메뉴 건너뛰기




Volumn 45, Issue 9, 2006, Pages 2927-2939

Atomic resolution crystal structures, EXAFS, and quantum chemical studies of rusticyanin and its two mutants provide insight into its unusual properties

Author keywords

[No Author keywords available]

Indexed keywords

ALLOYS; CALCULATIONS; DATA PROCESSING; FUNCTIONAL ASSESSMENT; MUTAGENS; PROTEINS;

EID: 33644696451     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi052372w     Document Type: Article
Times cited : (39)

References (65)
  • 1
    • 0026058985 scopus 로고
    • Amino acid sequence of the blue copper protein rusticyanin from Thiobacillus ferrooxidans
    • Ronk, M., and Shively, J. E. (1991) Amino acid sequence of the blue copper protein rusticyanin from Thiobacillus ferrooxidans, Biochemistry 30, 9435-9442.
    • (1991) Biochemistry , vol.30 , pp. 9435-9442
    • Ronk, M.1    Shively, J.E.2
  • 3
    • 0023645803 scopus 로고
    • Respiratory enzymes in thiobacillus ferrooxidans-a kinetic study of electron transfer between iron and rusticyanin in sulfate media
    • Blake, R. C., and Shute, E. A. (1987) Respiratory enzymes in thiobacillus ferrooxidans-a kinetic study of electron transfer between iron and rusticyanin in sulfate media, J. Biol. Chem. 262, 14983-4989.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14983-14989
    • Blake, R.C.1    Shute, E.A.2
  • 4
    • 0018860792 scopus 로고
    • A potentiometric and kinetic study on the respiratory chain of ferrous iron grown Thiobacillus ferrooxidans
    • Ingledew, W. J., and Cobley, J. G. (1980) A potentiometric and kinetic study on the respiratory chain of ferrous iron grown Thiobacillus ferrooxidans, Biochim. Biophys. Acta 590, 141-148.
    • (1980) Biochim. Biophys. Acta , vol.590 , pp. 141-148
    • Ingledew, W.J.1    Cobley, J.G.2
  • 5
    • 0025934531 scopus 로고    scopus 로고
    • Mixed-ligand complexes of iron with cyanide and phenanthroline as new probes of metalloprotein electron-transfer reactivity-analysis of reactions involving rusticyanin from Thiobacillus ferrooxidans
    • Blake, R., White, K. J., and Shute, E. A. (1996) Mixed-ligand complexes of iron with cyanide and phenanthroline as new probes of metalloprotein electron-transfer reactivity-analysis of reactions involving rusticyanin from Thiobacillus ferrooxidans, J. Biol. Chem. 266, 19203-19211.
    • (1996) J. Biol. Chem. , vol.266 , pp. 19203-19211
    • Blake, R.1    White, K.J.2    Shute, E.A.3
  • 6
    • 0030589040 scopus 로고    scopus 로고
    • Multiple wavelength anomalous diffraction (MAD) crystal structure of rusticyanin: A highly oxidizing cupredoxin with extreme acid stability
    • Walter, R. L., Ealick, S. E., Friedman, A. M., Blake, R. C., Proctor, P., and Shoham, M. (1996) Multiple wavelength anomalous diffraction (MAD) crystal structure of rusticyanin: A highly oxidizing cupredoxin with extreme acid stability, J. Mol. Biol. 265, 730-751.
    • (1996) J. Mol. Biol. , vol.265 , pp. 730-751
    • Walter, R.L.1    Ealick, S.E.2    Friedman, A.M.3    Blake, R.C.4    Proctor, P.5    Shoham, M.6
  • 7
    • 0032128139 scopus 로고    scopus 로고
    • Structure determination of a 16.8 kDa copper protein at 2.1 angstrom resolution using anomalous scattering data with direct methods
    • Harvey, I., Hao, Q., Duke, E. M. H., Ingledew, W. J., and Hasnain, S. S. (1998) Structure determination of a 16.8 kDa copper protein at 2.1 angstrom resolution using anomalous scattering data with direct methods, Acta Crystallogr., Sect, D 54, 629-635.
