메뉴 건너뛰기




Volumn 269, Issue 19, 2002, Pages 4905-4911

Spectroscopic characterization and ligand-binding properties of chlorite dismutase from the chlorate respiring bacterial strain GR-1

Author keywords

Chlorate respiration; Chlorite dismutase; EPR; ESR; Heme enzyme

Indexed keywords

CHLORATE; CHLORIDE; CHLORITE DISMUTASE; ENZYME; FERRIC HYDROXIDE; GLOBIN; GUANYLATE CYCLASE; HEMOPROTEIN; HISTIDINE; HYDROGEN PEROXIDE; IMIDAZOLE; NITRIC OXIDE; NITRITE; UNCLASSIFIED DRUG;

EID: 0036403133     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03208.x     Document Type: Article
Times cited : (47)

References (30)
  • 1
    • 0030011204 scopus 로고    scopus 로고
    • Transformation of (per) chlorate into chloride by a newly isolated bacterium: Reduction and dismutation
    • Rikken, G.B., Kroon, A.G.M. & van Ginkel, C.G. (1996) Transformation of (per) chlorate into chloride by a newly isolated bacterium: reduction and dismutation. Appl. Microbiol. Biotechnol. 45, 420-426.
    • (1996) Appl. Microbiol. Biotechnol. , vol.45 , pp. 420-426
    • Rikken, G.B.1    Kroon, A.G.M.2    Van Ginkel, C.G.3
  • 2
    • 0032729246 scopus 로고    scopus 로고
    • Purification and characterization of (per) chlorate reductase from the chlorate-respiring strain GR-1
    • Kengen, S.W.M., Rikken, G.B., Hagen, W.R. & van Ginkel, C.G. & Stams, A.J.M. (1999) Purification and characterization of (per) chlorate reductase from the chlorate-respiring strain GR-1. J. Bacteriol. 181, 6706-6711.
    • (1999) J. Bacteriol. , vol.181 , pp. 6706-6711
    • Kengen, S.W.M.1    Rikken, G.B.2    Hagen, W.R.3    Van Ginkel, C.G.4    Stams, A.J.M.5
  • 3
    • 0029801773 scopus 로고    scopus 로고
    • Purification and characterization of chlorite dismutase: A novel oxygen-generating enzyme
    • Ginkel, C.G., Rikken, G.B., Kroon, A.G.M. & Kengen, S.W.M. (1996) Purification and characterization of chlorite dismutase: a novel oxygen-generating enzyme. Arch. Microbiol. 166, 321-326.
    • (1996) Arch. Microbiol. , vol.166 , pp. 321-326
    • Ginkel, C.G.1    Rikken, G.B.2    Kroon, A.G.M.3    Kengen, S.W.M.4
  • 5
    • 0034918048 scopus 로고    scopus 로고
    • Chlorite-hemoprotein interaction as key role for the pharmacological activity of the chlorite-based drug WF10
    • Schempp, H., Reim, M. & Dornisch, K. (2001) Chlorite-hemoprotein interaction as key role for the pharmacological activity of the chlorite-based drug WF10. Arzneimittelforschung 51, 554-562.
    • (2001) Arzneimittelforschung , vol.51 , pp. 554-562
    • Schempp, H.1    Reim, M.2    Dornisch, K.3
  • 6
    • 0025971461 scopus 로고
    • S=9/2 EPR signals are evidence against coupling between the siroheme and the Fe/S cluster prosthetic groups in Desulfovibrio vulgaris (Hildenborough) dissimilatory sulfite reductase
    • Pierik, A.J. & Hagen, W.R. (1991) S-9/2 EPR signals are evidence against coupling between the siroheme and the Fe/S cluster prosthetic groups in Desulfovibrio vulgaris (Hildenborough) dissimilatory sulfite reductase. Eur. J. Biochem. 195, 505-516.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 505-516
    • Pierik, A.J.1    Hagen, W.R.2
  • 7
    • 77956777769 scopus 로고
    • EPR spectroscopy of iron-sulfur proteins
    • Hagen, W.R. (1992) EPR spectroscopy of iron-sulfur proteins. Adv. Inorg. Chem. 38, 165-222.
    • (1992) Adv. Inorg. Chem. , vol.38 , pp. 165-222
    • Hagen, W.R.1
  • 9
    • 49649145902 scopus 로고
    • EPR signal intensity and powder shapes. A reexamination
    • Aasa, R. & Vänngård, T. (1975) EPR signal intensity and powder shapes. A reexamination. J. Magn. Reson. 19, 308-315.
    • (1975) J. Magn. Reson. , vol.19 , pp. 308-315
    • Aasa, R.1    Vänngård, T.2
  • 10
    • 0031984429 scopus 로고    scopus 로고
    • Heme protein radicals: Formation, fate, and biological consequences
    • Giulivi, C. & Cadenas, E. (1998) Heme protein radicals: formation, fate, and biological consequences. Free Radic. Biol. Med. 24, 269-279.
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 269-279
    • Giulivi, C.1    Cadenas, E.2
  • 11
