메뉴 건너뛰기




Volumn 123, Issue 3, 1999, Pages 197-217

Inactivation of Coprinus cinereus peroxidase by 4-chloroaniline during turnover: Comparison with horseradish peroxidase and bovine lactoperoxidase

Author keywords

4 Chloroaniline; Coprinus cinereus peroxidase; Covalent binding; Electrospray MS; Heme; Inactivation; MALDI TOF MS; Peptide mapping; Suicide substrate

Indexed keywords

4 CHLOROANILINE; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE; LACTOPEROXIDASE; PEROXIDASE;

EID: 0032712923     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(99)00136-2     Document Type: Article
Times cited : (25)

References (33)
  • 2
    • 0000369104 scopus 로고
    • Metabolism of 3,4-dichloroaniline by Pseudomonas putida
    • You I.S., Bartha R. Metabolism of 3,4-dichloroaniline by Pseudomonas putida. J. Agr. Food. 30:1982;274-277.
    • (1982) J. Agr. Food , vol.30 , pp. 274-277
    • You, I.S.1    Bartha, R.2
  • 4
    • 0015450233 scopus 로고
    • Biochemical transformation of herbicide-derived anilines: Purification and characterization of causative enzymes
    • Bordeleau L.M., Bartha R. Biochemical transformation of herbicide-derived anilines: purification and characterization of causative enzymes. Can. J. Micro. 18:1972;1865-1871.
    • (1972) Can. J. Micro. , vol.18 , pp. 1865-1871
    • Bordeleau, L.M.1    Bartha, R.2
  • 6
    • 0017180363 scopus 로고
    • Aerobic versus anaerobic metabolism of halogenated anilines by Paracoccus sp
    • Bollag J.-M., Russel S. Aerobic versus anaerobic metabolism of halogenated anilines by Paracoccus sp. Microb. Ecol. 3:1976;65-73.
    • (1976) Microb. Ecol. , vol.3 , pp. 65-73
    • Bollag, J.-M.1    Russel, S.2
  • 7
    • 0017610466 scopus 로고
    • Formylation and acetylation of 4-chloroaniline by a Streptomyces sp
    • Russel S., Bollag J.-M. Formylation and acetylation of 4-chloroaniline by a Streptomyces sp. Act. Micro. 26:1977;59-64.
    • (1977) Act. Micro. , vol.26 , pp. 59-64
    • Russel, S.1    Bollag, J.-M.2
  • 8
    • 84963441203 scopus 로고
    • Structural and quantitative analysis of 4-chloroaniline derived oligomers
    • Simmons K.E., Minard R.D., Freyer A.J., Bollag J.-M. Structural and quantitative analysis of 4-chloroaniline derived oligomers. Int. J. Env. A. 26:1986;209-277.
    • (1986) Int. J. Env. A. , vol.26 , pp. 209-277
    • Simmons, K.E.1    Minard, R.D.2    Freyer, A.J.3    Bollag, J.-M.4
  • 9
    • 0023427347 scopus 로고
    • Oligomerization of 4-chloroaniline by oxidoreductases
    • Simmons K.E., Minard R.D., Bollag J.-M. Oligomerization of 4-chloroaniline by oxidoreductases. Env. Sci. Tec. 21:1987;999-1003.
    • (1987) Env. Sci. Tec. , vol.21 , pp. 999-1003
    • Simmons, K.E.1    Minard, R.D.2    Bollag, J.-M.3
  • 10
    • 0015458148 scopus 로고
    • Biochemical transformation of herbicide-derived anilines requirement of molecular modification
    • Bordeleau L.M., Bartha R. Biochemical transformation of herbicide-derived anilines requirement of molecular modification. Can. J. Micro. 18:1972;1873-1882.
    • (1972) Can. J. Micro. , vol.18 , pp. 1873-1882
    • Bordeleau, L.M.1    Bartha, R.2
  • 11
    • 0027411140 scopus 로고
    • Oligomers of 4-chloroaniline are intermediates formed during its biodegradation by Phanerochaete chrysosporium
    • Chang C.W., Bumpus J.A. Oligomers of 4-chloroaniline are intermediates formed during its biodegradation by Phanerochaete chrysosporium. FEMS Microb. 107:1993;337-342.
    • (1993) FEMS Microb. , vol.107 , pp. 337-342
    • Chang, C.W.1    Bumpus, J.A.2
  • 12
    • 0021880992 scopus 로고
    • Transformation of halogen alkyl-, and alkoxy-substituted anilines by laccase of Trametes versicolor
