메뉴 건너뛰기




Volumn 46, Issue 27, 2007, Pages 8017-8023

The redox properties of ascorbate peroxidase

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBATE PEROXIDASE; OXIDATIVE REACTIVITY; REDOX PROPERTIES;

EID: 34447334828     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7006492     Document Type: Article
Times cited : (34)

References (38)
  • 2
    • 0001001527 scopus 로고
    • Chemical Nature of the Secondary hydrogen peroxide compound formed by CcP and HRP
    • George, P. (1952) Chemical Nature of the Secondary hydrogen peroxide compound formed by CcP and HRP, Nature 169, 612-613.
    • (1952) Nature , vol.169 , pp. 612-613
    • George, P.1
  • 3
    • 0006563646 scopus 로고
    • The chemical nature of the second hydrogen peroxide compound formed by CcP and HRP
    • George, P. (1953) The chemical nature of the second hydrogen peroxide compound formed by CcP and HRP, Biochem. J. 54, 267-276.
    • (1953) Biochem. J , vol.54 , pp. 267-276
    • George, P.1
  • 4
    • 0030060369 scopus 로고    scopus 로고
    • The structure/function relationship and reduction potentials of high oxidation states of myoglobin and peroxidase
    • He, B., Sinclair, R., Copeland, B. R., Makino, R., and Powers, L. S. (1996) The structure/function relationship and reduction potentials of high oxidation states of myoglobin and peroxidase, Biochemistry 35, 2413-2420.
    • (1996) Biochemistry , vol.35 , pp. 2413-2420
    • He, B.1    Sinclair, R.2    Copeland, B.R.3    Makino, R.4    Powers, L.S.5
  • 5
    • 0028283661 scopus 로고
    • Oxidation-reduction properties of compounds I and II of Arthromyces ramosus peroxidase
    • Farhangrazi, Z. S., Copeland, B. R., Nakayama, T., Yamazaki, I., and Powers, L. S. (1994) Oxidation-reduction properties of compounds I and II of Arthromyces ramosus peroxidase, Biochemistry 33, 5647-5652.
    • (1994) Biochemistry , vol.33 , pp. 5647-5652
    • Farhangrazi, Z.S.1    Copeland, B.R.2    Nakayama, T.3    Yamazaki, I.4    Powers, L.S.5
  • 6
    • 0016410948 scopus 로고
    • Measurement of Enzyme E°′ values by Optically Transparent Thin Layer Electrochemical Cells
    • Heineman, W. R., Norris, B. J., and Goelz, J. F. (1975) Measurement of Enzyme E°′ values by Optically Transparent Thin Layer Electrochemical Cells, Anal. Chem. 47, 79-84.
    • (1975) Anal. Chem , vol.47 , pp. 79-84
    • Heineman, W.R.1    Norris, B.J.2    Goelz, J.F.3
  • 8
    • 0002671450 scopus 로고
    • Electrochemical and Spectroelectrochemical Studies of Biological Redox Components
    • Kadish, K. M, Ed, pp, American Chemical Society, Washington DC
    • Taniguchi, V. T., Ellis, W. R., Jr., Cammarata, V., Webb, J., Anson, F. C., and Gray, H. B. (1982) Electrochemical and Spectroelectrochemical Studies of Biological Redox Components, in Advances in Chemistry Series (Kadish, K. M., Ed.) pp 51-68, American Chemical Society, Washington DC.
    • (1982) Advances in Chemistry Series , pp. 51-68
    • Taniguchi, V.T.1    Ellis Jr., W.R.2    Cammarata, V.3    Webb, J.4    Anson, F.C.5    Gray, H.B.6
  • 9
    • 0028925951 scopus 로고
    • Variable-temperature spectroelectrochemical study of horseradish peroxidase
    • Farhangrazi, Z. S., Fossett, M. E., Powers, L. S., and Ellis, W. R. (1995) Variable-temperature spectroelectrochemical study of horseradish peroxidase, Biochemistry 34, 2866-2871.
