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Volumn 85, Issue 6, 2003, Pages 4047-4054

Single-Crystal EPR Study at 95 GHz of the Type 2 Copper Site of the Inhibitor-Bound Quercetin 2,3-Dioxygenase

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; DIETHYLDITHIOCARBAMIC ACID; FUNGAL ENZYME; HISTIDINE; NITROGEN; OXYGENASE; QUERCETIN 2,3 DIOXYGENASE; SULFUR; UNCLASSIFIED DRUG;

EID: 0344118900     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74818-8     Document Type: Article
Times cited : (10)

References (19)
  • 3
    • 0000288328 scopus 로고    scopus 로고
    • Theoretical study of the structural and spectroscopic properties of stellacyanin
    • De Kerpel, J. O. A., K. Pierloot, U. Ryde, and B. O. Roos. 1998. Theoretical study of the structural and spectroscopic properties of stellacyanin. J. Phys. Chem. B. 102:4638-4647.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 4638-4647
    • De Kerpel, J.O.A.1    Pierloot, K.2    Ryde, U.3    Roos, B.O.4
  • 6
    • 33845283303 scopus 로고
    • Spectroscopic and theoretical studies of the unusual EPR parameters of distorted tetrahedral cupric sites: Correlations to x-ray spectral features of core levels
    • Gewirth, A. A., S. L. Cohen, H. J. Schugar, and E. I. Solomon. 1987. Spectroscopic and theoretical studies of the unusual EPR parameters of distorted tetrahedral cupric sites: correlations to x-ray spectral features of core levels. Inorg. Chem. 26:1133-1146.
    • (1987) Inorg. Chem. , vol.26 , pp. 1133-1146
    • Gewirth, A.A.1    Cohen, S.L.2    Schugar, H.J.3    Solomon, E.I.4
  • 8
    • 0036311113 scopus 로고    scopus 로고
    • EPR characterization of the mononuclear Cu-containing Aspergillus japonicus quercetin 2,3-dioxygenase reveals dramatic changes upon anaerobic binding of substrates
    • Kooter, I. M., R. A. Steiner, B. W. Dijkstra, P. I. van Noort, M. R. Egmond, and M. Huber. 2002. EPR characterization of the mononuclear Cu-containing Aspergillus japonicus quercetin 2,3-dioxygenase reveals dramatic changes upon anaerobic binding of substrates. Eur. J. Biochem. 269:2971-2979.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 2971-2979
    • Kooter, I.M.1    Steiner, R.A.2    Dijkstra, B.W.3    Van Noort, P.I.4    Egmond, M.R.5    Huber, M.6
  • 9
    • 0029794252 scopus 로고    scopus 로고
    • Electronic structure of the perturbed blue copper site in nitrite reductase: Spectroscopic properties, bonding, and implications for the entatic/rack state
    • LaCroix, L. B., S. E. Shadle, Y. N. Wang, B. A. Averill, B. Hedman, K. O. Hodgson, and E. I. Solomon. 1996. Electronic structure of the perturbed blue copper site in nitrite reductase: spectroscopic properties, bonding, and implications for the entatic/rack state. J. Am. Chem. Soc. 118:7755-7768.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7755-7768
    • LaCroix, L.B.1    Shadle, S.E.2    Wang, Y.N.3    Averill, B.A.4    Hedman, B.5    Hodgson, K.O.6    Solomon, E.I.7
  • 10
    • 0016369980 scopus 로고
    • Structural implications derived from the analysis of the electron paramagnetic resonance spectra of natural and artificial copper proteins
    • Peisach, J., and W. E. Blumberg. 1974. Structural implications derived from the analysis of the electron paramagnetic resonance spectra of natural and artificial copper proteins. Arch. Biochem. Biophys. 165:691-708.
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 691-708
    • Peisach, J.1    Blumberg, W.E.2
  • 11
    • 33845377800 scopus 로고
    • Electronic structure and bonding of the blue copper site in plastocyanin
