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Volumn 3, Issue 10, 1996, Pages 851-857

Identification and localization of a stable sulfenic acid in peroxide- treated tetrachlorohydroquinone dehalogenase using electrospray mass spectrometry

Author keywords

glutathione S transferase; sulfenic acid; tetrachlorohydroquinone dehalogenase

Indexed keywords


EID: 0030266779     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/s1074-5521(96)90071-x     Document Type: Article
Times cited : (27)

References (22)
  • 1
    • 0026743357 scopus 로고
    • Purification and characterization of a tetrachloro-p-hydroquinone reductive dehalogenase from a Flavobacterium sp.
    • Xun, L., Topp, E. & Orser, C.S. (1992). Purification and characterization of a tetrachloro-p-hydroquinone reductive dehalogenase from a Flavobacterium sp. J. Bacteriol. 174, 8003-8007.
    • (1992) J. Bacteriol. , vol.174 , pp. 8003-8007
    • Xun, L.1    Topp, E.2    Orser, C.S.3
  • 2
    • 0026555180 scopus 로고
    • Glutathione is the reducing agent for the reductive dehalogenation of tetrachloro-p-hydroquinone by extracts from a Flavobacterium sp.
    • Xun, L., Topp, E. & Orser, C.S. (1992). Glutathione is the reducing agent for the reductive dehalogenation of tetrachloro-p-hydroquinone by extracts from a Flavobacterium sp. Biochem. Biophys. Res. Commun. 182, 361-366.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 361-366
    • Xun, L.1    Topp, E.2    Orser, C.S.3
  • 3
    • 0030445133 scopus 로고    scopus 로고
    • Exploration of the relationship between tetrachlorohydroquinone dehalogenase and the glutathione S-transferase superfamily
    • in press
    • McCarthy, D.L., Navarette, S., Willett, S.W., Babbitt, P.C. & Copley, S. D. (1996). Exploration of the relationship between tetrachlorohydroquinone dehalogenase and the glutathione S-transferase superfamily. Biochemistry, in press.
    • (1996) Biochemistry
    • McCarthy, D.L.1    Navarette, S.2    Willett, S.W.3    Babbitt, P.C.4    Copley, S.D.5
  • 4
    • 0030010730 scopus 로고    scopus 로고
    • A structurally derived consensus pattern for theta class glutathione transferases
    • Rossjohn, J., Board, P.G., Parker, M.W. & Wilce, M.C.J. (1996). A structurally derived consensus pattern for theta class glutathione transferases. Protein Eng. 9, 327-332.
    • (1996) Protein Eng. , vol.9 , pp. 327-332
    • Rossjohn, J.1    Board, P.G.2    Parker, M.W.3    Wilce, M.C.J.4
  • 6
    • 0007154605 scopus 로고
    • The reaction of tobacco mosaic virus with iodine
    • Fraenkel-Conrat, H. (1955). The reaction of tobacco mosaic virus with iodine. J. Biol. Chem. 217, 373-381.
    • (1955) J. Biol. Chem. , vol.217 , pp. 373-381
    • Fraenkel-Conrat, H.1
  • 7
    • 0024339293 scopus 로고
    • The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid
    • Poole, L.B. & Claiborne, A. (1989). The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid. J. Biol. Chem. 264, 12330-12338.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12330-12338
    • Poole, L.B.1    Claiborne, A.2
  • 8
    • 0024351073 scopus 로고
    • The streptococcal flavoprotein NADH oxidase. 1. Evidence linking NADH oxidase and NADH peroxidase cysteinyl redox centers
    • Ahmed, S.A. & Claiborne, A. (1989). The streptococcal flavoprotein NADH oxidase. 1. Evidence linking NADH oxidase and NADH peroxidase cysteinyl redox centers. J. Biol. Chem. 264, 19856-19863.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19856-19863
    • Ahmed, S.A.1    Claiborne, A.2
  • 9
    • 0027131771 scopus 로고
    • Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation
    • Claiborne, A., Miller, H., Parsonage, D. & Ross, R.P. (1993). Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. FASEB J. 7, 1483-1490.
    • (1993) FASEB J. , vol.7 , pp. 1483-1490
    • Claiborne, A.1    Miller, H.2    Parsonage, D.3    Ross, R.P.4
  • 10
    • 0025988889 scopus 로고
    • Peroxide modification of monoalkylated glutathione reductase: Stabilization of an active-site cysteine sulfenic acid
    • Miller, H. & Claiborne, A. (1991). Peroxide modification of monoalkylated glutathione reductase: stabilization of an active-site cysteine sulfenic acid. J. Biol. Chem. 266, 19342-19350.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19342-19350
    • Miller, H.1    Claiborne, A.2
