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Volumn 52, Issue 46, 2013, Pages 8267-8275

Metalloproteins diversified: The auracyanins are a family of cupredoxins that stretch the spectral and redox limits of blue copper proteins

Author keywords

[No Author keywords available]

Indexed keywords

BLUE-COPPER PROTEINS; CHLOROFLEXUS AURANTIACUS; ELECTRON TRANSFER PROTEINS; ELECTRON-TRANSFER REACTIONS; METALLO-PROTEINS; MIDPOINT POTENTIALS; TEMPERATURE DEPENDENT; UV-VIS ABSORPTION SPECTRA;

EID: 84888215080     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401163g     Document Type: Article
Times cited : (19)

References (48)
  • 1
    • 77954762503 scopus 로고    scopus 로고
    • Electron flow through metalloproteins
    • Gray, H. B. and Winkler, J. R. (2010) Electron flow through metalloproteins Biochim. Biophys. Acta 1797, 1563-1572
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1563-1572
    • Gray, H.B.1    Winkler, J.R.2
  • 2
    • 0011509370 scopus 로고    scopus 로고
    • Structural and functional aspects of metal sites in biology
    • Holm, R. H., Kennepohl, P., and Solomon, E. I. (1996) Structural and functional aspects of metal sites in biology Chem. Rev. 96, 2239-2314
    • (1996) Chem. Rev. , vol.96 , pp. 2239-2314
    • Holm, R.H.1    Kennepohl, P.2    Solomon, E.I.3
  • 3
    • 37349071628 scopus 로고    scopus 로고
    • Electron-Transfer Proteins
    • in (Gray, H. B. Stiefel, E, I. Valentine, J. S. and Bertini, I. Eds.) 1 st ed. pp, University Science Books, Herendon, VA
    • Banci, L., Bertini, I., Luchinat, C., and Turano, P. (2006) Electron-Transfer Proteins, in Biological Inorganic Chemistry: Structure and Reactivity (Gray, H. B., Stiefel, E, I., Valentine, J. S., and Bertini, I., Eds.) 1 st ed., pp 229-261, University Science Books, Herendon, VA.
    • (2006) Biological Inorganic Chemistry: Structure and Reactivity , pp. 229-261
    • Banci, L.1    Bertini, I.2    Luchinat, C.3    Turano, P.4
  • 4
  • 5
    • 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, 2491-2514
    • (1996) Chem. Rev. , vol.96 , pp. 2491-2514
    • Stephens, P.J.1    Jollie, D.R.2    Warshel, A.3
  • 6
    • 70449090691 scopus 로고    scopus 로고
    • Rationally tuning the reduction potential of a single cupredoxin beyond the natural range
    • Marshall, N. M., Garner, D. K., Wilson, T. D., Gao, Y.-G., Robinson, H., Nilges, M. J., and Lu, Y. (2009) Rationally tuning the reduction potential of a single cupredoxin beyond the natural range Nature 462, 113-116
    • (2009) Nature , vol.462 , pp. 113-116
    • Marshall, N.M.1    Garner, D.K.2    Wilson, T.D.3    Gao, Y.-G.4    Robinson, H.5    Nilges, M.J.6    Lu, Y.7
  • 7
    • 0022400183 scopus 로고
    • Cytochromes in Chloroflexus aurantiacus grown with and without oxygen
    • Pierson, B. (1985) Cytochromes in Chloroflexus aurantiacus grown with and without oxygen Arch. Microbiol. 143, 260-265
    • (1985) Arch. Microbiol. , vol.143 , pp. 260-265
    • Pierson, B.1
  • 9
    • 77955236947 scopus 로고    scopus 로고
    • Structural analysis of alternative complex III in the photosynthetic electron transfer chain of Chloroflexus aurantiacus
    • Gao, X., Xin, Y., Bell, P. D., Wen, J., and Blankenship, R. E. (2010) Structural analysis of alternative complex III in the photosynthetic electron transfer chain of Chloroflexus aurantiacus Biochemistry 49, 6670-6679
    • (2010) Biochemistry , vol.49 , pp. 6670-6679
    • Gao, X.1    Xin, Y.2    Bell, P.D.3    Wen, J.4    Blankenship, R.E.5
  • 10
    • 0026703005 scopus 로고
    • Isolation, characterization, and amino acid sequences of auracyanins, blue copper proteins from the green photosynthetic bacterium Chloroflexus aurantiacus
