메뉴 건너뛰기




Volumn 358, Issue 4, 2006, Pages 1081-1093

A Rearranging Ligand Enables Allosteric Control of Catalytic Activity in Copper-containing Nitrite Reductase

Author keywords

catalytic activity; copper; crystal structure; ligand; nitrate reductase

Indexed keywords

COPPER; LIGAND; NITRITE REDUCTASE; NITROGEN;

EID: 33646085537     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.02.042     Document Type: Article
Times cited : (13)

References (53)
  • 2
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • Zumft W.G. Cell biology and molecular basis of denitrification. Microbiol. Mol. Biol. Rev. 61 (1997) 533-616
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 3
    • 4143056986 scopus 로고    scopus 로고
    • Bidirectional catalysis by copper-containing nitrite reductase
    • Wijma H.J., Canters G.W., de Vries S., and Verbeet M.P. Bidirectional catalysis by copper-containing nitrite reductase. Biochemistry 43 (2004) 10467-10474
    • (2004) Biochemistry , vol.43 , pp. 10467-10474
    • Wijma, H.J.1    Canters, G.W.2    de Vries, S.3    Verbeet, M.P.4
  • 4
    • 0028298314 scopus 로고
    • X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: roles of two copper atoms in nitrite reduction
    • Kukimoto M., Nishiyama M., Murphy M.E., Turley S., Adman E.T., Horinouchi S., and Beppu T. X-ray structure and site-directed mutagenesis of a nitrite reductase from Alcaligenes faecalis S-6: roles of two copper atoms in nitrite reduction. Biochemistry 33 (1994) 5246-5252
    • (1994) Biochemistry , vol.33 , pp. 5246-5252
    • Kukimoto, M.1    Nishiyama, M.2    Murphy, M.E.3    Turley, S.4    Adman, E.T.5    Horinouchi, S.6    Beppu, T.7
  • 5
    • 0026353602 scopus 로고
    • The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes
    • Godden J.W., Turley S., Teller D.C., Adman E.T., Liu M.Y., Payne W.J., and LeGall J. The 2.3 angstrom X-ray structure of nitrite reductase from Achromobacter cycloclastes. Science 253 (1991) 438-442
    • (1991) Science , vol.253 , pp. 438-442
    • Godden, J.W.1    Turley, S.2    Teller, D.C.3    Adman, E.T.4    Liu, M.Y.5    Payne, W.J.6    LeGall, J.7
  • 6
    • 0026701748 scopus 로고
    • Evidence that the type-2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase
    • Libby E., and Averill B.A. Evidence that the type-2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase. Biochem. Biophys. Res. Commun. 187 (1992) 1529-1535
    • (1992) Biochem. Biophys. Res. Commun. , vol.187 , pp. 1529-1535
    • Libby, E.1    Averill, B.A.2
  • 7
    • 0034604550 scopus 로고    scopus 로고
    • Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase
    • Boulanger M.J., Kukimoto M., Nishiyama M., Horinouchi S., and Murphy M.E. Catalytic roles for two water bridged residues (Asp-98 and His-255) in the active site of copper-containing nitrite reductase. J. Biol. Chem. 275 (2000) 23957-23964
    • (2000) J. Biol. Chem. , vol.275 , pp. 23957-23964
    • Boulanger, M.J.1    Kukimoto, M.2    Nishiyama, M.3    Horinouchi, S.4    Murphy, M.E.5
  • 8
    • 0035822630 scopus 로고    scopus 로고
    • Alternate substrate binding modes to two mutant (D98N and H255N) forms of nitrite reductase from Alcaligenes faecalis S-6: structural model of a transient catalytic intermediate
    • Boulanger M.J., and Murphy M.E. Alternate substrate binding modes to two mutant (D98N and H255N) forms of nitrite reductase from Alcaligenes faecalis S-6: structural model of a transient catalytic intermediate. Biochemistry 40 (2001) 9132-9141
    • (2001) Biochemistry , vol.40 , pp. 9132-9141
    • Boulanger, M.J.1    Murphy, M.E.2
  • 9
    • 0030658026 scopus 로고    scopus 로고
    • Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications
    • Murphy M.E., Turley S., and Adman E.T. Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis. Mechanistic implications. J. Biol. Chem. 272 (1997) 28455-28460
    • (1997) J. Biol. Chem. , vol.272 , pp. 28455-28460
    • Murphy, M.E.1    Turley, S.2    Adman, E.T.3
  • 10
    • 0034097583 scopus 로고    scopus 로고
    • Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase
