메뉴 건너뛰기




Volumn 46, Issue 7, 2007, Pages 1900-1912

Generation of novel copper sites by mutation of the axial ligand of amicyanin. Atomic resolution structures and spectroscopic properties

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; CRYSTAL STRUCTURE; OXIDATION; PROTEINS; SPECTROSCOPIC ANALYSIS; SULFUR; ZINC;

EID: 33847023097     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0619674     Document Type: Article
Times cited : (22)

References (37)
  • 1
    • 0026411154 scopus 로고
    • Copper protein structures
    • Adman, E. T. (1991) Copper protein structures, Adv. Protein Chem. 42, 145-197.
    • (1991) Adv. Protein Chem , vol.42 , pp. 145-197
    • Adman, E.T.1
  • 2
    • 0024293340 scopus 로고
    • Structure of azurin from Alcaligenes denitrificans refinement at 1. 8 Å resolution and comparison of the two crystallographically independent molecules
    • Baker, E. N. (1988) Structure of azurin from Alcaligenes denitrificans refinement at 1. 8 Å resolution and comparison of the two crystallographically independent molecules, J. Mol. Biol. 203, 1071-1095.
    • (1988) J. Mol. Biol , vol.203 , pp. 1071-1095
    • Baker, E.N.1
  • 4
    • 0037020063 scopus 로고    scopus 로고
    • Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-Å resolution containing a full complement of coppers
    • Piontek, K., Antorini, M., and Choinowski, T. (2002) Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-Å resolution containing a full complement of coppers, J. Biol. Chem. 277, 37663-37669.
    • (2002) J. Biol. Chem , vol.277 , pp. 37663-37669
    • Piontek, K.1    Antorini, M.2    Choinowski, T.3
  • 6
    • 0030514355 scopus 로고    scopus 로고
    • X-ray crystal structure of the cupredoxin amicyanin from Paracoccus denitrificans, refined at 1.31 Å resolution
    • Cunane, L. M., Chen, Z., Durley, R. C. E., and Mathews, F. S. (1996) X-ray crystal structure of the cupredoxin amicyanin from Paracoccus denitrificans, refined at 1.31 Å resolution, Acta Crystallogr., Sect. D 52, 676-686.
    • (1996) Acta Crystallogr., Sect. D , vol.52 , pp. 676-686
    • Cunane, L.M.1    Chen, Z.2    Durley, R.C.E.3    Mathews, F.S.4
  • 8
    • 0028815160 scopus 로고
    • Expression and characterization of Met92Gln mutant plastocyanin from Silene pratensis
    • Hibino, T., Lee, B. H., and Takabe, T. (1995) Expression and characterization of Met92Gln mutant plastocyanin from Silene pratensis, J. Biochem. 117, 101-106.
    • (1995) J. Biochem , vol.117 , pp. 101-106
    • Hibino, T.1    Lee, B.H.2    Takabe, T.3
  • 9
    • 0031664911 scopus 로고    scopus 로고
    • Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: Plant-specific mononuclear blue copper proteins
    • Nersissian, A. M., Immoos, C., Hill, M. G., Hart, P. J., Williams, G., Herrmann, R. G., and Valentine, J. S. (1998) Uclacyanins, stellacyanins, and plantacyanins are distinct subfamilies of phytocyanins: plant-specific mononuclear blue copper proteins, Protein Sci. 7, 1915-1929.
    • (1998) Protein Sci , vol.7 , pp. 1915-1929
    • Nersissian, A.M.1    Immoos, C.2    Hill, M.G.3    Hart, P.J.4    Williams, G.5    Herrmann, R.G.6    Valentine, J.S.7
  • 10
    • 0000567106 scopus 로고
    • Resonance Raman excitation profiles indicate multiple Cys-Cu charge transfer transitions in type 1 copper proteins
    • Han, J., Loehr, T. M., Lu, Y., Valentine, J. S., Averill, B. A., and Sanders-Loehr, J. (1993) Resonance Raman excitation profiles indicate multiple Cys-Cu charge transfer transitions in type 1 copper proteins, J. Am. Chem. Soc. 115, 4256-4263.
