메뉴 건너뛰기




Volumn 1650, Issue 1-2, 2003, Pages 128-135

Solvent deuterium isotope effect on the oxidation of o-diphenols by tyrosinase

Author keywords

Isotope effect; Mushroom; Phenol; Polyphenol oxidase; Tyrosinase

Indexed keywords

4 TERT BUTYLCATECHOL; CATECHOL; ISOTOPE; MONOPHENOL MONOOXYGENASE; WATER; CATECHOL DERIVATIVE; DEUTERIUM; P TERT BUTYL CATECHOL; P-TERT-BUTYL CATECHOL;

EID: 0141907305     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00208-5     Document Type: Article
Times cited : (18)

References (30)
  • 1
    • 0002281576 scopus 로고    scopus 로고
    • The chemistry of melanins and related metabolites
    • Oxford: Univ. Press
    • Prota G., d'Ischia M., Napolitano A. The chemistry of melanins and related metabolites. The Pigmentary System. 1998;Univ. Press, Oxford.
    • (1998) The Pigmentary System
    • Prota, G.1    D'Ischia, M.2    Napolitano, A.3
  • 4
    • 0031213675 scopus 로고    scopus 로고
    • Sequence and structural features of plant and fungal tyrosinases
    • Van Gelder C.W.G., Flurkey W.H.F., Wichers H.J. Sequence and structural features of plant and fungal tyrosinases. Phytochemistry. 45:1997;1309-1323.
    • (1997) Phytochemistry , vol.45 , pp. 1309-1323
    • Van Gelder, C.W.G.1    Flurkey, W.H.F.2    Wichers, H.J.3
  • 5
    • 0002218318 scopus 로고
    • Structure and functions of the phenolase complex
    • Mason H.S. Structure and functions of the phenolase complex. Nature. 177:1956;79-81.
    • (1956) Nature , vol.177 , pp. 79-81
    • Mason, H.S.1
  • 9
    • 0025007218 scopus 로고
    • Agaricus bisporus metapotyrosinase: Preparation, characterization, and conversion to mixed-metal derivatives of the binuclear site
    • Yong G., Leone O., Strothkamp K.G. Agaricus bisporus metapotyrosinase: preparation, characterization, and conversion to mixed-metal derivatives of the binuclear site. Biochemistry. 29:1990;9684-9690.
    • (1990) Biochemistry , vol.29 , pp. 9684-9690
    • Yong, G.1    Leone, O.2    Strothkamp, K.G.3
  • 13
    • 0027453615 scopus 로고
    • Effect of L-ascorbic acid on the monophenolase activity of tyrosinase
    • Ros J.R., Rodríguez López J.N., García Cánovas F. Effect of L-ascorbic acid on the monophenolase activity of tyrosinase. Biochem. J. 295:1993;309-312.
    • (1993) Biochem. J. , vol.295 , pp. 309-312
    • Ros, J.R.1    Rodríguez López, J.N.2    García Cánovas, F.3
  • 18
    • 0028176278 scopus 로고
    • Inhibitor binding to the binuclear active site of tyrosinase: Temperature, pH, and solvent deuterium isotope effects
    • Conrad J.S., Dawson S.R., Hubbard E.R., Meyers T.E., Strothkamp K.G. Inhibitor binding to the binuclear active site of tyrosinase: temperature, pH, and solvent deuterium isotope effects. Biochemistry. 33:1994;5739-5744.
    • (1994) Biochemistry , vol.33 , pp. 5739-5744
    • Conrad, J.S.1    Dawson, S.R.2    Hubbard, E.R.3    Meyers, T.E.4    Strothkamp, K.G.5
  • 20
    • 0014939358 scopus 로고
    • Physicochemical and kinetic properties of mushroom tyrosinase
    • Duckworth H.W., Coleman J.E. Physicochemical and kinetic properties of mushroom tyrosinase. J. Biol. Chem. 245:1970;1613-1625.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1613-1625
    • Duckworth, H.W.1    Coleman, J.E.2
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quatification of microgram quatities of proteins utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quatification of microgram quatities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-256.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-256
    • Bradford, M.M.1
  • 22
    • 0017191181 scopus 로고
    • Calculating extinction coefficients for enzymatically produced o-quinones
    • Waite J.H. Calculating extinction coefficients for enzymatically produced o-quinones. Anal. Biochem. 75:1976;211-218.
    • (1976) Anal. Biochem. , vol.75 , pp. 211-218
    • Waite, J.H.1
  • 25
    • 0000169232 scopus 로고
    • An algorithm for least-squares estimation of nonlinear parameters
    • Marquardt D.W. An algorithm for least-squares estimation of nonlinear parameters. J. Soc. Ind. Appl. Math. 11:1963;431-441.
    • (1963) J. Soc. Ind. Appl. Math. , vol.11 , pp. 431-441
    • Marquardt, D.W.1
  • 27
    • 0033983446 scopus 로고    scopus 로고
    • Use of a Windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions
    • Garcia-Sevilla F., Garrido-del Solo C., Duggleby R.G., Garcia-Canovas F., Pedro R., Varon R. Use of a Windows program for simulation of the progress curves of reactants and intermediates involved in enzyme-catalyzed reactions. Biosystems. 54:1999;151-164.
    • (1999) Biosystems , vol.54 , pp. 151-164
    • Garcia-Sevilla, F.1    Garrido-Del Solo, C.2    Duggleby, R.G.3    Garcia-Canovas, F.4    Pedro, R.5    Varon, R.6
  • 28
    • 0020346954 scopus 로고
    • Solvent isotope effects on enzyme systems
    • Schowen K.B., Schowen R.L. Solvent isotope effects on enzyme systems. Methods Enzymol. 87:1982;551-606.
    • (1982) Methods Enzymol. , vol.87 , pp. 551-606
    • Schowen, K.B.1    Schowen, R.L.2
  • 29
    • 0009942589 scopus 로고
    • W.W. Cleland, M.H. O'Leary, & D.B. Northrop. Baltimore, MD: University Park Press
    • Schowen R.L. Cleland W.W., O'Leary M.H., Northrop D.B. Isotope Effects on Enzyme-Catalyzed Reactions. 1977;64-99 University Park Press, Baltimore, MD.
    • (1977) Isotope Effects on Enzyme-Catalyzed Reactions , pp. 64-99
    • Schowen, R.L.1
  • 30
    • 0003946118 scopus 로고
    • E. Caldin, & V. Gold. New York: Wiley
    • Albery J. Caldin E., Gold V. Proton-Transfer Reactions. 1975;263-315 Wiley, New York.
    • (1975) Proton-Transfer Reactions , pp. 263-315
    • Albery, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.