    • Penfield, K. W., A. A. Gewirth, and E. I. Solomon. 1985. Electronic structure and bonding of the blue copper site in plastocyanin. J. Am. Chem. Soc. 107:4519-4529.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 4519-4529
    • Penfield, K.W.1    Gewirth, A.A.2    Solomon, E.I.3
  • 12
    • 0032561819 scopus 로고    scopus 로고
    • Relation between the structure and spectroscopic properties of blue copper proteins
    • Pierloot, K., J. O. A. De Kerpel, U. Ryde, M. H. M. Olsson, and B. O. Roos. 1998. Relation between the structure and spectroscopic properties of blue copper proteins. J. Am. Chem. Soc. 120:13156-13166.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 13156-13166
    • Pierloot, K.1    De Kerpel, J.O.A.2    Ryde, U.3    Olsson, M.H.M.4    Roos, B.O.5
  • 13
    • 0008098143 scopus 로고
    • Electronic structures of active sites in copper proteins: Contributions to reactivity
    • Solomon, E. I., M. J. Baldwin, and M. D. Lowery. 1992. Electronic structures of active sites in copper proteins: contributions to reactivity. Chem. Rev. 92:521-542.
    • (1992) Chem. Rev. , vol.92 , pp. 521-542
    • Solomon, E.I.1    Baldwin, M.J.2    Lowery, M.D.3
  • 14
    • 0037168426 scopus 로고    scopus 로고
    • Anaerobic enzyme-substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase
    • Steiner, R. A., K. H. Kalk, and B. W. Dijkstra. 2002a. Anaerobic enzyme-substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase. Proc. Natl. Acad. Sci. USA. 99:16625-16630.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16625-16630
    • Steiner, R.A.1    Kalk, K.H.2    Dijkstra, B.W.3
  • 15
    • 0037172808 scopus 로고    scopus 로고
    • Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by x-ray crystallography: Inhibition, ordering effect, and mechanistic insights
    • Steiner, R. A., I. M. Kooter, and B. W. Dijkstra. 2002b. Functional analysis of the copper-dependent quercetin 2,3-dioxygenase. 1. Ligand-induced coordination changes probed by x-ray crystallography: inhibition, ordering effect, and mechanistic insights. Biochemistry. 41:7955-7962.
    • (2002) Biochemistry , vol.41 , pp. 7955-7962
    • Steiner, R.A.1    Kooter, I.M.2    Dijkstra, B.W.3
  • 16
    • 0035932675 scopus 로고    scopus 로고
    • A single-crystal electron paramagnetic resonance study at 95 GHz of the type I copper site of the green nitrite reductase of Alcaligenesfaecalis
    • van Gastel, M., M. J. Boulanger, G. W. Canters, M. Huber, M. E. P. Murphy, M. P. Verbeet, and E. J. J. Groenen. 2001. A single-crystal electron paramagnetic resonance study at 95 GHz of the type I copper site of the green nitrite reductase of Alcaligenesfaecalis. J. Phys. Chem. B. 105:2236-2243.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 2236-2243
    • Van Gastel, M.1    Boulanger, M.J.2    Canters, G.W.3    Huber, M.4    Murphy, M.E.P.5    Verbeet, M.P.6    Groenen, E.J.J.7
  • 17
    • 0034654186 scopus 로고    scopus 로고
    • Axial ligation in blue-copper proteins. A W-band electron spin echo detected electron paramagnetic resonance study of the azurin mutant M121H
    • van Gastel, M., G. W., Canters, H. Krupka, A. Messerschmidt, E. C. de Waal, G. C. M. Warmerdam, and E. J. J. Groenen. 2000. Axial ligation in blue-copper proteins. A W-band electron spin echo detected electron paramagnetic resonance study of the azurin mutant M121H. J. Am. Chem. Soc. 122:2322-2328.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2322-2328
    • Van Gastel, M.1    Canters, G.W.2    Krupka, H.3    Messerschmidt, A.4    De Waal, E.C.5    Warmerdam, G.C.M.6    Groenen, E.J.J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.