    • McManus, J. D., Brune, D. C., Han, J., Sanders-Loehr, J., Meyer, T. E., Cusanovich, M. a, Tollin, G., and Blankenship, R. E. (1992) Isolation, characterization, and amino acid sequences of auracyanins, blue copper proteins from the green photosynthetic bacterium Chloroflexus aurantiacus J. Biol. Chem. 267, 6531-6540
    • (1992) J. Biol. Chem. , vol.267 , pp. 6531-6540
    • McManus, J.D.1    Brune, D.C.2    Han, J.3    Sanders-Loehr, J.4    Meyer, T.E.5    Cusanovich, M.A.6    Tollin, G.7    Blankenship, R.E.8
  • 12
    • 84884674352 scopus 로고    scopus 로고
    • Alternative Complex III from phototrophic bacteria and its electron acceptor auracyanin
    • Majumder, E. L. W., King, J. D., and Blankenship, R. E. (2013) Alternative Complex III from phototrophic bacteria and its electron acceptor auracyanin Biochim. Biophys. Acta 1827, 1383-1391
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 1383-1391
    • Majumder, E.L.W.1    King, J.D.2    Blankenship, R.E.3
  • 13
    • 84862820783 scopus 로고    scopus 로고
    • Comparison of Chloroflexus aurantiacus strain J-10-fl proteomes of cells grown chemoheterotrophically and photoheterotrophically
    • Cao, L., Bryant, D. a, Schepmoes, A. a, Vogl, K., Smith, R. D., Lipton, M. S., and Callister, S. J. (2012) Comparison of Chloroflexus aurantiacus strain J-10-fl proteomes of cells grown chemoheterotrophically and photoheterotrophically Photosynth. Res. 110, 153-168
    • (2012) Photosynth. Res. , vol.110 , pp. 153-168
    • Cao, L.1    Bryant, D.A.2    Schepmoes, A.A.3    Vogl, K.4    Smith, R.D.5    Lipton, M.S.6    Callister, S.J.7
  • 15
    • 0018860792 scopus 로고
    • A potentiometric and kinetic study on the respiratory chain of ferrous-iron-grown Thiobacillus ferrooxidans
    • Ingledew, J W and C., J. G. (1980) A potentiometric and kinetic study on the respiratory chain of ferrous-iron-grown Thiobacillus ferrooxidans Biochim. Biophys. Acta 590, 141-158
    • (1980) Biochim. Biophys. Acta , vol.590 , pp. 141-158
    • Ingledew, J.W.1
  • 16
    • 0037065671 scopus 로고    scopus 로고
    • Nitrosocyanin, a red cupredoxin-like protein from Nitrosomonas europaea
    • Arciero, D., Pierce, B., Hendrich, M., and Hooper, A. (2002) Nitrosocyanin, a red cupredoxin-like protein from Nitrosomonas europaea Biochemistry 41, 1703-1709
    • (2002) Biochemistry , vol.41 , pp. 1703-1709
    • Arciero, D.1    Pierce, B.2    Hendrich, M.3    Hooper, A.4
  • 17
    • 33750317005 scopus 로고    scopus 로고
    • Spectroscopic methods in bioinorganic chemistry: Blue to green to red copper sites
    • Solomon, E. I. (2006) Spectroscopic methods in bioinorganic chemistry: blue to green to red copper sites Inorg. Chem. 45, 8012-8025
    • (2006) Inorg. Chem. , vol.45 , pp. 8012-8025
    • Solomon, E.I.1
  • 19
    • 79955851405 scopus 로고    scopus 로고
    • Incorporation of the red copper nitrosocyanin binding loop into blue copper azurin
    • Berry, S. M., Bladholm, E. L., Mostad, E. J., and Schenewerk, A. R. (2011) Incorporation of the red copper nitrosocyanin binding loop into blue copper azurin J. Biol. Inorg. Chem. 16, 473-480
    • (2011) J. Biol. Inorg. Chem. , vol.16 , pp. 473-480
    • Berry, S.M.1    Bladholm, E.L.2    Mostad, E.J.3    Schenewerk, A.R.4
  • 20
    • 33846418760 scopus 로고    scopus 로고
    • Engineering copper sites in proteins: Loops confer native structures and properties to chimeric cupredoxins
    • Li, C., Banfield, M. J., and Dennison, C. (2007) Engineering copper sites in proteins: loops confer native structures and properties to chimeric cupredoxins J. Am. Chem. Soc. 129, 709-718
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 709-718
    • Li, C.1    Banfield, M.J.2    Dennison, C.3
  • 21
    • 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
  • 22
    • 0035873518 scopus 로고    scopus 로고
