메뉴 건너뛰기




Volumn 585, Issue 6, 2011, Pages 861-864

Avoiding premature oxidation during the binding of Cu(II) to a dithiolate site in BsSCO. A rapid freeze-quench EPR study

Author keywords

Copper binding; Rapid freeze quench EPR; SCO protein; SCO1 homolog from Bacillus subtilis

Indexed keywords

BACILLUS SUBTILIS SCO1 PROTEIN; BACTERIAL PROTEIN; CUPRIC ION; CYSTEINE; CYTOCHROME C OXIDASE; UNCLASSIFIED DRUG;

EID: 79952575573     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.02.014     Document Type: Article
Times cited : (12)

References (24)
  • 1
    • 9444296498 scopus 로고    scopus 로고
    • SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae
    • Glerum, D.M., Shtanko, A. and Tzagoloff, A. (1996) SCO1 and SCO2 act as high copy suppressors of a mitochondrial copper recruitment defect in Saccharomyces cerevisiae. J. Biol. Chem. 271, 20531-20535.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20531-20535
    • Glerum, D.M.1    Shtanko, A.2    Tzagoloff, A.3
  • 2
    • 0034666433 scopus 로고    scopus 로고
    • Characterization of YpmQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis
    • Mattatall, N.R., Jazairi, J. and Hill, B.C. (2000) Characterization of YpmQ, an accessory protein required for the expression of cytochrome c oxidase in Bacillus subtilis. J. Biol. Chem. 275, 28802-28809.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28802-28809
    • Mattatall, N.R.1    Jazairi, J.2    Hill, B.C.3
  • 4
    • 14344266861 scopus 로고    scopus 로고
    • Identification of a disulfide switch in BsSco, a member of the Sco family of cytochrome c oxidase assembly proteins
    • DOI 10.1021/bi0480537
    • Ye, Q., Imriskova-Sosova, I., Hill, B.C. and Jia, Z. (2005) Identification of a disulfide switch in BsSco, a member of the Sco family of cytochrome c oxidase assembly proteins. Biochemistry 44, 2934-2942. (Pubitemid 40293668)
    • (2005) Biochemistry , vol.44 , Issue.8 , pp. 2934-2942
    • Ye, Q.1    Imriskova-Sosova, I.2    Hill, B.C.3    Jia, Z.4
  • 6
    • 58149196161 scopus 로고    scopus 로고
    • Stability of oxidized, reduced and copper bound forms of Bacillus subtilis Sco
    • Davidson, D.E. and Hill, B.C. (2009) Stability of oxidized, reduced and copper bound forms of Bacillus subtilis Sco. Biochim. Biophys. Acta. 1794, 275-281.
    • (2009) Biochim. Biophys. Acta. , vol.1794 , pp. 275-281
    • Davidson, D.E.1    Hill, B.C.2
  • 8
    • 0032882504 scopus 로고    scopus 로고
    • Mechanism of copper-catalyzed autoxidation of cysteine
    • DOI 10.1080/10715769900300571
    • Kachur, A.V., Koch, C.J. and Biaglow, J.E. (1999) Mechanism of copper-catalyzed autoxidation of cysteine. Free Radical Res. 31, 23-34. (Pubitemid 29425339)
    • (1999) Free Radical Research , vol.31 , Issue.1 , pp. 23-34
    • Kachur, A.V.1    Koch, C.J.2    Biaglow, J.E.3
  • 9
    • 77249087706 scopus 로고    scopus 로고
    • Reduction mechanism of a coordinated superoxide by thiols in acidic media
    • Mishra, R., Mukhopadhyay, S. and Banerjee, R. (2010) Reduction mechanism of a coordinated superoxide by thiols in acidic media. Dalton Trans. 39, 2692-2696.
    • (2010) Dalton Trans. , vol.39 , pp. 2692-2696
    • Mishra, R.1    Mukhopadhyay, S.2    Banerjee, R.3