    • 0018787247 scopus 로고
    • Electron spin resonance study of the role of nitric oxide and catalase in the activation of guanylate cyclase by sodium azide and hydroxylamine. Modulation of enzyme responses by heme proteins and their nitrosyl derivatives
    • Craven, P.A., DeRubertis, F.R. & Pratt, D.W. (1979) Electron spin resonance study of the role of nitric oxide and catalase in the activation of guanylate cyclase by sodium azide and hydroxylamine. Modulation of enzyme responses by heme proteins and their nitrosyl derivatives. J. Biol. Chem. 254, 8213-8222.
    • (1979) J. Biol. Chem. , vol.254 , pp. 8213-8222
    • Craven, P.A.1    DeRubertis, F.R.2    Pratt, D.W.3
  • 12
    • 0032497407 scopus 로고    scopus 로고
    • Structural changes in the heme proximal pocket induced by nitric oxide binding to soluble guanylate cyclase
    • Zhao, Y., Hoganson, C., Babcock, G.T. & Marletta, M.A. (1998) Structural changes in the heme proximal pocket induced by nitric oxide binding to soluble guanylate cyclase. Biochemistry. 37, 12458-12464.
    • (1998) Biochemistry , vol.37 , pp. 12458-12464
    • Zhao, Y.1    Hoganson, C.2    Babcock, G.T.3    Marletta, M.A.4
  • 13
    • 0021803386 scopus 로고
    • pH-induced cleavage of the proximal histidine to iron bond in the nitric oxide derivative of ferrous monomeric hemoproteins and of the 'chelated' protoheme model compound
    • Ascenzi, P., Coletta, M., Desideri, A. & Brunori, M. (1985) pH-induced cleavage of the proximal histidine to iron bond in the nitric oxide derivative of ferrous monomeric hemoproteins and of the 'chelated' protoheme model compound. Biochim. Biophys. Acta 829, 299-302.
    • (1985) Biochim. Biophys. Acta , vol.829 , pp. 299-302
    • Ascenzi, P.1    Coletta, M.2    Desideri, A.3    Brunori, M.4
  • 14
    • 0017593566 scopus 로고
    • 2g hole model to the directional properties of the g tensor, and a new method for calculating the ligand field parameters
    • 2g hole model to the directional properties of the g tensor, and a new method for calculating the ligand field parameters. Biochim. Biophys. Acta 491, 137-149.
    • (1977) Biochim. Biophys. Acta , vol.491 , pp. 137-149
    • Taylor, C.P.S.1
  • 15
    • 0014429411 scopus 로고
    • The electron structure of protoheme proteins. I. An electron paramagnetic resonance and optical study of horse-radish peroxidase and its derivatives
    • Blumberg, W.E., Peisach, J., Wittenberg, B.A. & Wittenberg, J.B. (1968) The electron structure of protoheme proteins. I. An electron paramagnetic resonance and optical study of horse-radish peroxidase and its derivatives. J. Biol. Chem. 243, 1854-1862.
    • (1968) J. Biol. Chem. , vol.243 , pp. 1854-1862
    • Blumberg, W.E.1    Peisach, J.2    Wittenberg, B.A.3    Wittenberg, J.B.4
  • 16
    • 0014429446 scopus 로고
    • The electron structure of protoheme proteins. II. An electron paramagnetic resonance and optical study of cytochrome c peroxidase its derivatives
    • Wittenberg, B.A., Kampa, L., Wittenberg, J.B., Blumberg, W.E. & Peisach, J. (1968) The electron structure of protoheme proteins. II. An electron paramagnetic resonance and optical study of cytochrome c peroxidase and its derivatives. J. Biol. Chem. 243, 1863-1870.
    • (1968) J. Biol. Chem. , vol.243 , pp. 1863-1870
    • Wittenberg, B.A.1    Kampa, L.2    Wittenberg, J.B.3    Blumberg, W.E.4    Peisach, J.5
  • 17
    • 0000382264 scopus 로고
    • A unified theory for low spin forms of all ferric heme proteins as studied by EPR
    • Chance, B., Yanetani, T. & Mildvan, A.S., eds. Academic Press, New York, USA
    • Blumberg, W.E. & Peisach, J. (1971) A unified theory for low spin forms of all ferric heme proteins as studied by EPR. Probes of Structure and Function of Macromolecules and Membranes (Chance, B., Yanetani, T. & Mildvan, A.S., eds), pp. 215-229. Academic Press, New York, USA.
    • (1971) Probes of Structure and Function of Macromolecules and Membranes , pp. 215-229
    • Blumberg, W.E.1    Peisach, J.2
  • 18
    • 0015239532 scopus 로고