  • 11
    • 0029160661 scopus 로고
    • Reaction of nitric oxide with the free sulfhydryl group of human serum albumin yields a sulfenic acid and nitrous oxide
    • DeMaster, E.G., Quast, B.J., Redfern, B. & Nagasawa, H.T. (1995). Reaction of nitric oxide with the free sulfhydryl group of human serum albumin yields a sulfenic acid and nitrous oxide. Biochemistry 34, 11494-11499.
    • (1995) Biochemistry , vol.34 , pp. 11494-11499
    • DeMaster, E.G.1    Quast, B.J.2    Redfern, B.3    Nagasawa, H.T.4
  • 12
  • 13
    • 0001637467 scopus 로고
    • Formation and reactions of sulfenic acids in proteins
    • Allison, W.S. (1976). Formation and reactions of sulfenic acids in proteins. Accounts Chem. Res. 9, 293-299.
    • (1976) Accounts Chem. Res. , vol.9 , pp. 293-299
    • Allison, W.S.1
  • 14
    • 0018085238 scopus 로고
    • The accessible cysteine residue of human transcortin: Evidence for oxidation of the sulphydryl group
    • Le Gaillard, F. & Dautrevaux, M. (1978). The accessible cysteine residue of human transcortin: evidence for oxidation of the sulphydryl group. FEBS Lett. 94, 63-67.
    • (1978) FEBS Lett. , vol.94 , pp. 63-67
    • Le Gaillard, F.1    Dautrevaux, M.2
  • 15
    • 0028087744 scopus 로고
    • A misfolded but active dimer of bovine seminal ribonuclease
    • Kim, J.-S. & Raines, R.T. (1994). A misfolded but active dimer of bovine seminal ribonuclease. Eur. J. Biochem. 224, 109-114.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 109-114
    • Kim, J.-S.1    Raines, R.T.2
  • 16
    • 0023658381 scopus 로고
    • The elucidation of the microheterogeneity of highly purified p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by various biochemical techniques
    • van Berkel, W.J.H. & Müller, F. (1987). The elucidation of the microheterogeneity of highly purified p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by various biochemical techniques. Eur. J. Biochem. 167, 35-46.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 35-46
    • Van Berkel, W.J.H.1    Müller, F.2
  • 17
    • 0016256290 scopus 로고
    • The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins
    • Benitez, L.V. & Allison, W.S. (1974). The inactivation of the acyl phosphatase activity catalyzed by the sulfenic acid form of glyceraldehyde 3-phosphate dehydrogenase by dimedone and olefins. J. Biol. Chem. 249, 6234-6243.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6234-6243
    • Benitez, L.V.1    Allison, W.S.2
  • 18
    • 0029737618 scopus 로고    scopus 로고
    • Structure of the native cysteine-sulfenic acid redox center of Enterococcal NADH peroxidase refined at 2.8 A resolution
    • Yeh, J.I., Claiborne, A. & Hol, W.G. (1996). Structure of the native cysteine-sulfenic acid redox center of Enterococcal NADH peroxidase refined at 2.8 A resolution. Biochemistry 35, 9951-9957.
    • (1996) Biochemistry , vol.35 , pp. 9951-9957
    • Yeh, J.I.1    Claiborne, A.2    Hol, W.G.3
  • 20
    • 0029003807 scopus 로고
    • Crystal structure of a theta-class glutathione transferase
    • Wilce, M.C.J., Board, P.G., Feil, S.C. & Parker, M.W. (1995). Crystal structure of a theta-class glutathione transferase. EMBO J. 14, 2133-2143.
    • (1995) EMBO J. , vol.14 , pp. 2133-2143
    • Wilce, M.C.J.1    Board, P.G.2    Feil, S.C.3    Parker, M.W.4
  • 21
    • 0029101750 scopus 로고
    • Evidence for an essential serine residue in the active site of the theta class glutathione transferases
    • Board, P.G., Coggan, M. & Wilce, M.C.J. & Parker, M.W. (1995). Evidence for an essential serine residue in the active site of the theta class glutathione transferases. Biochem. J. 311, 247-250.
    • (1995) Biochem. J. , vol.311 , pp. 247-250
    • Board, P.G.1    Coggan, M.2    Wilce, M.C.J.3    Parker, M.W.4
  • 22
    • 0027204866 scopus 로고
    • Characterization of a Flavobacterium glutathione S-transferase gene involved in reductive dechlorination
    • Orser, C.S., Dutton, J., Lange, C., Jablonski, P., Xun, L. & Hargis, M. (1993). Characterization of a Flavobacterium glutathione S-transferase gene involved in reductive dechlorination. J. Bacteriol. 175, 2640-2644.
    • (1993) J. Bacteriol. , vol.175 , pp. 2640-2644
    • Orser, C.S.1    Dutton, J.2    Lange, C.3    Jablonski, P.4    Xun, L.5    Hargis, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.