    • (1998) Acta Crystallogr., Sect, D , vol.54 , pp. 629-635
    • Harvey, I.1    Hao, Q.2    Duke, E.M.H.3    Ingledew, W.J.4    Hasnain, S.S.5
  • 8
    • 0030589038 scopus 로고    scopus 로고
    • NMR solution structure of Cu(I) rusticyanin from Thiobacillus ferrooxidans: Structural basis for the extreme acid stability and redox potential
    • Botuyan, M. V., Toypalmer, A., Chung, J., Blake, R. C., Beroza, P., Case, D. A., and Dyson, H. J. (1996) NMR solution structure of Cu(I) rusticyanin from Thiobacillus ferrooxidans: Structural basis for the extreme acid stability and redox potential, J. Mol. Biol. 263, 752-767.
    • (1996) J. Mol. Biol. , vol.263 , pp. 752-767
    • Botuyan, M.V.1    Toypalmer, A.2    Chung, J.3    Blake, R.C.4    Beroza, P.5    Case, D.A.6    Dyson, H.J.7
  • 9
    • 0029006333 scopus 로고
    • X-ray absorption studies and homology modelling define the structural features that specify the nature of the copper site in rusticyanin
    • Grossmann, J. G., Ingledew, W. J., Harvey, I., Strange, R. W., and Hasnain, S. S. (1995) X-ray absorption studies and homology modelling define the structural features that specify the nature of the copper site in rusticyanin, Biochemistry 34, 8406-8414.
    • (1995) Biochemistry , vol.34 , pp. 8406-8414
    • Grossmann, J.G.1    Ingledew, W.J.2    Harvey, I.3    Strange, R.W.4    Hasnain, S.S.5
  • 10
    • 0032544217 scopus 로고    scopus 로고
    • Modulating the redox potential and acid stability of rusticyanin by site-directed mutagenesis of Ser86
    • Hall, J. F., Kanbi, L. D., Harvey, I., Murphy, L. M., and Hasnain, S. S. (1998) Modulating the redox potential and acid stability of rusticyanin by site-directed mutagenesis of Ser86, Biochemistry 37, 11451-11458.
    • (1998) Biochemistry , vol.37 , pp. 11451-11458
    • Hall, J.F.1    Kanbi, L.D.2    Harvey, I.3    Murphy, L.M.4    Hasnain, S.S.5
  • 11
    • 0036296326 scopus 로고    scopus 로고
    • Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: Insights into the structural relationship with the cupredoxins and the multi copper proteins
    • Kanbi, L. D., Antonyuk, S., Hough, M. A., Hall, J. F., Dodd, F. E., and Hasnain, S. S. (2002) Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: Insights into the structural relationship with the cupredoxins and the multi copper proteins, J. Mol. Biol. 320, 263-275.
    • (2002) J. Mol. Biol. , vol.320 , pp. 263-275
    • Kanbi, L.D.1    Antonyuk, S.2    Hough, M.A.3    Hall, J.F.4    Dodd, F.E.5    Hasnain, S.S.6
  • 12
    • 0032697794 scopus 로고    scopus 로고
    • Interaction-induced redox switch in the electron-transfer complex rusticyanin-cytochrome c(4)
    • Guidici-Orticoni, M. T., Guerlesquin, F., Bruschi, M., and Nitschke, W. (1999). Interaction-induced redox switch in the electron-transfer complex rusticyanin-cytochrome c(4), J. Biol. Chem. 274, 30365-30369.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30365-30369
    • Guidici-Orticoni, M.T.1    Guerlesquin, F.2    Bruschi, M.3    Nitschke, W.4
  • 13
    • 0025854571 scopus 로고
    • X-ray crystal structure of the 2 site specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa
    • Nar, H., Messerschmidt, A., Huber, R., van de Kamp, M., and Canters, G. W. (1991) X-ray crystal structure of the 2 site specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa, J. Mol. Biol. 218, 427-447.
    • (1991) J. Mol. Biol. , vol.218 , pp. 427-447
    • Nar, H.1    Messerschmidt, A.2    Huber, R.3    Van De Kamp, M.4    Canters, G.W.5
  • 14
    • 0029187321 scopus 로고
    • Structure of a new azurin from the denitrifying bacterium Alcaligenes xylosoxidans at high resolution
    • Dodd, F. E., Hasnain, S. S., Abraham, Z. H. L., Eady, R. R., and Smith, B. E. (1995) Structure of a new azurin from the denitrifying bacterium Alcaligenes xylosoxidans at high resolution, Acta Crystallogr., Sect. D 51, 1052-1064.