    • (1993) J. Am. Chem. Soc , vol.115 , pp. 4256-4263
    • Han, J.1    Loehr, T.M.2    Lu, Y.3    Valentine, J.S.4    Averill, B.A.5    Sanders-Loehr, J.6
  • 11
    • 0034797851 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase
    • Davidson, V. L. (2001) Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase, Adv. Protein Chem. 58, 95-140.
    • (2001) Adv. Protein Chem , vol.58 , pp. 95-140
    • Davidson, V.L.1
  • 12
    • 0022400803 scopus 로고
    • An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties, and physiological role
    • Husain, M., and Davidson, V. L. (1985) An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties, and physiological role, J. Biol. Chem. 260, 14626-14629.
    • (1985) J. Biol. Chem , vol.260 , pp. 14626-14629
    • Husain, M.1    Davidson, V.L.2
  • 13
    • 0022998580 scopus 로고
    • Characterization of two inducible periplasmic c-type cytochromes from Paracoccus denitrificans
    • Husain, M., and Davidson, V. L. (1986) Characterization of two inducible periplasmic c-type cytochromes from Paracoccus denitrificans, J. Biol. Chem. 261, 8577-8580.
    • (1986) J. Biol. Chem , vol.261 , pp. 8577-8580
    • Husain, M.1    Davidson, V.L.2
  • 15
    • 0028296944 scopus 로고
    • Structure of an electron transfer complex: Methylamine dehydrogenase, amicyanin, and cytochrome c551i
    • Chen, L., Durley, R. C., Mathews, F. S., and Davidson, V. L. (1994) Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i, Science 264, 86-90.
    • (1994) Science , vol.264 , pp. 86-90
    • Chen, L.1    Durley, R.C.2    Mathews, F.S.3    Davidson, V.L.4
  • 16
    • 0032497926 scopus 로고    scopus 로고
    • Molecular basis for interprotein complex-dependent effects on the redox properties of amicyanin
    • Zhu, Z., Cunane, L. M., Chen, Z., Durley, R. C., Mathews, F. S., and Davidson, V. L. (1998) Molecular basis for interprotein complex-dependent effects on the redox properties of amicyanin, Biochemistry 37, 17128-17136.
    • (1998) Biochemistry , vol.37 , pp. 17128-17136
    • Zhu, Z.1    Cunane, L.M.2    Chen, Z.3    Durley, R.C.4    Mathews, F.S.5    Davidson, V.L.6
  • 17
    • 18544370722 scopus 로고    scopus 로고
    • Site-directed mutagenesis of proline 94 to alanine in amicyanin converts a true electron transfer reaction into one that is kinetically coupled
    • Sun, D., Li, X., Mathews, F. S., and Davidson, V. L. (2005) Site-directed mutagenesis of proline 94 to alanine in amicyanin converts a true electron transfer reaction into one that is kinetically coupled, Biochemistry 44, 7200-7206.
    • (2005) Biochemistry , vol.44 , pp. 7200-7206
    • Sun, D.1    Li, X.2    Mathews, F.S.3    Davidson, V.L.4
  • 18
    • 33745847159 scopus 로고    scopus 로고
    • Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated
    • Ma, J. K., Carrell, C. J., Mathews, F. S., and Davidson, V. L. (2006) Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated, Biochemistry 45, 8284-8293.
    • (2006) Biochemistry , vol.45 , pp. 8284-8293
    • Ma, J.K.1    Carrell, C.J.2    Mathews, F.S.3    Davidson, V.L.4
  • 19
    • 3242666035 scopus 로고    scopus 로고
    • Structural studies of two mutants of amicyanin from Paracoccus denitrificans that stabilize the reduced state of the copper
    • Carrell, C. J., Sun, D., Jiang, S., Davidson, V. L., and Mathews, F. S. (2004) Structural studies of two mutants of amicyanin from Paracoccus denitrificans that stabilize the reduced state of the copper, Biochemistry 43, 9372-9380.