    • Sulfheme proteins. I. Optical and magnetic properties of sulfmyoglobin and its derivatives
    • Berzofsky, J.A., Peisach, J. & Blumberg, W.E. (1971) Sulfheme proteins. I. Optical and magnetic properties of sulfmyoglobin and its derivatives. J. Biol. Chem. 246, 3367-3377.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3367-3377
    • Berzofsky, J.A.1    Peisach, J.2    Blumberg, W.E.3
  • 19
    • 0001459583 scopus 로고
    • Hemoglobin and myoglobin in their reactions with ligands
    • Neuberger, A. & Tatum, E.L., eds. North-Holland Publishing Co, Amsterdam
    • Antonini, E. & Brunori, M. (1971) Hemoglobin and myoglobin in their reactions with ligands. Frontiers of Biology (Neuberger, A. & Tatum, E.L., eds), pp. 445. North-Holland Publishing Co, Amsterdam.
    • (1971) Frontiers of Biology , pp. 445
    • Antonini, E.1    Brunori, M.2
  • 20
    • 0028228808 scopus 로고
    • Soluble guanylate cyclase from bovine lung: Activation with nitric oxide and carbonmonoxide and spectral characterization of the ferrous and ferric states
    • Stone, J.R. & Marletta, M.A. (1994) Soluble guanylate cyclase from bovine lung: activation with nitric oxide and carbonmonoxide and spectral characterization of the ferrous and ferric states. Biochemistry 33, 5636-5640.
    • (1994) Biochemistry , vol.33 , pp. 5636-5640
    • Stone, J.R.1    Marletta, M.A.2
  • 22
    • 0033377046 scopus 로고    scopus 로고
    • Studying the structure and regulation of soluble guanylyl cyclase
    • Koesling, D. (1999) Studying the structure and regulation of soluble guanylyl cyclase. Methods 19, 485-493.
    • (1999) Methods , vol.19 , pp. 485-493
    • Koesling, D.1
  • 24
    • 0016682440 scopus 로고
    • Effects of 2,4-substituents of deuteroheme upon redox potentials of horse-radish peroxidases
    • Yamada, H., Makino, R. & Yamazaki, I. (1975) Effects of 2,4-substituents of deuteroheme upon redox potentials of horse-radish 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
  • 25
    • 0010976907 scopus 로고
    • Heme Proteins and oxygen
    • Jacobs, A. & Worwood, M., eds. Academic Press, London
    • Williams, R.J.P. (1974) Heme Proteins and oxygen. In Iron in Biochemistry and Medicine (Jacobs, A. & Worwood, M., eds), pp. 183-219. Academic Press, London.
    • (1974) Iron in Biochemistry and Medicine , pp. 183-219
    • Williams, R.J.P.1
  • 26
    • 0002950246 scopus 로고
    • Oxidation-reduction potentials of the metmyoglobin-myoglobin system
    • Taylor, J.F. & Morgan, V.E. (1942) Oxidation-reduction potentials of the metmyoglobin-myoglobin system. J. Biol. Chem. 144, 15-20.
    • (1942) J. Biol. Chem. , vol.144 , pp. 15-20
    • Taylor, J.F.1    Morgan, V.E.2
  • 27
    • 0022259864 scopus 로고
    • The effect of chloride on the redox and EPR properties of myeloperoxidase
    • Ikeda-Saito, M. & 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
  • 28
    • 0025766930 scopus 로고
    • Proton NMR investigation into the basis for the relatively high redox potential of lignin peroxidase
    • Banci, L., Bertini, I., Turano, P., Tien, M. & Kirk, T.K. (1991) Proton NMR investigation into the basis for the relatively high redox potential of lignin peroxidase. Proc. Natl. Acad. Sci. USA 88, 6956-6960.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6956-6960
    • Banci, L.1    Bertini, I.2    Turano, P.3    Tien, M.4    Kirk, T.K.5
  • 29
    • 0023390322 scopus 로고
    • Oxidation of metmyoglobin by chlorite ion: A spectrophotometric study
    • Behere, D.V. & Shedbalkar, V.P. (1987) Oxidation of metmyoglobin by chlorite ion: a spectrophotometric study. Indian J. Biochem. Biophys. 24, 244-247.
    • (1987) Indian J. Biochem. Biophys. , vol.24 , pp. 244-247
    • Behere, D.V.1    Shedbalkar, V.P.2
  • 30
    • 0001851317 scopus 로고    scopus 로고
    • The role of the proximal ligand in heme enzymes
    • Poulos, T.L. (1996) The role of the proximal ligand in heme enzymes. J. Biol. Inorg. Chem. 1, 356-359.
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 356-359
    • Poulos, T.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.