  • 10
    • 0030978638 scopus 로고    scopus 로고
    • Mechanism of production of hydroxyl radicals in the copper-catalyzed oxidation of dithiothreitol
    • Kachur, A.V., Held, K.D., Koch, C.J. and Biaglow, J.E. (1997) Mechanism of production of hydroxyl radicals in the copper-catalyzed oxidation of dithiothreitol. Radiat. Res. 147, 409-415.
    • (1997) Radiat. Res. , vol.147 , pp. 409-415
    • Kachur, A.V.1    Held, K.D.2    Koch, C.J.3    Biaglow, J.E.4
  • 11
    • 22844442226 scopus 로고    scopus 로고
    • Copper-catalyzed protein oxidation and its modulation by carbon dioxide: Enhancement of protein radicals in cells
    • Ramirez, D.C., Mejiba, S.E. and Mason, R.P. (2005) Copper-catalyzed protein oxidation and its modulation by carbon dioxide: enhancement of protein radicals in cells. J. Biol. Chem. 280, 27402-27411.
    • (2005) J. Biol. Chem. , vol.280 , pp. 27402-27411
    • Ramirez, D.C.1    Mejiba, S.E.2    Mason, R.P.3
  • 12
    • 29344435547 scopus 로고    scopus 로고
    • Characterization of the redox and metal binding activity of BsSco, a protein implicated in the assembly of cytochrome c oxidase
    • DOI 10.1021/bi051343i
    • Imriskova-Sosova, I., Andrews, D., Yam, K., Davidson, D., Yachnin, B. and Hill, B.C. (2005) Characterization of the redox and metal binding activity of BsSco, a protein implicated in the assembly of cytochrome c oxidase. Biochemistry 44, 16949-16956. (Pubitemid 43007223)
    • (2005) Biochemistry , vol.44 , Issue.51 , pp. 16949-16956
    • Imriskova-Sosova, I.1    Andrews, D.2    Yam, K.3    Davidson, D.4    Yachnin, B.5    Hill, B.C.6
  • 13
    • 28444449850 scopus 로고    scopus 로고
    • Spectroscopic studies of metal binding and metal selectivity in Bacillus subtilis BSco, a homologue of the yeast mitochondrial protein Sco1p
    • Andruzzi, L., Nakano, M., Nilges, M.J. and Blackburn, N.J. (2005) Spectroscopic studies of metal binding and metal selectivity in Bacillus subtilis BSco, a homologue of the yeast mitochondrial protein Sco1p. J. Am. Chem. Soc. 127, 16548-16558.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 16548-16558
    • Andruzzi, L.1    Nakano, M.2    Nilges, M.J.3    Blackburn, N.J.4
  • 14
    • 66349133626 scopus 로고    scopus 로고
    • Probing the kinetics and thermodynamics of copper(II) binding to Bacillus subtilis Sco, a protein involved in the assembly of the Cu(A) center of cytochrome c oxidase
    • Cawthorn, T.R., Poulsen, B.E., Davidson, D.E., Andrews, D. and Hill, B.C. (2009) Probing the kinetics and thermodynamics of copper(II) binding to Bacillus subtilis Sco, a protein involved in the assembly of the Cu(A) center of cytochrome c oxidase. Biochemistry 48, 4448-4454.
    • (2009) Biochemistry , vol.48 , pp. 4448-4454
    • Cawthorn, T.R.1    Poulsen, B.E.2    Davidson, D.E.3    Andrews, D.4    Hill, B.C.5
  • 15
    • 12344323483 scopus 로고    scopus 로고
    • Direct evidence that the reaction intermediate of metallo-β- lactamase L1 is metal bound
    • DOI 10.1021/bi048385b
    • Garrity, J.D., Bennett, B. and Crowder, M.W. (2005) Direct evidence that the reaction intermediate of metallo-beta-lactamase L1 is metal bound. Biochemistry 44, 1078-1087. (Pubitemid 40129667)
