메뉴 건너뛰기




Volumn 367, Issue 2, 2008, Pages 457-461

Elucidation of the factors affecting the oxidative activity of Acremonium sp. HI-25 ascorbate oxidase by an electrochemical approach

Author keywords

Ascorbate oxidase; Bioelectrocatalysis; Enzyme kinetics; Multicopper oxidase; p Hydroquinone derivatives

Indexed keywords

ASCORBATE OXIDASE; HYDROQUINONE DERIVATIVE;

EID: 38349048271     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.12.159     Document Type: Article
Times cited : (5)

References (22)
  • 5
    • 0037062591 scopus 로고    scopus 로고
    • Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics
    • Bertrand T., Jolivalt C., Briozzo P., Caminade E., Joly N., Madzak C., and Mougin C. Crystal structure of a four-copper laccase complexed with an arylamine: insights into substrate recognition and correlation with kinetics. Biochemistry 41 (2002) 7325-7333
    • (2002) Biochemistry , vol.41 , pp. 7325-7333
    • Bertrand, T.1    Jolivalt, C.2    Briozzo, P.3    Caminade, E.4    Joly, N.5    Madzak, C.6    Mougin, C.7
  • 7
    • 0029937108 scopus 로고    scopus 로고
    • Oxidation of phenols, anilines, and benzenethiols by fungal laccases: correlation between activity and redox potentials as well as halide inhibition
    • Xu F. Oxidation of phenols, anilines, and benzenethiols by fungal laccases: correlation between activity and redox potentials as well as halide inhibition. Biochemistry 35 (1996) 7608-7614
    • (1996) Biochemistry , vol.35 , pp. 7608-7614
    • Xu, F.1
  • 8
    • 33750310022 scopus 로고    scopus 로고
    • Structural basis of the ferrous iron specificity of the yeast ferroxidase, Fet3p
    • Stoj C.S., Augustine A.J., Zeigler L., Solomon E.I., and Kosman D.J. Structural basis of the ferrous iron specificity of the yeast ferroxidase, Fet3p,. Biochemistry 45 (2006) 12741-12749
    • (2006) Biochemistry , vol.45 , pp. 12741-12749
    • Stoj, C.S.1    Augustine, A.J.2    Zeigler, L.3    Solomon, E.I.4    Kosman, D.J.5
  • 9
    • 27344435602 scopus 로고    scopus 로고
    • The copper-iron connection in biology: structure of the metallo-oxidase Fet3p
    • Taylor A.B., Stoj C.S., Ziegler L., Kosman D.J., and Hart P.J. The copper-iron connection in biology: structure of the metallo-oxidase Fet3p. Proc. Natl. Acad. Sci. 102 (2005) 15459-15464
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 15459-15464
    • Taylor, A.B.1    Stoj, C.S.2    Ziegler, L.3    Kosman, D.J.4    Hart, P.J.5
  • 10
    • 0028033749 scopus 로고
    • Substrate specificity of ascorbate oxidase: unexpected similarity to the reduction site of dopamine β-monooxygenase
    • Wimalasena K., and Dharmasena S. Substrate specificity of ascorbate oxidase: unexpected similarity to the reduction site of dopamine β-monooxygenase. Biochem. Biophys. Res. Commun. 203 (1994) 1471-1476
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 1471-1476
    • Wimalasena, K.1    Dharmasena, S.2
  • 12
    • 0030888155 scopus 로고    scopus 로고
    • Inhibition of ascorbate oxidase by phenolic compounds, enzymatic and spectroscopic studies
    • Gaspard S., Monzani E., Casella L., Gullotti M., Maritano S., and Marchesini A. Inhibition of ascorbate oxidase by phenolic compounds, enzymatic and spectroscopic studies. Biochemistry 36 (1997) 4852-4859
    • (1997) Biochemistry , vol.36 , pp. 4852-4859
    • Gaspard, S.1    Monzani, E.2    Casella, L.3    Gullotti, M.4    Maritano, S.5    Marchesini, A.6
  • 13
    • 33846682551 scopus 로고    scopus 로고
    • Ascorbate oxidase-catalyzed electrochemical reduction of dioxygen using 2,6-dichloroindophenol as an electron-transfer mediator
    • Murata K., Sugihara M., Nakamura N., and Ohno H. Ascorbate oxidase-catalyzed electrochemical reduction of dioxygen using 2,6-dichloroindophenol as an electron-transfer mediator. Chem. Lett. 35 (2006) 1232-1233
    • (2006) Chem. Lett. , vol.35 , pp. 1232-1233
    • Murata, K.1    Sugihara, M.2    Nakamura, N.3    Ohno, H.4
  • 14
    • 38349063461 scopus 로고    scopus 로고
    • P.M.H. Kroneck, F.A. Armstrong, H. Merkle, A. Marchesini, Ascorbate oxidase: molecular properties and catalytic activity, in: P.A. Seib, B.M. Tolbert (Eds.), Ascorbic Acid: Chemistry, Metabolism, and Uses, Advances in Chemistry Series, vol. 200, ACS, Washington, DC, 1982, pp. 223-248.
  • 15
    • 0036827246 scopus 로고    scopus 로고
    • Theory of steady-state catalytic current of mediated bioelectrocatalysis
    • Matsumoto R., Kano K., and Ikeda T. Theory of steady-state catalytic current of mediated bioelectrocatalysis. J. Electroanal. Chem. 535 (2002) 37-40
    • (2002) J. Electroanal. Chem. , vol.535 , pp. 37-40
    • Matsumoto, R.1    Kano, K.2    Ikeda, T.3
  • 17
    • 0031033309 scopus 로고    scopus 로고
    • Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases
    • Xu F. Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases. J. Biol. Chem. 272 (1997) 924-928
    • (1997) J. Biol. Chem. , vol.272 , pp. 924-928
    • Xu, F.1
  • 22
    • 1542345413 scopus 로고    scopus 로고
    • Probing the location of the substrate binding site of ascorbate oxidase near type 1 copper: an investigation through spectroscopic, inhibition and docking studies
    • Santagostini L., Gullotti M., Gioia L.D., Fantucci P., Franzini E., Marchesini A., Monzani E., and Casella L. Probing the location of the substrate binding site of ascorbate oxidase near type 1 copper: an investigation through spectroscopic, inhibition and docking studies. Int. J. Biochem. Cell Biol. 36 (2004) 881-892
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 881-892
    • Santagostini, L.1    Gullotti, M.2    Gioia, L.D.3    Fantucci, P.4    Franzini, E.5    Marchesini, A.6    Monzani, E.7    Casella, L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.