    • (1995) Acta Crystallogr., Sect. D , vol.51 , pp. 1052-1064
    • Dodd, F.E.1    Hasnain, S.S.2    Abraham, Z.H.L.3    Eady, R.R.4    Smith, B.E.5
  • 15
    • 0035098048 scopus 로고    scopus 로고
    • Structure of the M148Q mutant of rusticyanin at 1.5 angstrom: A model for the copper site of stellacyanin
    • Hough, M. A., Hall, J. F., Kanbi, L. D., and Hasnain, S. S. (2001) Structure of the M148Q mutant of rusticyanin at 1.5 angstrom: a model for the copper site of stellacyanin, Acta Crystallogr., Sect. D 57, 355-360.
    • (2001) Acta Crystallogr., Sect. D , vol.57 , pp. 355-360
    • Hough, M.A.1    Hall, J.F.2    Kanbi, L.D.3    Hasnain, S.S.4
  • 16
    • 0034645617 scopus 로고    scopus 로고
    • Role of the surface-exposed and copper-coordinating histidine in blue copper proteins: The electron-transfer and redox-coupled ligand binding properties of His117Gly azurin
    • Jeuken, L. J. C., van Vliet, P., Verbeet, M. P., Camba, R., McEvoy, J. P., Armstrong, F. K., and Canters, G. W. (2000) Role of the surface-exposed and copper-coordinating histidine in blue copper proteins: The electron-transfer and redox-coupled ligand binding properties of His117Gly azurin, J. Am. Chem. Soc. 122, 12186-12194.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12186-12194
    • Jeuken, L.J.C.1    Van Vliet, P.2    Verbeet, M.P.3    Camba, R.4    McEvoy, J.P.5    Armstrong, F.K.6    Canters, G.W.7
  • 17
    • 0037066129 scopus 로고    scopus 로고
    • Alcaligenes xylosoxidans dissimilatory nitrite reductase: Alanine substitution of the surface-exposed histidine 139 ligand of the type 1 copper center prevents electron transfer to the catalytic center
    • Prudencio, M., Sawers, G., Fairhurst, S. A., Yousafzai, F. K., and Eady, R. R. (2002) Alcaligenes xylosoxidans dissimilatory nitrite reductase: Alanine substitution of the surface-exposed histidine 139 ligand of the type 1 copper center prevents electron transfer to the catalytic center, Biochemistry 41, 3430-3438.
    • (2002) Biochemistry , vol.41 , pp. 3430-3438
    • Prudencio, M.1    Sawers, G.2    Fairhurst, S.A.3    Yousafzai, F.K.4    Eady, R.R.5
  • 18
    • 3042694367 scopus 로고    scopus 로고
    • Determinants of the relative reduction potentials of type-1 copper sites in proteins
    • Li, H., Webb, S. P., Ivanic, J., and Jensen, J. H. (2004) Determinants of the relative reduction potentials of type-1 copper sites in proteins, J. Am. Chem. Soc. 126, 8010-8019.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8010-8019
    • Li, H.1    Webb, S.P.2    Ivanic, J.3    Jensen, J.H.4
  • 19
    • 3042588009 scopus 로고    scopus 로고
    • Theoretical determination of the standard reduction potential of plastocyanin in vitro
    • Datta, S. N., Sudhamsu, J., and Pandey, A. (2004) Theoretical determination of the standard reduction potential of plastocyanin in vitro, J. Phys. Chem. 108, 8007-8016.
    • (2004) J. Phys. Chem. , vol.108 , pp. 8007-8016
    • Datta, S.N.1    Sudhamsu, J.2    Pandey, A.3
  • 20
    • 2542539752 scopus 로고    scopus 로고
    • Computational approaches to structural and functional analysis of plastocyanin and other blue copper proteins
    • De Rienzo, F., Gabdoulline, R. R., Wade, R. C., Sola, M., and Menziani, M. C. (2004) Computational approaches to structural and functional analysis of plastocyanin and other blue copper proteins, Cell. Mol. Life Sci. 61, 1123-1142.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1123-1142
    • De Rienzo, F.1    Gabdoulline, R.R.2    Wade, R.C.3    Sola, M.4    Menziani, M.C.5
  • 23
    • 0034090156 scopus 로고    scopus 로고
    • Structures of oxidized and reduced azurin II from Alcaligenes xylosoxidans at 1.75 angstrom resolution
    • Dodd, F. E., Abraham, Z. H. L., Eady, R. R., and Hasnain, S. S. (2000) Structures of oxidized and reduced azurin II from Alcaligenes xylosoxidans at 1.75 angstrom resolution, Acta Crystallogr., Sect. D 56, 690-696.