    • (2004) Biochemistry , vol.43 , pp. 9372-9380
    • Carrell, C.J.1    Sun, D.2    Jiang, S.3    Davidson, V.L.4    Mathews, F.S.5
  • 20
    • 0032546618 scopus 로고    scopus 로고
    • Site-directed mutagenesis of Phe 97 to Glu in amicyanin alters the electronic coupling for interprotein electron transfer from quinol methylamine dehydrogenase
    • Davidson, V. L., Jones, L. H., and Zhu, Z. (1998) Site-directed mutagenesis of Phe 97 to Glu in amicyanin alters the electronic coupling for interprotein electron transfer from quinol methylamine dehydrogenase, Biochemistry 37, 7371-7377.
    • (1998) Biochemistry , vol.37 , pp. 7371-7377
    • Davidson, V.L.1    Jones, L.H.2    Zhu, Z.3
  • 21
    • 0030669092 scopus 로고    scopus 로고
    • Factors which stabilize the methylamine dehydrogenase-amicyanin electron transfer protein complex revealed by site-directed mutagenesis
    • Davidson, V. L., Jones, L. H., Graichen, M. E., Mathews, F. S., and Hosler, J. P. (1997) Factors which stabilize the methylamine dehydrogenase-amicyanin electron transfer protein complex revealed by site-directed mutagenesis, Biochemistry 36, 12733-12738.
    • (1997) Biochemistry , vol.36 , pp. 12733-12738
    • Davidson, V.L.1    Jones, L.H.2    Graichen, M.E.3    Mathews, F.S.4    Hosler, J.P.5
  • 22
    • 0026720414 scopus 로고
    • The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans
    • Chistoserdov, A. Y., Boyd, J., Mathews, F. S., and Lidstrom, M. E. (1992) The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans, Biochem. Biophys. Res. Commun. 184, 1181-1189.
    • (1992) Biochem. Biophys. Res. Commun , vol.184 , pp. 1181-1189
    • Chistoserdov, A.Y.1    Boyd, J.2    Mathews, F.S.3    Lidstrom, M.E.4
  • 23
    • 0034622646 scopus 로고    scopus 로고
    • The Met99Gln mutant of amicyanin from Paracoccus versutus
    • Diederix, R. E., Canters, G. W., and Dennison, C. (2000) The Met99Gln mutant of amicyanin from Paracoccus versutus, Biochemistry 39, 9551-9560.
    • (2000) Biochemistry , vol.39 , pp. 9551-9560
    • Diederix, R.E.1    Canters, G.W.2    Dennison, C.3
  • 24
    • 0023042214 scopus 로고
    • Preliminary X-ray crystallographic study of amicyanin from Paracoccus denitrificans
    • Lim, L. W., Mathews, F. S., Husain, M., and Davidson, V. L. (1986) Preliminary X-ray crystallographic study of amicyanin from Paracoccus denitrificans, J. Mol. Biol. 189, 257-258.
    • (1986) J. Mol. Biol , vol.189 , pp. 257-258
    • Lim, L.W.1    Mathews, F.S.2    Husain, M.3    Davidson, V.L.4
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected by oscillation methods
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected by oscillation methods, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High resolution refinement
    • Sheldrick, G. M., and Schneider, T. R. (1997) SHELXL: High resolution refinement, Methods Enzymol. 277, 319-343.
    • (1997) Methods Enzymol , vol.277 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 27
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. (1999) XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density, J. Struct. Biol. 125, 156-165.
    • (1999) J. Struct. Biol , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 28
    • 27844525458 scopus 로고    scopus 로고
    • Role of the Type I copper center in determining the stability of amicyanin
    • Ma, J. K., Bishop, G. R., and Davidson, V. L. (2005) Role of the Type I copper center in determining the stability of amicyanin, Arch. Biochem. Biophys. 444, 27-33.
