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Volumn 43, Issue 29, 2004, Pages 9372-9380

Structural studies of two mutants of amicyanin from Paracoccus denitrificans that stabilize the reduced state of the copper

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; ENZYMES; HYDROGEN BONDS; PH EFFECTS; REDOX REACTIONS;

EID: 3242666035     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049634z     Document Type: Article
Times cited : (35)

References (37)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 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
  • 4
    • 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. D52, 676-686.
    • (1996) Acta Crystallogr. , vol.D52 , pp. 676-686
    • Cunane, L.M.1    Chen, Z.2    Durley, R.C.E.3    Mathews, F.S.4
  • 6
    • 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
  • 7
    • 0036185564 scopus 로고    scopus 로고
    • An outer-sphere hydrogen-bond network constrains copper coordination in blue proteins
    • Machczynski, M. C., Gray, H. B., and Richards, J. H. (2002) An outer-sphere hydrogen-bond network constrains copper coordination in blue proteins, J. Inorg. Biochem. 88, 375-380.
    • (2002) J. Inorg. Biochem. , vol.88 , pp. 375-380
    • Machczynski, M.C.1    Gray, H.B.2    Richards, J.H.3
  • 8
    • 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
  • 9
    • 0023054012 scopus 로고
    • Crystal structure analyses of reduced (CuI) poplar plastocyanin at six pH values
    • Guss, J. M., Harrowell, P. R., Murata, M., Norris, V. A., and Freeman, H. C. (1986) Crystal structure analyses of reduced (CuI) poplar plastocyanin at six pH values, J. Mol. Biol. 192, 361-387.
    • (1986) J. Mol. Biol. , vol.192 , pp. 361-387
    • Guss, J.M.1    Harrowell, P.R.2    Murata, M.3    Norris, V.A.4    Freeman, H.C.5
  • 10
    • 0023003367 scopus 로고
    • Measurement of the oxidation-reduction potentials of amicyanin and c-type cytochromes from Paracoccus denitrificans
    • Gray, K. A., Knaff, D. B., Husain, M., and Davidson, V. L. (1986) Measurement of the oxidation-reduction potentials of amicyanin and c-type cytochromes from Paracoccus denitrificans, FEBS Lett. 207, 239-242.
    • (1986) FEBS Lett. , vol.207 , pp. 239-242
    • Gray, K.A.1    Knaff, D.B.2    Husain, M.3    Davidson, V.L.4
  • 11
    • 0025026513 scopus 로고
    • Methylamine dehydrogenases from methylotrophic bacteria
    • Davidson, V. L. (1990) Methylamine dehydrogenases from methylotrophic bacteria, Methods Enzymol. 188, 241-246.
    • (1990) Methods Enzymol. , vol.188 , pp. 241-246
    • Davidson, V.L.1
  • 12
    • 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
  • 13
    • 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
  • 14
    • 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
  • 15
    • 0037208360 scopus 로고    scopus 로고
    • An overview of the CCP4 project in protein crystallography: An example of a collaborative project
    • Winn, M. D. (2003) An overview of the CCP4 project in protein crystallography: An example of a collaborative project, J. Synchrotron Radiat. 10, 23-25.
    • (2003) J. Synchrotron Radiat. , vol.10 , pp. 23-25
    • Winn, M.D.1
  • 17
    • 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
  • 18
    • 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
  • 19
    • 0037452548 scopus 로고    scopus 로고
    • Effects of engineering uphill electron transfer into the methylamine dehydrogenase-amicyanin-cytochrome c-551i complex
    • Sun, D., and Davidson, V. L. (2003) Effects of engineering uphill electron transfer into the methylamine dehydrogenase-amicyanin-cytochrome c-551i complex, Biochemistry 42, 1772-1776.
    • (2003) Biochemistry , vol.42 , pp. 1772-1776
    • Sun, D.1    Davidson, V.L.2
  • 20
    • 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
  • 21
    • 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
  • 22
    • 0023667457 scopus 로고
    • The crystal structure of pseudoazurin from Acaligenes faecalis S-6 determined at 2.9 Å resolution
    • Petratos, K., Banner, D. W., Beppu, T., Wilson, K. S., and Tsemoglou, D. (1987) The crystal structure of pseudoazurin from Acaligenes faecalis S-6 determined at 2.9 Å resolution, FEBS Lett. 218, 209-214.
    • (1987) FEBS Lett. , vol.218 , pp. 209-214
    • Petratos, K.1    Banner, D.W.2    Beppu, T.3    Wilson, K.S.4    Tsemoglou, D.5
  • 23
    • 0026525991 scopus 로고
    • Site-directed mutagenesis of pseudoazurin from Alcaligenes faecalis S-6; Pro80Ala mutant exhibits marked increase in reduction potential
    • Nishiyama, M., Suzuki, J., Ohnuki, T., Chang, H. C., Horinouchi, S., Turley, S., Adman, E. T., and Beppu, T. (1992) Site-directed mutagenesis of pseudoazurin from Alcaligenes faecalis S-6; Pro80Ala mutant exhibits marked increase in reduction potential, Protein Eng. 5, 177-184.