    • Kataoka K., Furusawa H., Takagi K., Yamaguchi K., and Suzuki S. Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase. J. Biochem. (Tokyo) 127 (2000) 345-350
    • (2000) J. Biochem. (Tokyo) , vol.127 , pp. 345-350
    • Kataoka, K.1    Furusawa, H.2    Takagi, K.3    Yamaguchi, K.4    Suzuki, S.5
  • 11
    • 1542378734 scopus 로고    scopus 로고
    • Electronic structures of metal sites in proteins and models: contribution to function in blue copper proteins
    • Solomon E.I., Szilagyi R.K., DeBeer George S., and Basumallick L. Electronic structures of metal sites in proteins and models: contribution to function in blue copper proteins. Chem. Rev. 104 (2004) 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
  • 12
    • 0006198801 scopus 로고
    • Type-1 and type-2 copper sites obtained by external addition of ligands to a His117gly azurin mutant
    • Den Blaauwen T., Van de Kamp M., and Canters G.W. Type-1 and type-2 copper sites obtained by external addition of ligands to a His117gly azurin mutant. J. Am. Chem. Soc. 113 (1991) 5050-5052
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5050-5052
    • Den Blaauwen, T.1    Van de Kamp, M.2    Canters, G.W.3
  • 13
    • 0034625312 scopus 로고    scopus 로고
    • The structural role of the copper-coordinating and surface- exposed histidine residue in the blue copper protein azurin
    • Jeuken L.J.C., Ubbink M., Bitter J.H., van Vliet P., Meyer-Klaucke W., and Canters G.W. The structural role of the copper-coordinating and surface- exposed histidine residue in the blue copper protein azurin. J. Mol. Biol. 299 (2000) 737-755
    • (2000) J. Mol. Biol. , vol.299 , pp. 737-755
    • Jeuken, L.J.C.1    Ubbink, M.2    Bitter, J.H.3    van Vliet, P.4    Meyer-Klaucke, W.5    Canters, G.W.6
  • 14
    • 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. 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 (2000) 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
  • 15
    • 0030070183 scopus 로고    scopus 로고
    • The role of His117 in the redox reactions of azurin from Pseudomonas aeruginosa
    • Gorren A.C., den Blaauwen T., Canters G.W., Hopper D.J., and Duine J.A. The role of His117 in the redox reactions of azurin from Pseudomonas aeruginosa. FEBS Letters 381 (1996) 140-142
    • (1996) FEBS Letters , vol.381 , pp. 140-142
    • Gorren, A.C.1    den Blaauwen, T.2    Canters, G.W.3    Hopper, D.J.4    Duine, J.A.5
  • 16
    • 0030058062 scopus 로고    scopus 로고
    • Spectroscopic and mechanistic studies of type-1 and type-2 copper sites in Pseudomonas aeruginosa azurin as obtained by addition of external ligands to mutant His46Gly
    • van Pouderoyen G., Andrew C.R., Loehr T.M., Sanders-Loehr J., Mazumdar S., Allen H., et al. Spectroscopic and mechanistic studies of type-1 and type-2 copper sites in Pseudomonas aeruginosa azurin as obtained by addition of external ligands to mutant His46Gly. Biochemistry 35 (1996) 1397-1407
    • (1996) Biochemistry , vol.35 , pp. 1397-1407
    • van Pouderoyen, G.1    Andrew, C.R.2    Loehr, T.M.3    Sanders-Loehr, J.4    Mazumdar, S.5    Allen, H.6
  • 17
    • 0029844543 scopus 로고    scopus 로고
    • Dimerization of a His117Gly azurin mutant by external addition of 1,omega-di(imidazol-1-yl)alkanes
    • van Pouderoyen G., den Blaauwen T., Reedijk J., and Canters G.W. Dimerization of a His117Gly azurin mutant by external addition of 1,omega-di(imidazol-1-yl)alkanes. Biochemistry 35 (1996) 13205-13211
    • (1996) Biochemistry , vol.35 , pp. 13205-13211
    • van Pouderoyen, G.1    den Blaauwen, T.2    Reedijk, J.3    Canters, G.W.4
  • 18
    • 33748229590 scopus 로고
    • Novel biological copper proteins through anion addition to the mutant Met121Gly of Pseudomonas aeruginosa azurin
    • Vidakovic M., and Germanas J.P. Novel biological copper proteins through anion addition to the mutant Met121Gly of Pseudomonas aeruginosa azurin. Angew. Chem., Int. Ed. 34 (1995) 1622-1624
    • (1995) Angew. Chem., Int. Ed. , vol.34 , pp. 1622-1624
    • Vidakovic, M.1    Germanas, J.P.2
  • 20
    • 0242668714 scopus 로고    scopus 로고
    • Reconstitution of the type-1 active site of the H145G/A variants of nitrite reductase by ligand insertion