    • (2000) Acta Crystallogr., Sect. D , vol.56 , pp. 690-696
    • Dodd, F.E.1    Abraham, Z.H.L.2    Eady, R.R.3    Hasnain, S.S.4
  • 24
    • 19944397871 scopus 로고    scopus 로고
    • Axial methionine has much less influence on reduction potentials in a Cu-A center than in a blue copper center
    • Hwang, H. J., Berry, S. M., Nilges, M. J., and Lu, Y. (2005) Axial methionine has much less influence on reduction potentials in a Cu-A center than in a blue copper center, J. Am. Chem. Soc. 127, 7274-7275.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 7274-7275
    • Hwang, H.J.1    Berry, S.M.2    Nilges, M.J.3    Lu, Y.4
  • 25
    • 1542378734 scopus 로고    scopus 로고
    • Electronic structures of metal sites in proteins and models: Contributions to function in blue copper proteins
    • Solomon, E. I., Szilagyi, R. K., DeBeer, S. G., and Basumallick, L. (2004) Electronic structures of metal sites in proteins and models: Contributions to function in blue copper proteins, Chem. Rev. 104, 419-458.
    • (2004) Chem. Rev. , vol.104 , pp. 419-458
    • Solomon, E.I.1    Szilagyi, R.K.2    DeBeer, S.G.3    Basumallick, L.4
  • 27
    • 0029274711 scopus 로고
    • Electronic structure of the reduced blue copper active site-contributions to reduction potentials and geometry
    • Guckert, J. A., Lowery, M. D., and Solomon, E. I. (1995) Electronic structure of the reduced blue copper active site-contributions to reduction potentials and geometry, J. Am. Chem. Soc. 117, 2817-2844.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2817-2844
    • Guckert, J.A.1    Lowery, M.D.2    Solomon, E.I.3
  • 28
    • 0033613245 scopus 로고    scopus 로고
    • Role of the axial ligand in type 1 Cu centers studied by point mutations of Met148 in rusticyanin
    • Hall, J. F., Kanbi, L. D., Strange, R. W., and Hasnain, S. S. (1999) Role of the axial ligand in type 1 Cu centers studied by point mutations of Met148 in rusticyanin, Biochemistry 38, 12675-12680.
    • (1999) Biochemistry , vol.38 , pp. 12675-12680
    • Hall, J.F.1    Kanbi, L.D.2    Strange, R.W.3    Hasnain, S.S.4
  • 29
    • 0035936568 scopus 로고    scopus 로고
    • NMR studies on copper(II) rusticyanin: Is the Cu-SCys interaction responsible for the high redox potentials in blue copper proteins?
    • Donaire, A., Jimenez, B., Moratal, J. M., Hall, J. F., and Hasnain, S. S. (2001) NMR studies on copper(II) rusticyanin: Is the Cu-SCys interaction responsible for the high redox potentials in blue copper proteins?, Biochemistry 40, 837-846.
