메뉴 건너뛰기




Volumn 366, Issue 3, 2002, Pages 883-888

A novel, kinetically stable, catalytically active, all-ferric, nitrite-bound complex of Paracoccus pantotrophus cytochrome cd1

Author keywords

d1 haem; Enzyme activation; Ligand switching; Nitrite reductase

Indexed keywords

CONFORMATIONS; ENZYMES; NEGATIVE IONS; OXIDATION; REDUCTION; STOICHIOMETRY;

EID: 0037106352     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020795     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft, W. G. (1997) Cell biology and molecular basis of denitrification. Microbiol. Mol. Biol. Rev. 61, 533-616
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 2
    • 0028811652 scopus 로고
    • Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions
    • Berks, B. C., Ferguson, S. J., Moir J. W. B. and Richardson, D. J. (1995) Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions. Biochim. Biophys. Acta 1232, 97-173
    • (1995) Biochim. Biophys. Acta , vol.1232 , pp. 97-173
    • Berks, B.C.1    Ferguson, S.J.2    Moir, J.W.B.3    Richardson, D.J.4
  • 3
  • 11
    • 0038320771 scopus 로고    scopus 로고
    • 1 from Paracoccus pantotrophus exhibits kinetically gated, conformationally dependent, highly cooperative two-electron redox behavior
    • 1 from Paracoccus pantotrophus exhibits kinetically gated, conformationally dependent, highly cooperative two-electron redex behavior Biochemistry 39, 4234-4249
    • (2000) Biochemistry , vol.39 , pp. 4234-4249
    • Koppenhöfer, A.1    Turner, K.L.2    Allen, J.W.A.3    Chapman, S.K.4    Ferguson, S.J.5
  • 14
    • 0032574685 scopus 로고    scopus 로고
    • Electronic structural information from Q-band ENDOR on the type 1 and type 2 copper liganding environment in wild-type and mutant forms of copper-containing nitrite reductase
    • Veselov, A., Olesen, K., Sienkiewicz, A., Shapleigh, J. P. and Scholes, C. P. (1998) Electronic structural information from Q-band ENDOR on the type 1 and type 2 copper liganding environment in wild-type and mutant forms of copper-containing nitrite reductase. Biochemistry 37, 6095-6105
    • (1998) Biochemistry , vol.37 , pp. 6095-6105
    • Veselov, A.1    Olesen, K.2    Sienkiewicz, A.3    Shapleigh, J.P.4    Scholes, C.P.5
  • 15
    • 0027340210 scopus 로고
    • 1-type nitrite reductase from, and the absence of a copper-type nitrite reductase from, the aerobic denitrifier Thiosphaera pantotropha; the role of pseudoazurin as an electron donor
    • 1-type nitrite reductase from, and the absence of a copper-type nitrite reductase from, the aerobic denitrifier Thiosphaera pantotropha; the role of pseudoazurin as an electron donor. Eur. J. Biochem. 212, 377-385
    • (1993) Eur. J. Biochem. , vol.212 , pp. 377-385
    • Moir, J.W.B.1    Baratta, D.2    Richardson, D.J.3    Ferguson, S.J.4
  • 16
    • 0031051445 scopus 로고    scopus 로고
    • The pseudoazurin gene from Thiosphaera pantotropha: Analysis of upstream putative regulatory sequences and overexpression in Escherichia coli
    • Leung, Y. C., Chan, C., Reader, J. S., Willis, A. C., van Spanning, R. J. M., Ferguson, S. J. and Radford, S. E. (1997) The pseudoazurin gene from Thiosphaera pantotropha: analysis of upstream putative regulatory sequences and overexpression in Escherichia coli. Biochem. J. 321, 699-705
    • (1997) Biochem. J. , vol.321 , pp. 699-705
    • Leung, Y.C.1    Chan, C.2    Reader, J.S.3    Willis, A.C.4    Van Spanning, R.J.M.5    Ferguson, S.J.6    Radford, S.E.7
  • 19
    • 0035956858 scopus 로고    scopus 로고
    • The nitrite reductase from Pseudomonas aeruginosa: Essential role of two active-site histidines in the catalytic and structural properties
    • Cutruzzolà, F., Brown, K., Wilson, E. K., Bellelli, A., Arese, M., Tegoni, M., Cambillau, C. and Brunori, M. (2001) The nitrite reductase from Pseudomonas aeruginosa: essential role of two active-site histidines in the catalytic and structural properties. Proc. Natl. Acad. Sci. U.S.A. 98, 2232-2237
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2232-2237
    • Cutruzzolà, F.1    Brown, K.2    Wilson, E.K.3    Bellelli, A.4    Arese, M.5    Tegoni, M.6    Cambillau, C.7    Brunori, M.8
  • 20
    • 0001076517 scopus 로고    scopus 로고
    • Dissimilatory nitrite and nitric oxide reductases
    • Averill, B. A. (1996) Dissimilatory nitrite and nitric oxide reductases. Chem. Rev. 96, 2951-2964
    • (1996) Chem. Rev. , vol.96 , pp. 2951-2964