    • Wijma H.J., Boulanger M.J., Molon A., Fittipaldi M., Huber M., Murphy M.E., et al. Reconstitution of the type-1 active site of the H145G/A variants of nitrite reductase by ligand insertion. Biochemistry 42 (2003) 4075-4083
    • (2003) Biochemistry , vol.42 , pp. 4075-4083
    • Wijma, H.J.1    Boulanger, M.J.2    Molon, A.3    Fittipaldi, M.4    Huber, M.5    Murphy, M.E.6
  • 21
    • 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. Role of the axial ligand in type 1 Cu centers studied by point mutations of met148 in rusticyanin. Biochemistry 38 (1999) 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
  • 22
    • 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. Spectroscopic and electrochemical properties of the Met86Gln mutant of Achromobacter cycloclastes pseudoazurin. J. Inorg. Biochem. 82 (2000) 79-84
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 79-84
    • Kataoka, K.1    Kondo, A.2    Yamaguchi, K.3    Suzuki, S.4
  • 23
    • 0037418715 scopus 로고    scopus 로고
    • Characterization and function of Met150Gln mutant of copper-containing nitrite reductase from Achromobacter cycloclastes IAM1013
    • Kataoka K., Yamaguchi K., Sakai S., Takagi K., and Suzuki S. Characterization and function of Met150Gln mutant of copper-containing nitrite reductase from Achromobacter cycloclastes IAM1013. Biochem. Biophys. Res. Commun. 303 (2003) 519-524
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 519-524
    • Kataoka, K.1    Yamaguchi, K.2    Sakai, S.3    Takagi, K.4    Suzuki, S.5
  • 24
    • 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. Probing the role of axial methionine in the blue copper center of azurin with unnatural amino acids. J. Am. Chem. Soc. 125 (2003) 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
  • 25
    • 0034622646 scopus 로고    scopus 로고
    • The Met99Gln mutant of amicyanin from Paracoccus versutus
    • Diederix R.E.M., Canters G.W., and Dennison C. The Met99Gln mutant of amicyanin from Paracoccus versutus. Biochemistry 39 (2000) 9551-9560
    • (2000) Biochemistry , vol.39 , pp. 9551-9560
    • Diederix, R.E.M.1    Canters, G.W.2    Dennison, C.3
  • 26
    • 0032574836 scopus 로고    scopus 로고
    • Spectroscopic, kinetic, and electrochemical characterization of heterologously expressed wild-type and mutant forms of copper- containing nitrite reductase from Rhodobacter sphaeroides 2.4.3
    • Olesen K., Veselov A., Zhao Y., Wang Y., Danner B., Scholes C.P., and Shapleigh J.P. Spectroscopic, kinetic, and electrochemical characterization of heterologously expressed wild-type and mutant forms of copper- containing nitrite reductase from Rhodobacter sphaeroides 2.4.3. Biochemistry 37 (1998) 6086-6094
    • (1998) Biochemistry , vol.37 , pp. 6086-6094
    • Olesen, K.1    Veselov, A.2    Zhao, Y.3    Wang, Y.4    Danner, B.5    Scholes, C.P.6    Shapleigh, J.P.7
  • 27
    • 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. Reduction potentials and their pH dependence in site-directed-mutant forms of azurin from Pseudomonas aeruginosa. Eur. J. Biochem. 212 (1993) 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
  • 28
    • 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. X-ray analysis and spectroscopic characterization of M121Q azurin. A copper site model for stellacyanin. J. Mol. Biol. 229 (1993) 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
  • 29
    • 0030069115 scopus 로고    scopus 로고
    • Environment of copper in Pseudomonas aeruginosa azurin probed by binding of exogenous ligands to Met121X (X=Gly, Ala, Val, Leu, or Asp) mutants
    • Bonander N., Karlsson B.G., and Vanngard T. Environment of copper in Pseudomonas aeruginosa azurin probed by binding of exogenous ligands to Met121X (X=Gly, Ala, Val, Leu, or Asp) mutants. Biochemistry 35 (1996) 2429-2436
    • (1996) Biochemistry , vol.35 , pp. 2429-2436
    • Bonander, N.1    Karlsson, B.G.2    Vanngard, T.3
  • 30
    • 0030512439 scopus 로고    scopus 로고
    • Mutant Met121Ala of Pseudomonas aeruginosa azurin and its azide derivative: crystal structure and spectral properties