    • Hoff T., Liu S.-Y., Bollag J.-M. Transformation of halogen alkyl-, and alkoxy-substituted anilines by laccase of Trametes versicolor. Appl. Envir. 40:1985;1040-1045.
    • (1985) Appl. Envir. , vol.40 , pp. 1040-1045
    • Hoff, T.1    Liu, S.-Y.2    Bollag, J.-M.3
  • 13
    • 0345442179 scopus 로고
    • Inactivation of lactoperoxidase by 4-chloroaniline
    • Bumpus J.A., Tatarko T., Chang C.W. Inactivation of lactoperoxidase by 4-chloroaniline. J. Agr. Food. 41:1993;2197-2201.
    • (1993) J. Agr. Food , vol.41 , pp. 2197-2201
    • Bumpus, J.A.1    Tatarko, T.2    Chang, C.W.3
  • 14
    • 0344580112 scopus 로고
    • Oxidation of 4-chloroaniline catalyzed by human myeloperoxidase
    • Bakkenist A.R.J., Plat H, Wever R. Oxidation of 4-chloroaniline catalyzed by human myeloperoxidase. Bioorg. Chem. 10:1981;324-328.
    • (1981) Bioorg. Chem. , vol.10 , pp. 324-328
    • Bakkenist, A.R.J.1    Plat, H.2    Wever, R.3
  • 15
    • 0018035455 scopus 로고
    • Chloroperoxidase-catalyzed oxidation of 4-chloroaniline to 4-chloronitrosobenzene
    • Corbett M.D., Chipko B.R., Baden D.G. Chloroperoxidase-catalyzed oxidation of 4-chloroaniline to 4-chloronitrosobenzene. Biochem. J. 175:1978;353-360.
    • (1978) Biochem. J. , vol.175 , pp. 353-360
    • Corbett, M.D.1    Chipko, B.R.2    Baden, D.G.3
  • 16
    • 0014235435 scopus 로고
    • Studies in peroxidases action-XVIII. The oxidation of 4-chloroaniline-further studies
    • Holland V.R., Saunders B.C. Studies in peroxidases action-XVIII. The oxidation of 4-chloroaniline-further studies. Tetrahedron. 24:1968;585-588.
    • (1968) Tetrahedron , vol.24 , pp. 585-588
    • Holland, V.R.1    Saunders, B.C.2
  • 18
    • 0028084782 scopus 로고
    • Three-dimentional structure of a recombinant peroxidase from Coprinus cinereus at 2.6 A resolution
    • Peterson J.F.W., Kadziola A., Larsen S. Three-dimentional structure of a recombinant peroxidase from Coprinus cinereus at 2.6 A resolution. FEBS Lett. 339:1994;291-296.
    • (1994) FEBS Lett. , vol.339 , pp. 291-296
    • Peterson, J.F.W.1    Kadziola, A.2    Larsen, S.3
  • 20
    • 33845183471 scopus 로고
    • Substrate oxidation by the heme edge of fungal peroxidases: Reaction of Coprinus cinereus peroxidase with hydrazines and sodium azide
    • Depillis G.D., Ortiz de Montellano P.R. Substrate oxidation by the heme edge of fungal peroxidases: reaction of Coprinus cinereus peroxidase with hydrazines and sodium azide. Biochem. 28:1989;7947-7952.
    • (1989) Biochem. , vol.28 , pp. 7947-7952
    • Depillis, G.D.1    Ortiz De Montellano, P.R.2
  • 21
    • 0024297764 scopus 로고
    • Mechanism-based inactivation of horseradish peroxidase by sodium azide: Formation of mesoazidoprotoporphyrin IX
    • Ortiz de Montellano P.R., David S.K., Ator M., Tew D. Mechanism-based inactivation of horseradish peroxidase by sodium azide: formation of mesoazidoprotoporphyrin IX. Biochemistry. 27:1988;5470-5476.
    • (1988) Biochemistry , vol.27 , pp. 5470-5476
    • Ortiz De Montellano, P.R.1    David, S.K.2    Ator, M.3    Tew, D.4
  • 23
    • 0029969406 scopus 로고    scopus 로고
    • Probing the aromatic-donor-binding site of horseradish peroxidase using site-directed mutagenesis and the suicide substrate phenylhydrazine
    • Gilfoyle D.J., Rodriguez-Lopez J.N., Smith A.T. Probing the aromatic-donor-binding site of horseradish peroxidase using site-directed mutagenesis and the suicide substrate phenylhydrazine. Eur. J. Bioch. 236:1996;714-722.
    • (1996) Eur. J. Bioch. , vol.236 , pp. 714-722
    • Gilfoyle, D.J.1    Rodriguez-Lopez, J.N.2    Smith, A.T.3