    • (1995) Biochemistry , vol.34 , pp. 2866-2871
    • Farhangrazi, Z.S.1    Fossett, M.E.2    Powers, L.S.3    Ellis, W.R.4
  • 10
    • 0032533557 scopus 로고    scopus 로고
    • Mediator-Assisted Continuous-Flow Column Electrolytic Spectroelectrochemical Technique for the Measurement of Protein Redox Potentials. Application to Peroxidase
    • Torimura, M., Mochuziki, M., Kano, K., Ikeda, T., and Ueda, T. (1998) Mediator-Assisted Continuous-Flow Column Electrolytic Spectroelectrochemical Technique for the Measurement of Protein Redox Potentials. Application to Peroxidase, Anal. Chem. 70, 4690-4695.
    • (1998) Anal. Chem , vol.70 , pp. 4690-4695
    • Torimura, M.1    Mochuziki, M.2    Kano, K.3    Ikeda, T.4    Ueda, T.5
  • 11
    • 0000462317 scopus 로고    scopus 로고
    • Direct measurement of the reduction potentials of catalytically active cytochrome c peroxidase compound I: Voltammetric detection of a reversible, cooperative two-electron transfer reaction
    • Mondal, M. S., Fuller, H. A., and Armstrong, F. A. (1996) Direct measurement of the reduction potentials of catalytically active cytochrome c peroxidase compound I: voltammetric detection of a reversible, cooperative two-electron transfer reaction, J. Am. Chem. Soc. 118, 263-264.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 263-264
    • Mondal, M.S.1    Fuller, H.A.2    Armstrong, F.A.3
  • 12
    • 0034792757 scopus 로고    scopus 로고
    • Redox properties of the couple compound I/native enzyme of myeloperoxidase and eosinophil peroxidases
    • Arnold, J., Furtmuller, P. G., Regelsberger, G., and Obinger, C. (2001) Redox properties of the couple compound I/native enzyme of myeloperoxidase and eosinophil peroxidases, Eur. J. Biochem. 268, 5142-5148.
    • (2001) Eur. J. Biochem , vol.268 , pp. 5142-5148
    • Arnold, J.1    Furtmuller, P.G.2    Regelsberger, G.3    Obinger, C.4
  • 14
    • 0037423684 scopus 로고    scopus 로고
    • Redox properties of the couple compound I/compound II and compound II/native enzyme of human myeloperoxidase
    • Furtmuller, P. G., Arnold, J., Jantschko, W., Pichler, H., and Obinger, C. (2003) Redox properties of the couple compound I/compound II and compound II/native enzyme of human myeloperoxidase, Biochem. Biophys. Res. Commun. 301, 551-557.
    • (2003) Biochem. Biophys. Res. Commun , vol.301 , pp. 551-557
    • Furtmuller, P.G.1    Arnold, J.2    Jantschko, W.3    Pichler, H.4    Obinger, C.5
  • 17
    • 0037137219 scopus 로고    scopus 로고
    • Substrate binding and catalytic mechanism in ascorbate peroxidase: Evidence for two ascorbate binding sites
    • Lad, L., Mewies, M., and Raven, E. L. (2002) Substrate binding and catalytic mechanism in ascorbate peroxidase: evidence for two ascorbate binding sites, Biochemistry 41, 13774-13781.
    • (2002) Biochemistry , vol.41 , pp. 13774-13781
    • Lad, L.1    Mewies, M.2    Raven, E.L.3
  • 18
    • 33746883936 scopus 로고    scopus 로고
    • Macdonald, I. K., Badyal, S. K., Ghamsari, L., Moody, P. C. E., and Raven, E. L. (2006) The Interaction of Ascorbate Peroxidase with Substrates: a Mechanistic and Structural Analysis, Biochemistry 45, 7808-7817.
    • Macdonald, I. K., Badyal, S. K., Ghamsari, L., Moody, P. C. E., and Raven, E. L. (2006) The Interaction of Ascorbate Peroxidase with Substrates: a Mechanistic and Structural Analysis, Biochemistry 45, 7808-7817.