    • (2001) Biochemistry , vol.40 , pp. 837-846
    • Donaire, A.1    Jimenez, B.2    Moratal, J.M.3    Hall, J.F.4    Hasnain, S.S.5
  • 31
    • 0042816458 scopus 로고    scopus 로고
    • Probing the role of axial methionine in the blue copper center of azurin with unnatural amino acids
    • Berry, S. M., Ralle, M., Low, D. W., Blackburn, N. J., and Lu, Y. (2003) Probing the role of axial methionine in the blue copper center of azurin with unnatural amino acids, J. Am. Chem. Soc. 125, 8760-8768.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8760-8768
    • Berry, S.M.1    Ralle, M.2    Low, D.W.3    Blackburn, N.J.4    Lu, Y.5
  • 33
    • 0037473550 scopus 로고    scopus 로고
    • Frozen density functional free energy simulations of redox proteins: Computational studies of the reduction potential of plastocyanin and rusticyanin
    • Olsson, M. H. M., Hong, G. Y., and Warshel, A. (2003) Frozen density functional free energy simulations of redox proteins: Computational studies of the reduction potential of plastocyanin and rusticyanin, J. Am. Chem. Soc. 125, 5025-5039.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5025-5039
    • Olsson, M.H.M.1    Hong, G.Y.2    Warshel, A.3
  • 34
    • 0031576658 scopus 로고    scopus 로고
    • Catalytic mechanism of the enzyme papain: Predictions with a hybrid quantum mechanical molecular mechanical potential
    • Harrison, M. J., Burton, N. A., and Hillier, I. H. (1997) Catalytic mechanism of the enzyme papain: Predictions with a hybrid quantum mechanical molecular mechanical potential, J. Am. Chem. Soc. 119, 12285-12291.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 12285-12291
    • Harrison, M.J.1    Burton, N.A.2    Hillier, I.H.3
  • 35
    • 0001531848 scopus 로고    scopus 로고
    • Protein control of redox potentials of iron-sulfur proteins
    • Stephens, P. J., Jollie, D. R., and Warshel, A. (1996) Protein control of redox potentials of iron-sulfur proteins, Chem. Rev. 96, 2491-2513.
    • (1996) Chem. Rev. , vol.96 , pp. 2491-2513
    • Stephens, P.J.1    Jollie, D.R.2    Warshel, A.3
  • 36
    • 84986513644 scopus 로고
    • A combined quantum chemical and molecular mechanical potential for molecular dynamics simulations
    • Field, M. J., Bash, P. A., and Karplus, M. (1990) A combined quantum chemical and molecular mechanical potential for molecular dynamics simulations, J. Comput. Chem. 11, 700-733.
    • (1990) J. Comput. Chem. , vol.11 , pp. 700-733
    • Field, M.J.1    Bash, P.A.2    Karplus, M.3
  • 37
    • 0040828601 scopus 로고
    • Electron transfer reaction of rusticyanin, a blue copper protein from Thiobacillus ferrooxidans, at modified gold electrodes
    • Haladjian, J., Bruschi, M., Nunzi, F., and Bianco, P. (1993) Electron transfer reaction of rusticyanin, a blue copper protein from Thiobacillus ferrooxidans, at modified gold electrodes, J. Electroanal. Chem. 352, 329-335.
    • (1993) J. Electroanal. Chem. , vol.352 , pp. 329-335
    • Haladjian, J.1    Bruschi, M.2    Nunzi, F.3    Bianco, P.4
  • 38
    • 0027450475 scopus 로고
    • The structural characterization of azurin from Pseudomonas aeruginosa and some of its methionine-121 mutants
    • Murphy, L. M., Strange, R. W., Karlsson, B. G., Lundberg, L. G., Pascher, T., Reinhammar, B., and Hasnain, S. S. (1993) The structural characterization of azurin from Pseudomonas aeruginosa and some of its methionine-121 mutants, Biochemistry 32, 1965-1975.
    • (1993) Biochemistry , vol.32 , pp. 1965-1975
    • Murphy, L.M.1    Strange, R.W.2    Karlsson, B.G.3    Lundberg, L.G.4    Pascher, T.5    Reinhammar, B.6    Hasnain, S.S.7
  • 39
    • 0026745126 scopus 로고
    • Crystallisation and preliminary X-ray crystallographic studies of rusticyanin from Thiobacillus ferrooxidans
    • Djebli, A., Proctor, P., Blake, R. C., and Shoham, M. (1992) Crystallisation and preliminary X-ray crystallographic studies of rusticyanin from Thiobacillus ferrooxidans, J. Mol. Biol. 227, 581-582.
    • (1992) J. Mol. Biol. , vol.227 , pp. 581-582
    • Djebli, A.1    Proctor, P.2    Blake, R.C.3    Shoham, M.4
  • 40
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • (Carter, C. W., and Sweet, R. M., Eds.), Academic Press, New York
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, in Methods in Enzymology: Macromolecular Crystallography (Carter, C. W., and Sweet, R. M., Eds.) Part A, pp 307-326, Academic Press, New York.
    • (1997) Methods in Enzymology: Macromolecular Crystallography , Issue.PART A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 84920325457 scopus 로고
    • Amore-an automated package for molecular replacement
    • Navaza, J. (1994) Amore-an automated package for molecular replacement, Acta Crystallogr., Sect. A 50, 157-163.