    • Crystal structure of a novel red copper protein from Nitrosomonas europaea
    • Lieberman, R. and Arciero, D. (2001) Crystal structure of a novel red copper protein from Nitrosomonas europaea Biochemistry 5674-5681
    • (2001) Biochemistry , pp. 5674-5681
    • Lieberman, R.1    Arciero, D.2
  • 23
    • 0026353602 scopus 로고
    • The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycoclastes
    • Godden, A. J. W., Turley, S., Teller, D. C., Adman, E. T., Liu, M. Y., and Legall, J. (1991) The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycoclastes Science 253, 438-442
    • (1991) Science , vol.253 , pp. 438-442
    • Godden, A.J.W.1    Turley, S.2    Teller, D.C.3    Adman, E.T.4    Liu, M.Y.5    Legall, J.6
  • 24
    • 0023130391 scopus 로고
    • The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a signal peptide. Cloning and sequencing of the azurin gene
    • Canters, G. W. (1987) The azurin gene from Pseudomonas aeruginosa codes for a pre-protein with a signal peptide. Cloning and sequencing of the azurin gene FEBS Lett. 212, 168-172
    • (1987) FEBS Lett. , vol.212 , pp. 168-172
    • Canters, G.W.1
  • 26
    • 61849102905 scopus 로고    scopus 로고
    • The crystal structure of auracyanin A at 1.85 A resolution: The structures and functions of auracyanins A and B, two almost identical "blue" copper proteins, in the photosynthetic bacterium Chloroflexus aurantiacus
    • Lee, M., Del Rosario, M. C., Harris, H. H., Blankenship, R. E., Guss, J. M., and Freeman, H. C. (2009) The crystal structure of auracyanin A at 1.85 A resolution: the structures and functions of auracyanins A and B, two almost identical "blue" copper proteins, in the photosynthetic bacterium Chloroflexus aurantiacus J. Biol. Inorg. Chem. 14, 329-345
    • (2009) J. Biol. Inorg. Chem. , vol.14 , pp. 329-345
    • Lee, M.1    Del Rosario, M.C.2    Harris, H.H.3    Blankenship, R.E.4    Guss, J.M.5    Freeman, H.C.6
  • 27
    • 37549006458 scopus 로고    scopus 로고
    • The role played by the alpha-helix in the unfolding pathway and stability of azurin: Switching between hierarchic and nonhierarchic folding
    • Manetto, G. D., Grasso, D. M., Milardi, D., Pappalardo, M., Guzzi, R., Sportelli, L., Verbeet, M. P., Canters, G. W., and La Rosa, C. (2007) The role played by the alpha-helix in the unfolding pathway and stability of azurin: switching between hierarchic and nonhierarchic folding ChemBioChem 8, 1941-1949
    • (2007) ChemBioChem , vol.8 , pp. 1941-1949
    • Manetto, G.D.1    Grasso, D.M.2    Milardi, D.3    Pappalardo, M.4    Guzzi, R.5    Sportelli, L.6    Verbeet, M.P.7    Canters, G.W.8    La Rosa, C.9
  • 28
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • Stoll, S. and Schweiger, A. (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR J. Magn. Reson. 178, 42-55
    • (2006) J. Magn. Reson. , vol.178 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 29
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura, K., Dudley, J., Nei, M., and Kumar, S. (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0 Mol. Biol. Evol. 24, 1596-1599
    • (2007) Mol. Biol. Evol. , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 30
    • 0032924955 scopus 로고    scopus 로고
    • Auracyanin A from the thermophilic green gliding photosynthetic bacterium Chloroflexus aurantiacus represents an unusual class of small blue copper proteins
    • Van Driessche, G., Hu, W., Van de Werken, G., Selvaraj, F., McManus, J. D., Blankenship, R. E., and Van Beeumen, J. J. (1999) Auracyanin A from the thermophilic green gliding photosynthetic bacterium Chloroflexus aurantiacus represents an unusual class of small blue copper proteins Protein Sci. 8, 947-957
    • (1999) Protein Sci. , vol.8 , pp. 947-957