  • 19
    • 0028901185 scopus 로고
    • Crystal structure of recombinant pea cytosolic ascorbate peroxidase
    • Patterson, W. R., and Poulos, T. L. (1995) Crystal structure of recombinant pea cytosolic ascorbate peroxidase, Biochemistry 34, 4331-4341.
    • (1995) Biochemistry , vol.34 , pp. 4331-4341
    • Patterson, W.R.1    Poulos, T.L.2
  • 20
    • 27444436075 scopus 로고    scopus 로고
    • Redox and spectroscopic properties of human indoleamine 2,3-dioxygenase and a His303Ala variant: Implications for catalysis
    • Papadopoulou, N. D., Mewies, M., McLean, K. J., Seward, H. E., Svistunenko, D. A., Munro, A. W., and Raven, E. L. (2005) Redox and spectroscopic properties of human indoleamine 2,3-dioxygenase and a His303Ala variant: implications for catalysis, Biochemistry 44, 14318-14328.
    • (2005) Biochemistry , vol.44 , pp. 14318-14328
    • Papadopoulou, N.D.1    Mewies, M.2    McLean, K.J.3    Seward, H.E.4    Svistunenko, D.A.5    Munro, A.W.6    Raven, E.L.7
  • 21
    • 0002435359 scopus 로고
    • Curti, B, Ronchi, S, and Zanetti, G, Eds, pp, Walter de Gruyter & Co, New York
    • Massey, V. (1991) in Flavins and Flavoproteins (Curti, B., Ronchi, S., and Zanetti, G., Eds.) pp 59-66, Walter de Gruyter & Co., New York.
    • (1991) Flavins and Flavoproteins , pp. 59-66
    • Massey, V.1
  • 23
    • 34447321539 scopus 로고    scopus 로고
    • Binstead, R. A, and Zuberbuehler, A. D, Spectrum Software Associates, Chapel Hill, NC
    • Binstead, R. A., and Zuberbuehler, A. D., Spectrum Software Associates, Chapel Hill, NC.
  • 24
    • 0032535122 scopus 로고    scopus 로고
    • Class I heme peroxidases: Characterisation of soybean ascorbate peroxidase
    • Jones, D. K., Dalton, D. A., Rosell, F. I., and Lloyd Raven, E. (1998) Class I heme peroxidases: characterisation of soybean ascorbate peroxidase, Arch. Biochem. Biophys. 360, 173-178.
    • (1998) Arch. Biochem. Biophys , vol.360 , pp. 173-178
    • Jones, D.K.1    Dalton, D.A.2    Rosell, F.I.3    Lloyd Raven, E.4
  • 26
    • 0001372224 scopus 로고    scopus 로고
    • Energetics of cation radical formation at the proximal active site tryptophan of cytochrome c peroxidase and ascorbate peroxidase
    • Jensen, G. M. (1998) Energetics of cation radical formation at the proximal active site tryptophan of cytochrome c peroxidase and ascorbate peroxidase, J. Phys. Chem. 102, 8221-8228.
    • (1998) J. Phys. Chem , vol.102 , pp. 8221-8228
    • Jensen, G.M.1
  • 27
    • 0034602533 scopus 로고    scopus 로고
    • Two-electron reduction and one-electron oxidation of organic hydroperoxides by human myleoperoxidase
    • Furtmuller, P. G., Burner, U., Jantschko, W., Regelsberger, G., and Obinger, C. (2000) Two-electron reduction and one-electron oxidation of organic hydroperoxides by human myleoperoxidase, FEBS Lett. 484, 139-143.
    • (2000) FEBS Lett , vol.484 , pp. 139-143
    • Furtmuller, P.G.1    Burner, U.2    Jantschko, W.3    Regelsberger, G.4    Obinger, C.5
  • 28
    • 0042474177 scopus 로고    scopus 로고
    • Understanding functional diversity and substrate specificity in haem peroxidases: What can we learn from ascorbate peroxidase?
    • Raven, E. L. (2003) Understanding functional diversity and substrate specificity in haem peroxidases: what can we learn from ascorbate peroxidase?, Nat. Prod. Rep. 20, 367-381.
