahy, J.-P.4    Ricoux, R.5    Desbois, A.6    Zimmermann, J.-L.7    Mansuy, D.8
  • 25
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations
    • Cleland W.W. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim. Biophys. Acta. 67:1963;104-137.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 26
    • 0343811604 scopus 로고
    • Bovine adrenal medullary dopamine β-hydroxylase: Purification by affinity chromatography, kinetic studies and presence of essential histidyl residues
    • Aunis D., Miras-Portugal M.-T., Mandel P. Bovine adrenal medullary dopamine β-hydroxylase: purification by affinity chromatography, kinetic studies and presence of essential histidyl residues. Biochim. Biophys. Acta. 327:1973;313-327.
    • (1973) Biochim. Biophys. Acta , vol.327 , pp. 313-327
    • Aunis, D.1    Miras-Portugal, M.-T.2    Mandel, P.3
  • 27
    • 0028364425 scopus 로고
    • Nitric oxide assay using hemoglobin method
    • Murphy M.E., Noack E. Nitric oxide assay using hemoglobin method. Methods Enzymol. 233:1994;240-250.
    • (1994) Methods Enzymol. , vol.233 , pp. 240-250
    • Murphy, M.E.1    Noack, E.2
  • 28
    • 0037013431 scopus 로고    scopus 로고
    • Electrochemical and peroxidase oxidation study of N -hydroxyguanidine derivatives as NO-donors
    • Cai T., Xian M., Wang P.G. Electrochemical and peroxidase oxidation study of. N -hydroxyguanidine derivatives as NO-donors Bioorg. Med. Chem. Lett. 12:2002;1507-1510.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 1507-1510
    • Cai, T.1    Xian, M.2    Wang, P.G.3
  • 29
    • 0042062298 scopus 로고    scopus 로고
    • Oxidation of N -hydroxyguanidines by copper(II): Model systems for elucidating the physiological chemistry of the nitric oxide biosynthetic intermediate N -hydroxy-L-arginine
    • Cho J.Y., Dutton A., Miller T., Houk K.N., Fukuto J. Oxidation of. N -hydroxyguanidines by copper(II): model systems for elucidating the physiological chemistry of the nitric oxide biosynthetic intermediate N -hydroxy-L-arginine Arch. Biochem. Biophys. 417:2003;65-76.
    • (2003) Arch. Biochem. Biophys. , vol.417 , pp. 65-76
    • Cho, J.Y.1    Dutton, A.2    Miller, T.3    Houk, K.N.4    Fukuto, J.5
  • 31
    • 0034708824 scopus 로고    scopus 로고
    • ω -hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase
    • ω -hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase J. Biol. Chem. 275:2000;8582-8591.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8582-8591
    • Hirst, J.1    Goodin, D.B.2
  • 32
    • 0032497909 scopus 로고    scopus 로고
    • Microsomal cytochrome P450 dependent oxidation of N-hydroxyguanidines, amidoximes and ketoximes: Mechanism of the oxidative cleavage of their C=N(OH) bond with formation of nitrogen oxides
    • Jousserandot A., Boucher J.-L., Henry Y., Niklaus B., Clement B., Mansuy D. Microsomal cytochrome P450 dependent oxidation of N-hydroxyguanidines, amidoximes and ketoximes: mechanism of the oxidative cleavage of their C=N(OH) bond with formation of nitrogen oxides. Biochemistry. 37:1998;17179-17191.
    • (1998) Biochemistry , vol.37 , pp. 17179-17191
    • Jousserandot, A.1    Boucher, J.-L.2    Henry, Y.3    Niklaus, B.4    Clement, B.5    Mansuy, D.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.