    • Van Driessche, G.1    Hu, W.2    Van De Werken, G.3    Selvaraj, F.4    McManus, J.D.5    Blankenship, R.E.6    Van Beeumen, J.J.7
  • 31
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D. G., and Heringa, J. (2000) T-Coffee: A novel method for fast and accurate multiple sequence alignment J. Mol. Biol. 302, 205-217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 32
    • 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 George, S., 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 George, S.3    Basumallick, L.4
  • 33
    • 79952101722 scopus 로고    scopus 로고
    • Recent advances in understanding blue copper proteins
    • Solomon, E. I. and Hadt, R. G. (2011) Recent advances in understanding blue copper proteins Coord. Chem. Rev. 255, 774-789
    • (2011) Coord. Chem. Rev. , vol.255 , pp. 774-789
    • Solomon, E.I.1    Hadt, R.G.2
  • 34
    • 33845280170 scopus 로고
    • Electronic structure of plastocyanin: Excited state spectral features
    • Gewirth, A. and Solomon, E. (1988) Electronic structure of plastocyanin: excited state spectral features J. Am. Chem. Soc. 110, 3811-3819
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 3811-3819
    • Gewirth, A.1    Solomon, E.2
  • 35
    • 0032560925 scopus 로고    scopus 로고
    • Spectroscopic and geometric variations in perturbed blue copper centers: Electronic structures of stellacyanin and cucumber basic protein
    • LaCroix, L. and Randall, D. (1998) Spectroscopic and geometric variations in perturbed blue copper centers: electronic structures of stellacyanin and cucumber basic protein J. Am. Chem. Soc. 7863, 9621-9631
    • (1998) J. Am. Chem. Soc. , vol.7863 , pp. 9621-9631
    • Lacroix, L.1    Randall, D.2
  • 36
    • 0032544647 scopus 로고    scopus 로고
    • Gene synthesis, expression, and mutagenesis of zucchini mavicyanin: The fourth ligand of blue copper center is Gln
    • Kataoka, K., Nakai, M., Yamaguchi, K., and Suzuki, S. (1998) Gene synthesis, expression, and mutagenesis of zucchini mavicyanin: the fourth ligand of blue copper center is Gln Biochem. Biophys. Res. Commun. 250, 409-413
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 409-413
    • Kataoka, K.1    Nakai, M.2    Yamaguchi, K.3    Suzuki, S.4
  • 37
    • 0033734431 scopus 로고    scopus 로고
    • Spectroscopic and electrochemical properties of the Met86Gln mutant of Achromobacter cycloclastes pseudoazurin
    • Kataoka, K., Kondo, a, Yamaguchi, K., and Suzuki, S. (2000) Spectroscopic and electrochemical properties of the Met86Gln mutant of Achromobacter cycloclastes pseudoazurin J. Inorg. Biochem. 82, 79-84
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 79-84
    • Kataoka, K.1    Kondo, A.2    Yamaguchi, K.3    Suzuki, S.4
  • 38
    • 0033977211 scopus 로고    scopus 로고
    • Loop-directed mutagenesis of the blue copper protein amicyanin from Paracoccus versutus and its effect on the structure and the activity of the type-1 copper site
    • Buning, C., Canters, G. W., Comba, P., Dennison, C., Jeuken, L., Melter, M., and Sanders-Loehr, J. (2000) Loop-directed mutagenesis of the blue copper protein amicyanin from Paracoccus versutus and its effect on the structure and the activity of the type-1 copper site J. Am. Chem. Soc. 122, 204-211
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 204-211
    • Buning, C.1    Canters, G.W.2    Comba, P.3    Dennison, C.4    Jeuken, L.5    Melter, M.6    Sanders-Loehr, J.7
  • 39
    • 65249168774 scopus 로고    scopus 로고
    • Thermodynamic equilibrium between blue and green copper sites and the role of the protein in controlling function
    • Ghosh, S., Xie, X., Dey, A., Sun, Y., Scholes, C. P., and Solomon, E. I. (2009) Thermodynamic equilibrium between blue and green copper sites and the role of the protein in controlling function Proc. Natl. Acad. Sci. U.S.A. 106, 4969-4974