    • (1994) Acta Crystallogr., Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 44
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. A., and Huber, R. (1991) Accurate bond and angle parameters for X-ray protein structure refinement, Acta Crystallogr., Sect. A 47, 392-400.
    • (1991) Acta Crystallogr., Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 45
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • Sheldrick, G. M., and Schneider, T. R. (1997) SHELXL: High-resolution refinement, in Methods Enzymol. 277, 319-343.
    • (1997) Methods Enzymol , vol.277 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 46
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr., Sect. A 47, 110-119.
    • (1991) Acta Crystallogr., Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 47
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993). Procheck: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 25, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.25 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 48
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr. 53, 240-255.
    • (1997) Acta Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 50
    • 0030497978 scopus 로고    scopus 로고
    • Efficient rebuilding of protein structures
    • Kleywegt, G. J., and Jones, T. A. (1996) Efficient rebuilding of protein structures, Acta Crystallogr., Sect. D 52, 829-832.
    • (1996) Acta Crystallogr., Sect. D , vol.52 , pp. 829-832
    • Kleywegt, G.J.1    Jones, T.A.2
  • 52
    • 84986527758 scopus 로고
    • IMOMM-A new integrated ab initio plus molecular mechanics geometry optimisation scheme of equilibrium structures and transition states
    • Maseras, F., and Morokuma, K. (1995) IMOMM-A new integrated ab initio plus molecular mechanics geometry optimisation scheme of equilibrium structures and transition states, J. Comput. Chem. 16, 1170-1179.
    • (1995) J. Comput. Chem. , vol.16 , pp. 1170-1179
    • Maseras, F.1    Morokuma, K.2
  • 53
    • 0037473497 scopus 로고    scopus 로고
    • Geometry optimization with QM/MM, ONIOM, and other combined methods. I. Microiterations and constraints
    • Vreven, T., Morokuma, K., Farkas, O., Schlegel, H. B., and Frisch, M. J. (2003) Geometry optimization with QM/MM, ONIOM, and other combined methods. I. Microiterations and constraints, J. Comput. Chem. 24, 760-769.
    • (2003) J. Comput. Chem. , vol.24 , pp. 760-769
    • Vreven, T.1    Morokuma, K.2    Farkas, O.3    Schlegel, H.B.4    Frisch, M.J.5
  • 56
    • 33645941402 scopus 로고
    • The OPLS potential functions for proteins-energy minimisations for cyclic peptides and crambin
    • Jorgensen, W. L., and Tiradorives, J. (1988) The OPLS potential functions for proteins-energy minimisations for cyclic peptides and crambin, J. Am. Chem. Soc. 110, 1657-1666.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1657-1666
    • Jorgensen, W.L.1    Tiradorives, J.2
  • 57
    • 0036558223 scopus 로고    scopus 로고
    • A new molecular mechanics force field for the oxidized form of blue copper proteins
    • Comba, P., and Remenyi, R. (2002) A new molecular mechanics force field for the oxidized form of blue copper proteins, J. Comput. Chem. 23, 697-705.
    • (2002) J. Comput. Chem. , vol.23 , pp. 697-705
    • Comba, P.1    Remenyi, R.2
  • 58
    • 0033152783 scopus 로고    scopus 로고
    • Expanding the model: Anisotropic displacement parameters in protein structure refinement
    • Merritt, E. A. (1999) Expanding the model: anisotropic displacement parameters in protein structure refinement, Acta Crystallogr., Sect. D 55, 1109-1117.
    • (1999) Acta Crystallogr., Sect. D , vol.55 , pp. 1109-1117
    • Merritt, E.A.1
  • 59
    • 0034129580 scopus 로고    scopus 로고
    • 3D EXAFS refinement of the Cu site of azurin sheds light on the nature of structural change at the metal centre in an oxidation-reduction process: An integrated approach combining EXAFS and crystallography
    • Cheung, K. C., Strange, R. W., and Hasnain, S. S. (2000) 3D EXAFS refinement of the Cu site of azurin sheds light on the nature of structural change at the metal centre in an oxidation-reduction process: an integrated approach combining EXAFS and crystallography, Acta Crystallogr., Sect. D 56, 697-704.