    • (2005) Biochemistry , vol.44 , Issue.3 , pp. 1078-1087
    • Garrity, J.D.1    Bennett, B.2    Crowder, M.W.3
  • 17
    • 24944481144 scopus 로고
    • Influence of the host lattice upon the EPR coupling parameters of copper-8-hydroxyquinolinate
    • Rist, G.H., Ammeter, J. and Günthard, H.-H. (1968) Influence of the host lattice upon the EPR coupling parameters of copper-8-hydroxyquinolinate. J. Chem. Phys. 49, 2210-2217.
    • (1968) J. Chem. Phys. , vol.49 , pp. 2210-2217
    • Rist, G.H.1    Ammeter, J.2    Günthard, H.-H.3
  • 18
    • 33846941106 scopus 로고
    • L-band parallel mode EPR. Measurement of quadrupole coupling through direct observation of secondary transitions
    • Rothenberger, K.S., Nilges, M.J., Altman, T.E., Glab, K., Belford, R.L., Froncisz, W. and Hyde, J.S. (1986) L-band parallel mode EPR. Measurement of quadrupole coupling through direct observation of secondary transitions. Chem. Phys. Lett. 124, 295-298.
    • (1986) Chem. Phys. Lett. , vol.124 , pp. 295-298
    • Rothenberger, K.S.1    Nilges, M.J.2    Altman, T.E.3    Glab, K.4    Belford, R.L.5    Froncisz, W.6    Hyde, J.S.7
  • 19
    • 20544449810 scopus 로고
    • Evaluation of copper nuclear quadrupolar coupling in thio complexes by completion of the coordination sphere
    • Liczwek, D.L., Belford, R.L., Pilbrow, J.R. and Hyde, J.S. (1983) Evaluation of copper nuclear quadrupolar coupling in thio complexes by completion of the coordination sphere. J. Phys. Chem. 87, 2509-2512.
    • (1983) J. Phys. Chem. , vol.87 , pp. 2509-2512
    • Liczwek, D.L.1    Belford, R.L.2    Pilbrow, J.R.3    Hyde, J.S.4
  • 20
    • 0016369980 scopus 로고
    • Structural implications derived from the analysis of electron paramagnetic resonance spectra of natural and artificial copper proteins
    • Peisach, J. and Blumberg, W.E. (1974) Structural implications derived from the analysis of 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
  • 21
    • 67649389968 scopus 로고    scopus 로고
    • EPR of Cu2+ prion protein constructs at 2 GHz using the g(perpendicular) region to characterize nitrogen ligation
    • Hyde, J.S., Bennett, B., Walter, E.D., Millhauser, G.L., Sidabras, J.W. and Antholine, W.E. (2009) EPR of Cu2+ prion protein constructs at 2 GHz using the g(perpendicular) region to characterize nitrogen ligation. Biophys. J. 96, 3354-3362.
    • (2009) Biophys. J. , vol.96 , pp. 3354-3362
    • Hyde, J.S.1    Bennett, B.2    Walter, E.D.3    Millhauser, G.L.4    Sidabras, J.W.5    Antholine, W.E.6
  • 24
    • 73149111478 scopus 로고    scopus 로고
    • H135A controls the redox activity of the Sco copper center. Kinetic and spectroscopic studies of the His135Ala variant of Bacillus subtilis Sco
    • Siluvai, G.S., Nakano, M.M., Mayfield, M., Nilges, M.J. and Blackburn, N.J. (2009) H135A controls the redox activity of the Sco copper center. Kinetic and spectroscopic studies of the His135Ala variant of Bacillus subtilis Sco. Biochemistry 48, 12133-12144.
    • (2009) Biochemistry , vol.48 , pp. 12133-12144
    • Siluvai, G.S.1    Nakano, M.M.2    Mayfield, M.3    Nilges, M.J.4    Blackburn, N.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.