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 4969-4974
    • Ghosh, S.1    Xie, X.2    Dey, A.3    Sun, Y.4    Scholes, C.P.5    Solomon, E.I.6
  • 40
    • 0022400803 scopus 로고
    • An inducible periplasmic blue copper protein from
    • Husain, M. and Davidsons, V. L. (1985) An inducible periplasmic blue copper protein from J. Biol. Chem. 260, 14626-14629
    • (1985) J. Biol. Chem. , vol.260 , pp. 14626-14629
    • Husain, M.1    Davidsons, V.L.2
  • 41
    • 84961982126 scopus 로고    scopus 로고
    • Spectroscopic and DFT studies of second-sphere variants of the type 1 copper site in azurin: Covalent and nonlocal electrostatic contributions to reduction potentials
    • Hadt, R. G., Sun, N., Marshall, N. M., Hodgson, K. O., Hedman, B., Lu, Y., and Solomon, E. I. (2012) Spectroscopic and DFT studies of second-sphere variants of the type 1 copper site in azurin: covalent and nonlocal electrostatic contributions to reduction potentials J. Am. Chem. Soc. 134, 16701-16716
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 16701-16716
    • Hadt, R.G.1    Sun, N.2    Marshall, N.M.3    Hodgson, K.O.4    Hedman, B.5    Lu, Y.6    Solomon, E.I.7
  • 43
    • 33751385403 scopus 로고
    • Halocyanin, an archaebacterial blue copper protein (type I) from Natronobacterium pharaonis
    • Scharf, B. and Engelhard, M. (1993) Halocyanin, an archaebacterial blue copper protein (type I) from Natronobacterium pharaonis Biochemistry 32, 12894-12900
    • (1993) Biochemistry , vol.32 , pp. 12894-12900
    • Scharf, B.1    Engelhard, M.2
  • 44
    • 0023003367 scopus 로고
    • Measurement of the oxidation-reduction potentials of amicyanin and c-type cytochromes from Paracoccus denitrificans
    • Gray, K., Knaff, D., Husain, M., and Davidson, V. (1986) Measurement of the oxidation-reduction potentials of amicyanin and c-type cytochromes from Paracoccus denitrificans FEBS Lett. 207, 2-5
    • (1986) FEBS Lett. , vol.207 , pp. 2-5
    • Gray, K.1    Knaff, D.2    Husain, M.3    Davidson, V.4
  • 45
    • 84867019070 scopus 로고    scopus 로고
    • The X-ray crystal structure of a pseudoazurin from Sinorhizobium meliloti
    • Laming, E. M., McGrath, A. P., Guss, J. M., Kappler, U., and Maher, M. J. (2012) The X-ray crystal structure of a pseudoazurin from Sinorhizobium meliloti J. Inorg. Biochem. 115, 148-154
    • (2012) J. Inorg. Biochem. , vol.115 , pp. 148-154
    • Laming, E.M.1    McGrath, A.P.2    Guss, J.M.3    Kappler, U.4    Maher, M.J.5
  • 46
    • 84866987833 scopus 로고    scopus 로고
    • How are "atypical" sulfite dehydrogenases linked to cell metabolism? Interactions between the SorT sulfite dehydrogenase and small redox proteins
    • Low, L., Ryan Kilmartin, J., Paul, V, B., and Ulrike, K. (2011) How are "atypical" sulfite dehydrogenases linked to cell metabolism? Interactions between the SorT sulfite dehydrogenase and small redox proteins Front. Microbiol. 2, 58
    • (2011) Front. Microbiol. , vol.2 , pp. 58
    • Low, L.1    Ryan Kilmartin, J.2    Paul, V.B.3    Ulrike, K.4
  • 47
    • 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
  • 48
    • 0026611038 scopus 로고
    • The importance of Asn47 for structure and reactivity of azurin from Alcaligenes denitrificans as studied by site-directed mutagenesis and spectroscopy
    • Hoitink, C. W. and Canters, G. W. (1992) The importance of Asn47 for structure and reactivity of azurin from Alcaligenes denitrificans as studied by site-directed mutagenesis and spectroscopy J. Biol. Chem. 267, 13836-13842
    • (1992) J. Biol. Chem. , vol.267 , pp. 13836
    • Hoitink, C.W.1    Canters, G.W.2


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