    • Averill, B.A.1
  • 21
    • 0025290038 scopus 로고
    • The reaction of Pseudomonas nitrite reductase and nitrite. A stopped-flow and EPR study
    • Silvestrini, M. C., Tordi, M. G., Musci, G. and Brunori, M. (1990) The reaction of Pseudomonas nitrite reductase and nitrite. A stopped-flow and EPR study. J. Biol. Chem. 265, 11783-11787
    • (1990) J. Biol. Chem. , vol.265 , pp. 11783-11787
    • Silvestrini, M.C.1    Tordi, M.G.2    Musci, G.3    Brunori, M.4
  • 22
    • 0015988812 scopus 로고
    • Cytochrome oxidase from Pseudomonas aeruginosa III. Reduction of hydroxylamine
    • Singh, J. (1973) Cytochrome oxidase from Pseudomonas aeruginosa III. Reduction of hydroxylamine. Biochim. Biophys. Acta 333, 28-36
    • (1973) Biochim. Biophys. Acta , vol.333 , pp. 28-36
    • Singh, J.1
  • 23
    • 2142669537 scopus 로고    scopus 로고
    • Redox reactions: Electrons as common intermediates
    • Taylor and Francis, London
    • Wrigglesworth, J. M. (1997) Redox reactions: electrons as common intermediates. In Energy and Life, Taylor and Francis, London
    • (1997) Energy and Life
    • Wrigglesworth, J.M.1
  • 25
    • 0016756863 scopus 로고
    • The nitric oxide compounds of Pseudomonas aeruginosa nitrite reductase and their probable participation in the nitrite reduction
    • Shimada, H. and Orii, Y. (1975) The nitric oxide compounds of Pseudomonas aeruginosa nitrite reductase and their probable participation in the nitrite reduction. FEBS Lett, 54, 237-240
    • (1975) FEBS Lett. , vol.54 , pp. 237-240
    • Shimada, H.1    Orii, Y.2
  • 26
    • 0018644989 scopus 로고
    • A re-evaluation of some basic structural and functional properties of Pseudomonas cytochrome oxidase
    • Silvestrini, M. C., Colosimo, A., Brunori, M., Walsh, T. A., Barber, D. and Greenwood, C. (1979) A re-evaluation of some basic structural and functional properties of Pseudomonas cytochrome oxidase. Biochem. J. 183, 701-709
    • (1979) Biochem. J. , vol.183 , pp. 701-709
    • Silvestrini, M.C.1    Colosimo, A.2    Brunori, M.3    Walsh, T.A.4    Barber, D.5    Greenwood, C.6
  • 28
    • 0020570426 scopus 로고
    • Electron paramagnetic resonance study of the interaction of some anionic ligands with oxidized Pseudomonas cytochrome oxidase
    • Muhoberac, B. B. and Wharton, D. C. (1983) Electron paramagnetic resonance study of the interaction of some anionic ligands with oxidized Pseudomonas cytochrome oxidase. J. Biol. Chem. 258, 3019-3027
    • (1983) J. Biol. Chem. , vol.258 , pp. 3019-3027
    • Muhoberac, B.B.1    Wharton, D.C.2
  • 29
    • 0032923887 scopus 로고    scopus 로고
    • Bacterial nitric oxide synthesis
    • Cutruzzolà, F. (1999) Bacterial nitric oxide synthesis. Biochim. Biophys. Acta 1411, 231-249
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 231-249
    • Cutruzzolà, F.1
  • 31
    • 0019433764 scopus 로고
    • The characterization and magnetic properties of the azide and imidazole derivatives of Pseudomonas nitrite reductase
    • Walsh, T. A., Johnson, M. K., Thomson, A. J., Barber, D. and Greenwood, C. (1981) The characterization and magnetic properties of the azide and imidazole derivatives of Pseudomonas nitrite reductase J. Inorg. Biochem. 14, 1-14
    • (1981) J. Inorg. Biochem. , vol.14 , pp. 1-14
    • Walsh, T.A.1    Johnson, M.K.2    Thomson, A.J.3    Barber, D.4    Greenwood, C.5
  • 32
    • 0024294308 scopus 로고
    • Magnetization of the sulfite and nitrite complexes of oxidized sulfite and nitrite reductases: EPR silent spin S = 1/2 states
    • Day, E. P., Peterson, J., Bonvoisin, J. J., Young, L. J., Wilkerson, J. O. and Siegel, L. M. (1988) Magnetization of the sulfite and nitrite complexes of oxidized sulfite and nitrite reductases: EPR silent spin S = 1/2 states. Biochemistry 27, 2126-2132
    • (1988) Biochemistry , vol.27 , pp. 2126-2132
    • Day, E.P.1    Peterson, J.2    Bonvoisin, J.J.3    Young, L.J.4    Wilkerson, J.O.5    Siegel, L.M.6
  • 33
    • 0030610044 scopus 로고    scopus 로고
    • 4-containing active centre of sulfite reductase in different states of oxidation: Heme activation via reduction-gated exogenous ligand exchange
    • 4-containing active centre of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange. Biochemistry 36, 12101-12119
    • (1997) Biochemistry , vol.36 , pp. 12101-12119
    • Crane, B.R.1    Siegel, L.M.2    Getzoff, E.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.