  • 24
    • 0027403497 scopus 로고
    • Amino acid sequence of Coprinus macrorhizus peroxidase and cDNA sequence encoding Coprinus cinereus peroxidase, a new family of fungal peroxidases
    • Baunsgaard L., Dalborg H., Houen G., Rasmussen E.M., Welinder K.G. Amino acid sequence of Coprinus macrorhizus peroxidase and cDNA sequence encoding Coprinus cinereus peroxidase, a new family of fungal peroxidases. Eur. J. Bioch. 213:1993;605-611.
    • (1993) Eur. J. Bioch. , vol.213 , pp. 605-611
    • Baunsgaard, L.1    Dalborg, H.2    Houen, G.3    Rasmussen, E.M.4    Welinder, K.G.5
  • 27
    • 0017041348 scopus 로고
    • Covalent structure of the glycoprotein horseradish peroxidase
    • Welinder K.G. Covalent structure of the glycoprotein horseradish peroxidase. FEBS Lett. 72:1976;19-23.
    • (1976) FEBS Lett. , vol.72 , pp. 19-23
    • Welinder, K.G.1
  • 28
    • 0030910381 scopus 로고    scopus 로고
    • Autocatalytic processing of heme by lactoperoxidase produces the native Protein-bound prosthetic group
    • DePillis G.D., Ozaki S-I., Kuo J.M., Maltby D.A., Ortiz de Montellano P.R. Autocatalytic processing of heme by lactoperoxidase produces the native Protein-bound prosthetic group. J. Biol. Chem. 272:1997;8857-8860.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8857-8860
    • Depillis, G.D.1    Ozaki, S.-I.2    Kuo, J.M.3    Maltby, D.A.4    Ortiz De Montellano, P.R.5
  • 29
    • 0032561204 scopus 로고    scopus 로고
    • The heme prosthetic group of lactoperoxidase: Structural characteristics of heme 1 and heme 1-peptides
    • Rae T.D., Goff H.M. The heme prosthetic group of lactoperoxidase: structural characteristics of heme 1 and heme 1-peptides. J. Bio. Mol. B. 273:1998;27968-27977.
    • (1998) J. Bio. Mol. B. , vol.273 , pp. 27968-27977
    • Rae, T.D.1    Goff, H.M.2
  • 30
    • 0021875282 scopus 로고
    • Kinetics of suicide substrates: Practical procedures for determine parameters
    • Waley S.G. Kinetics of suicide substrates: practical procedures for determine parameters. Biochem. J. 227:1985;843-849.
    • (1985) Biochem. J. , vol.227 , pp. 843-849
    • Waley, S.G.1
  • 31
    • 0028985005 scopus 로고
    • Isolation and identification of protoheme IX derivatives during autolytic cleavage of human myeloperoxidase
    • Taylor K.L., Strobel F., Yue K.T., Ram P., Pohl J, Woods A.S., Kindade J.K. Jr. Isolation and identification of protoheme IX derivatives during autolytic cleavage of human myeloperoxidase. Arch. Bioch. 316:1995;635-642.
    • (1995) Arch. Bioch. , vol.316 , pp. 635-642
    • Taylor, K.L.1    Strobel, F.2    Yue, K.T.3    Ram, P.4    Pohl, J.5    Woods, A.S.6    Kindade J.K., Jr.7
  • 32
    • 0023644531 scopus 로고
    • Protein control of prothestic heme reactivity: Reaction of substrates with the heme edge of horseradish peroxidase
    • Ator M.A., Ortiz de Montellano P.R. Protein control of prothestic heme reactivity: reaction of substrates with the heme edge of horseradish peroxidase. J. Biol. Chem. 262:1987;1542-1551.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1542-1551
    • Ator, M.A.1    Ortiz De Montellano, P.R.2
  • 33
    • 0024309382 scopus 로고
    • Reactions of protein radical in peroxide-treated myoglobin: Formation of a heme-protein cross-link
    • Catalano C.E., Choe Y.S., Ortiz de Montellano P.R. Reactions of protein radical in peroxide-treated myoglobin: formation of a heme-protein cross-link. J. Biol. Chem. 264:1989;10534-10541.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10534-10541
    • Catalano, C.E.1    Choe, Y.S.2    Ortiz De Montellano, P.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.