    • (2000) Acta Crystallogr., Sect. D , vol.56 , pp. 697-704
    • Cheung, K.C.1    Strange, R.W.2    Hasnain, S.S.3
  • 60
    • 0037208353 scopus 로고    scopus 로고
    • Marriage of XAFS and crystallography for structure-function studies of metalloproteins
    • Hasnain, S. S., and Strange, R. W. (2003) Marriage of XAFS and crystallography for structure-function studies of metalloproteins, J. Synchrotron Radiat. 10, 9-15.
    • (2003) J. Synchrotron Radiat. , vol.10 , pp. 9-15
    • Hasnain, S.S.1    Strange, R.W.2
  • 61
    • 0037270393 scopus 로고    scopus 로고
    • XAFS studies of nitrogenase: The MoFe and VFe proteins and the use of crystallographic coordinates in three-dimensional EXAFS data analysis
    • Strange, R. W., Eady, R. R., Lawson, D., and Hasnain, S. S. (2003) XAFS studies of nitrogenase: the MoFe and VFe proteins and the use of crystallographic coordinates in three-dimensional EXAFS data analysis, J. Synchrotron Radiat. 10, 71-75.
    • (2003) J. Synchrotron Radiat. , vol.10 , pp. 71-75
    • Strange, R.W.1    Eady, R.R.2    Lawson, D.3    Hasnain, S.S.4
  • 62
    • 0028964815 scopus 로고
    • Structural and spectroscopic studies of the copper site of stellacyanin
    • Strange, R. W., Reinhammar, B., Murphy, L. M., and Hasnain, S. S. (1995) Structural and spectroscopic studies of the copper site of stellacyanin, Biochemistry 34, 220-231.
    • (1995) Biochemistry , vol.34 , pp. 220-231
    • Strange, R.W.1    Reinhammar, B.2    Murphy, L.M.3    Hasnain, S.S.4
  • 63
    • 0034840203 scopus 로고    scopus 로고
    • Redox thermodynamics of mutant forms of the rubredoxin from Clostridium pasteurianum: Identification of a stable Fe-111 (S-Cys)(3)(OH) centre in the C6S mutant
    • Xiao, Z., Gardner, A. R., Cross, M., Maes, E. M., Czernuszewicz, R. S., Sola, M., and Wedd, A. G. (2001) Redox thermodynamics of mutant forms of the rubredoxin from Clostridium pasteurianum: identification of a stable Fe-111 (S-Cys)(3)(OH) centre in the C6S mutant, J. Biol. Inorg. Chem. 6, 638-649.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 638-649
    • Xiao, Z.1    Gardner, A.R.2    Cross, M.3    Maes, E.M.4    Czernuszewicz, R.S.5    Sola, M.6    Wedd, A.G.7
  • 64
    • 0032490087 scopus 로고    scopus 로고
    • The rubredoxin from Clostridium pasteurianum: Mutation of the iron cysteinyl ligands to serine. Crystal and molecular structures of oxidized and dithionite-treated forms of the Cys42Ser mutant
    • Xiao, Z. G., Lavery, M. J., Ayhen, M., Scrofani, S. D. B., Wilce, M. C. J., Guss, J. M., Tregloan, P. A., George, G. N., and Wedd, A. G. (1998) The rubredoxin from Clostridium pasteurianum: Mutation of the iron cysteinyl ligands to serine. Crystal and molecular structures of oxidized and dithionite-treated forms of the Cys42Ser mutant, J. Am. Chem. Soc. 120, 4135-4150.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4135-4150
    • Xiao, Z.G.1    Lavery, M.J.2    Ayhen, M.3    Scrofani, S.D.B.4    Wilce, M.C.J.5    Guss, J.M.6    Tregloan, P.A.7    George, G.N.8    Wedd, A.G.9
  • 65
    • 31644435754 scopus 로고    scopus 로고
    • Structure and redox properties of the protein, rubredoxin, and its ligand and metal mutants studied by electronic structure calculation
    • Sundararajan, M., Hillier, I. H., and Burton, N. A. (2006) Structure and redox properties of the protein, rubredoxin, and its ligand and metal mutants studied by electronic structure calculation, J. Phys. Chem. A 110, 785-790.
    • (2006) J. Phys. Chem. A , vol.110 , pp. 785-790
    • Sundararajan, M.1    Hillier, I.H.2    Burton, N.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.