    • (2005) Arch. Biochem. Biophys , vol.444 , pp. 27-33
    • Ma, J.K.1    Bishop, G.R.2    Davidson, V.L.3
  • 29
    • 49049134325 scopus 로고
    • The loop-gap resonator: A new microwave lumped circuit ESR sample structure
    • Froncisz, W., and Hyde, J. S. (1982) The loop-gap resonator: A new microwave lumped circuit ESR sample structure, J. Magn. Reson. 47, 515.
    • (1982) J. Magn. Reson , vol.47 , pp. 515
    • Froncisz, W.1    Hyde, J.S.2
  • 30
    • 0011847913 scopus 로고
    • Electron paramagnetic resonance Q-band bridge with GaAS field-effect transistor signal amplifier and low-noise Gunn diode oscillator
    • Hyde, J. S., Newton, M. E., Strangeway, R. A., Camenisch, T. G., and Froncisz, W. (1991) Electron paramagnetic resonance Q-band bridge with GaAS field-effect transistor signal amplifier and low-noise Gunn diode oscillator, Rev. Sci. Instrum. 62, 2969-2975.
    • (1991) Rev. Sci. Instrum , vol.62 , pp. 2969-2975
    • Hyde, J.S.1    Newton, M.E.2    Strangeway, R.A.3    Camenisch, T.G.4    Froncisz, W.5
  • 31
    • 0023043203 scopus 로고
    • Properties of Paracoccus denitrificans amicyanin
    • Husain, M., Davidson, V. L., and Smith, A. J. (1986) Properties of Paracoccus denitrificans amicyanin, Biochemistry 25, 2431-2436.
    • (1986) Biochemistry , vol.25 , pp. 2431-2436
    • Husain, M.1    Davidson, V.L.2    Smith, A.J.3
  • 33
    • 0000797893 scopus 로고
    • Electron nuclear double resonance spectra of stellacyanin, a blue copper protein
    • Roberts, J. E., Brown, T. G., Hoffman, B. M., and Peisach, J. (1980) Electron nuclear double resonance spectra of stellacyanin, a blue copper protein, J. Am. Chem. Soc. 102, 825-829.
    • (1980) J. Am. Chem. Soc , vol.102 , pp. 825-829
    • Roberts, J.E.1    Brown, T.G.2    Hoffman, B.M.3    Peisach, J.4
  • 34
    • 0027503415 scopus 로고
    • X-ray analysis and spectroscopic characterization of M121Q azurin. A copper site model for stellacyanin
    • Romero, A., Hoitink, C. W., Nar, H., Huber, R., Messerschmidt, A., and Canters, G. W. (1993) X-ray analysis and spectroscopic characterization of M121Q azurin. A copper site model for stellacyanin, J. Mol. Biol. 229, 1007-1021.
    • (1993) J. Mol. Biol , vol.229 , pp. 1007-1021
    • Romero, A.1    Hoitink, C.W.2    Nar, H.3    Huber, R.4    Messerschmidt, A.5    Canters, G.W.6
  • 35
    • 0027998885 scopus 로고
    • Rack-induced bonding in blue-copper proteins
    • Malmstrom, B. G. (1994) Rack-induced bonding in blue-copper proteins, Eur. J. Biochem. 223, 711-718.
    • (1994) Eur. J. Biochem , vol.223 , pp. 711-718
    • Malmstrom, B.G.1
  • 36
    • 0011176009 scopus 로고
    • Coordination environment and fluoride binding of type 2 copper in the blue copper protein ascorbate oxidase
    • Dawson, J. H., Dooley, D. M., and Gray, H. B. (1980) Coordination environment and fluoride binding of type 2 copper in the blue copper protein ascorbate oxidase, Proc. Natl. Acad. Sci. U.S.A. 77, 5028-5031.
    • (1980) Proc. Natl. Acad. Sci. U.S.A , vol.77 , pp. 5028-5031
    • Dawson, J.H.1    Dooley, D.M.2    Gray, H.B.3
  • 37
    • 0026597444 scopus 로고
    • Free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992) Free R-value: a novel statistical quantity for assessing the accuracy of crystal structures, Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.