    • Tsai L., Bonander N., Harata K., Karlsson B.G., Vänngard T., Langer V., and Sjölin L. Mutant Met121Ala of Pseudomonas aeruginosa azurin and its azide derivative: crystal structure and spectral properties. Acta Crystallog. sect. D 52 (1996) 950-958
    • (1996) Acta Crystallog. sect. D , vol.52 , pp. 950-958
    • Tsai, L.1    Bonander, N.2    Harata, K.3    Karlsson, B.G.4    Vänngard, T.5    Langer, V.6    Sjölin, L.7
  • 31
    • 0035932675 scopus 로고    scopus 로고
    • A single-crystal electron paramagnetic resonance study at 95 GHz of the type-1 copper site of the green nitrite reductase of Alcaligenes faecalis
    • van Gastel M., Boulanger M.J., Canters G.W., Huber M., Murphy M.E.P., Verbeet M.P., and Groenen E.J.J. A single-crystal electron paramagnetic resonance study at 95 GHz of the type-1 copper site of the green nitrite reductase of Alcaligenes faecalis. J. Phys. Chem. B 105 (2001) 2236-2243
    • (2001) J. Phys. Chem. B , vol.105 , pp. 2236-2243
    • van Gastel, M.1    Boulanger, M.J.2    Canters, G.W.3    Huber, M.4    Murphy, M.E.P.5    Verbeet, M.P.6    Groenen, E.J.J.7
  • 32
    • 0032561819 scopus 로고    scopus 로고
    • Relation between the structure and spectroscopic properties of blue copper proteins
    • Pierloot K., De Kerpel J.O.A., Ryde U., Olsson M.H.M., and Roos B.O. Relation between the structure and spectroscopic properties of blue copper proteins. J. Am. Chem. Soc. 120 (1998) 13156-13166
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 13156-13166
    • Pierloot, K.1    De Kerpel, J.O.A.2    Ryde, U.3    Olsson, M.H.M.4    Roos, B.O.5
  • 33
    • 0029794252 scopus 로고    scopus 로고
    • Electronic structure of the perturbed blue copper site in nitrite reductase: spectroscopic properties, bonding, and implications for the entatic/rack state
    • LaCroix L.B., Shadle S.E., Wang Y.N., Averill B.A., Hedman B., Hodgson K.O., and Solomon E.I. Electronic structure of the perturbed blue copper site in nitrite reductase: spectroscopic properties, bonding, and implications for the entatic/rack state. J. Am. Chem. Soc. 118 (1996) 7755-7768
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7755-7768
    • LaCroix, L.B.1    Shadle, S.E.2    Wang, Y.N.3    Averill, B.A.4    Hedman, B.5    Hodgson, K.O.6    Solomon, E.I.7
  • 34
    • 0033180952 scopus 로고    scopus 로고
    • Protein strain in blue copper proteins studied by free energy pertubations
    • De Kerpel J.O.A., and Ryde U. Protein strain in blue copper proteins studied by free energy pertubations. Proteins: Struct. Funct. Genet. 36 (1999) 157-174
    • (1999) Proteins: Struct. Funct. Genet. , vol.36 , pp. 157-174
    • De Kerpel, J.O.A.1    Ryde, U.2
  • 35
    • 0036303516 scopus 로고    scopus 로고
    • Biochemical and crystallographic studies of the Met144Ala, Asp92Asn and His254Phe mutants of the nitrite reductase from Alcaligenes xylosoxidans provide insight into the enzyme mechanism
    • Ellis M.J., Prudencio M., Dodd F.E., Strange R.W., Sawers G., Eady R.R., and Hasnain S.S. Biochemical and crystallographic studies of the Met144Ala, Asp92Asn and His254Phe mutants of the nitrite reductase from Alcaligenes xylosoxidans provide insight into the enzyme mechanism. J. Mol. Biol. 316 (2002) 51-64
    • (2002) J. Mol. Biol. , vol.316 , pp. 51-64
    • Ellis, M.J.1    Prudencio, M.2    Dodd, F.E.3    Strange, R.W.4    Sawers, G.5    Eady, R.R.6    Hasnain, S.S.7
  • 37
    • 1542298245 scopus 로고    scopus 로고
    • Met144Ala mutation of the copper-containing nitrite reductase from Alcaligenes xylosoxidans reverses the intramolecular electron transfer
    • Farver O., Eady R.R., Sawers G., Prudencio M., and Pecht I. Met144Ala mutation of the copper-containing nitrite reductase from Alcaligenes xylosoxidans reverses the intramolecular electron transfer. FEBS Letters 12 (2004) 173-176
    • (2004) FEBS Letters , vol.12 , pp. 173-176
    • Farver, O.1    Eady, R.R.2    Sawers, G.3    Prudencio, M.4    Pecht, I.5
  • 38
    • 33646119315 scopus 로고    scopus 로고
    • Cowen, J. A. (1993). Introduction. In Inorganic Biochemistry, p. 7, VCH Publishers, Inc., New York, Weinheim, Cambridge.