    • (2003) Nat. Prod. Rep , vol.20 , pp. 367-381
    • Raven, E.L.1
  • 29
    • 1642561658 scopus 로고    scopus 로고
    • Defining substrate specificity in haem peroxidases
    • Sharp, K. H., Moody, P. C. E., and Raven, E. L. (2003) Defining substrate specificity in haem peroxidases, Dalton Trans. 4208-4215.
    • (2003) Dalton Trans , pp. 4208-4215
    • Sharp, K.H.1    Moody, P.C.E.2    Raven, E.L.3
  • 30
    • 0037388770 scopus 로고    scopus 로고
    • The crystal structure of the ascorbate peroxidase/ascorbate complex
    • Sharp, K. H., Mewies, M., Moody, P. C. E., and Raven, E. L. (2003) The crystal structure of the ascorbate peroxidase/ascorbate complex, Nat. Struct. Biol. 10, 303-307.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 303-307
    • Sharp, K.H.1    Mewies, M.2    Moody, P.C.E.3    Raven, E.L.4
  • 32
    • 0036304241 scopus 로고    scopus 로고
    • The role of histidine 42 in ascorbate peroxidase: Kinetic analysis of the H42A and H42E variants
    • Lad, L., Mewies, M., Basran, J., Scrutton, N. S., and Raven, E. L. (2002) The role of histidine 42 in ascorbate peroxidase: kinetic analysis of the H42A and H42E variants, Eur. J. Biochem. 369, 3182-3192.
    • (2002) Eur. J. Biochem , vol.369 , pp. 3182-3192
    • Lad, L.1    Mewies, M.2    Basran, J.3    Scrutton, N.S.4    Raven, E.L.5
  • 33
    • 0016682440 scopus 로고
    • Effrects of 2,4-substituents of deuteroheme upon redox potentials of horseradish peroxidases
    • Yamada, H., Makino, R., and Yamazaki, I. (1975) Effrects of 2,4-substituents of deuteroheme upon redox potentials of horseradish peroxidases, Arch. Biochem. Biophys. 169, 344-353.
    • (1975) Arch. Biochem. Biophys , vol.169 , pp. 344-353
    • Yamada, H.1    Makino, R.2    Yamazaki, I.3
  • 34
    • 0017137164 scopus 로고
    • Oxidation-reduction potential measurements on chloroperoxidase and its complexes
    • Makino, R., Chiang, R., and Hager, L. P. (1976) Oxidation-reduction potential measurements on chloroperoxidase and its complexes, Biochemistry 15, 4748-4754.
    • (1976) Biochemistry , vol.15 , pp. 4748-4754
    • Makino, R.1    Chiang, R.2    Hager, L.P.3
  • 36
    • 0018273821 scopus 로고
    • Oxidation-reduction potential measurements of cytochrome c peroxidase and pH dependent spectral transitions in the ferrous enzyme
    • Conroy, C. W., Tyma, P., Daum, P. H., and Erman, J. E. (1978) Oxidation-reduction potential measurements of cytochrome c peroxidase and pH dependent spectral transitions in the ferrous enzyme, Biochim. Biophys. Acta 537, 62-69.
    • (1978) Biochim. Biophys. Acta , vol.537 , pp. 62-69
    • Conroy, C.W.1    Tyma, P.2    Daum, P.H.3    Erman, J.E.4
  • 37
    • 0022259864 scopus 로고
    • The effect of chloride on the redox and EPR properties of myeloperoxidase
    • Ikeda-Saito, M., and Prince, R. C. (1985) The effect of chloride on the redox and EPR properties of myeloperoxidase, J. Biol. Chem. 260, 8301-8305.
    • (1985) J. Biol. Chem , vol.260 , pp. 8301-8305
    • Ikeda-Saito, M.1    Prince, R.C.2
  • 38
    • 0020989338 scopus 로고
    • The reduction potential of lactoperoxidase
    • Ohlsson, P. I., and Paul, G. (1983) The reduction potential of lactoperoxidase, Acta. Chem. Scand 37, 917-921.
    • (1983) Acta. Chem. Scand , vol.37 , pp. 917-921
    • Ohlsson, P.I.1    Paul, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.