    • (1992) Protein Eng. , vol.5 , pp. 177-184
    • Nishiyama, M.1    Suzuki, J.2    Ohnuki, T.3    Chang, H.C.4    Horinouchi, S.5    Turley, S.6    Adman, E.T.7    Beppu, T.8
  • 24
    • 0027536105 scopus 로고
    • Reduction potentials and their ph dependence in site-directed-mutant forms of azurin from Pseudomonas aeruginosa
    • Pascher, T., Karlsson, B. G., Nordling, M., Malmstrom, B. G., and Vanngard, T. (1993) Reduction potentials and their ph dependence in site-directed-mutant forms of azurin from Pseudomonas aeruginosa, Eur. J. Biochem. 212, 289-296.
    • (1993) Eur. J. Biochem. , vol.212 , pp. 289-296
    • Pascher, T.1    Karlsson, B.G.2    Nordling, M.3    Malmstrom, B.G.4    Vanngard, T.5
  • 25
    • 0025953438 scopus 로고
    • Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at ph 5.5 and ph 9.0. A ph-induced conformational transition involves a peptide bond flip
    • Nar, H., Messerschmidt, A., Huber, R., van de Kamp, M., and Canters, G. W. (1991) Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at ph 5.5 and ph 9.0. A ph-induced conformational transition involves a peptide bond flip, J. Mol. Biol. 221, 765-772.
    • (1991) J. Mol. Biol. , vol.221 , pp. 765-772
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3    Van De Kamp, M.4    Canters, G.W.5
  • 26
    • 0030780641 scopus 로고    scopus 로고
    • Site-directed mutants of pseudoazurin: Explanation of increased redox potentials from X-ray structures and from calculation of redox potential differences
    • Libeu, C. A., Kukimoto, M., Nishiyama, M., Horinouchi, S., and Adman, E. T. (1997) Site-directed mutants of pseudoazurin: Explanation of increased redox potentials from X-ray structures and from calculation of redox potential differences, Biochemistry 36, 13160-13179.
    • (1997) Biochemistry , vol.36 , pp. 13160-13179
    • Libeu, C.A.1    Kukimoto, M.2    Nishiyama, M.3    Horinouchi, S.4    Adman, E.T.5
  • 27
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus, R. A., and Sutin, N. (1985) Electron transfers in chemistry and biology, Biochim. Biophys. Acta 811, 265-322.
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 28
    • 0030037410 scopus 로고    scopus 로고
    • Electron transfer from copper to heme within the methylamine dehydrogenase-amicyanin-cytochrome c-551i complex
    • Davidson, V. L., and Jones, L. H. (1996) Electron transfer from copper to heme within the methylamine dehydrogenase-amicyanin-cytochrome c-551i complex, Biochemistry 35, 8120-8125.
    • (1996) Biochemistry , vol.35 , pp. 8120-8125
    • Davidson, V.L.1    Jones, L.H.2
  • 29
    • 0028360177 scopus 로고
    • Kinetic and thermodynamic analysis of a physiologic intermolecular electron transfer reaction between methylamine dehydrogenase and amicyanin
    • Brooks, H. B., and Davidson, V. L. (1994) Kinetic and thermodynamic analysis of a physiologic intermolecular electron transfer reaction between methylamine dehydrogenase and amicyanin, Biochemistry 33, 5696-5701.
    • (1994) Biochemistry , vol.33 , pp. 5696-5701
    • Brooks, H.B.1    Davidson, V.L.2
  • 30
    • 0000947245 scopus 로고
    • Free energy dependence of the electron transfer reaction between methylamine dehydrogenase and amicyanin
    • Brooks, H. B., and Davidson, V. L. (1994) Free energy dependence of the electron transfer reaction between methylamine dehydrogenase and amicyanin, J. Am. Chem. Soc. 116, 11202-11202.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11202-11202
    • Brooks, H.B.1    Davidson, V.L.2
  • 31
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brunger, 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
    • Brunger, A.T.1
  • 32
    • 0001099937 scopus 로고
    • Traitment statistique des erreurs dans la determination des structures cristallines
    • Luzzati, V. (1952) Traitment statistique des erreurs dans la determination des structures cristallines, Acta Crystallogr. 5, 802-810.
    • (1952) Acta Crystallogr. , vol.5 , pp. 802-810
    • Luzzati, V.1
  • 33
    • 0033106268 scopus 로고    scopus 로고
    • Remarks about protein structure precision
    • Cruickshank, D. W. I. (1999) Remarks about protein structure precision, Acta Crystallogr. D 55, 583-601.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 583-601
    • Cruickshank, D.W.I.1
  • 34
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) Molscript: A program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 35
    • 0030815133 scopus 로고    scopus 로고
    • Raster 3D: Photorealistic molecular graphics
    • Merritt, E. A., and Bacon, D. J. (1997) Raster 3D: Photorealistic molecular graphics, Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


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