  • 39
    • 0030780641 scopus 로고    scopus 로고
    • Site-directed mutants of pseudoazurin: explenation of increased redox potentials from X-ray structures and from calculation of redox potential differences
    • Libeu C.A.P., Kukimoto M., Nishiyama M., Horinouchi S., and Adman E.T. Site-directed mutants of pseudoazurin: explenation of increased redox potentials from X-ray structures and from calculation of redox potential differences. Biochemistry 36 (1997) 13160-13179
    • (1997) Biochemistry , vol.36 , pp. 13160-13179
    • Libeu, C.A.P.1    Kukimoto, M.2    Nishiyama, M.3    Horinouchi, S.4    Adman, E.T.5
  • 40
    • 0026411154 scopus 로고    scopus 로고
    • Adman, E. T. (1991). Copper protein structures. In Advances in Protein Chemistry, vol. 42, pp. 145-197.
  • 41
    • 0027229994 scopus 로고
    • Cloning and characterization of a nitrite reductase gene from Alcaligenes faecalis and its expression in Escherichia coli
    • Nishiyama M., Suzuki J., Kukimoto M., Ohnuki T., Horinouchi S., and Beppu T. Cloning and characterization of a nitrite reductase gene from Alcaligenes faecalis and its expression in Escherichia coli. J. Gen. Microbiol. 139 (1993) 725-733
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 725-733
    • Nishiyama, M.1    Suzuki, J.2    Kukimoto, M.3    Ohnuki, T.4    Horinouchi, S.5    Beppu, T.6
  • 42
    • 0019498490 scopus 로고
    • A blue protein as an inactivating factor for nitrite reductase from Alcaligenes faecalis strain S-6
    • Kakutani T., Watanabe H., Arima K., and Beppu T. A blue protein as an inactivating factor for nitrite reductase from Alcaligenes faecalis strain S-6. J. Biochem. (Tokyo) 89 (1981) 463-472
    • (1981) J. Biochem. (Tokyo) , vol.89 , pp. 463-472
    • Kakutani, T.1    Watanabe, H.2    Arima, K.3    Beppu, T.4
  • 43
    • 0028958832 scopus 로고
    • Identification of interaction site of pseudoazurin with its redox partner, copper-containing nitrite reductase from Alcaligenes faecalis S-6
    • Kukimoto M., Nishiyama M., Ohnuki T., Turley S., Adman E.T., Horinouchi S., and Beppu T. Identification of interaction site of pseudoazurin with its redox partner, copper-containing nitrite reductase from Alcaligenes faecalis S-6. Protein Eng. 8 (1995) 153-158
    • (1995) Protein Eng. , vol.8 , pp. 153-158
    • Kukimoto, M.1    Nishiyama, M.2    Ohnuki, T.3    Turley, S.4    Adman, E.T.5    Horinouchi, S.6    Beppu, T.7
  • 44
    • 0029995615 scopus 로고    scopus 로고
    • Studies on protein-protein interaction between copper-containing nitrite reductase and pseudoazurin from Alcaligenes faecalis S-6
    • Kukimoto M., Nishiyama M., Tanokura M., Adman E.T., and Horinouchi S. Studies on protein-protein interaction between copper-containing nitrite reductase and pseudoazurin from Alcaligenes faecalis S-6. J. Biol. Chem. 271 (1996) 13680-13683
    • (1996) J. Biol. Chem. , vol.271 , pp. 13680-13683
    • Kukimoto, M.1    Nishiyama, M.2    Tanokura, M.3    Adman, E.T.4    Horinouchi, S.5
  • 45
    • 0028945240 scopus 로고
    • A quantitative test for copper using bicinchoninic acid
    • Brenner A.J., and Harris E.D. A quantitative test for copper using bicinchoninic acid. Anal. Biochem. 226 (1995) 80-84
    • (1995) Anal. Biochem. , vol.226 , pp. 80-84
    • Brenner, A.J.1    Harris, E.D.2
  • 46
    • 0018115502 scopus 로고
    • Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems
    • Dutton P.L.G. Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems. Methods Enzymol. 54 (1978) 411-435
    • (1978) Methods Enzymol. , vol.54 , pp. 411-435
    • Dutton, P.L.G.1
  • 47
    • 33646089555 scopus 로고    scopus 로고
    • Campbell, I. D. & Dwek, R. A. (1984). Scattering. In Biological Spectroscopy, p. 220, The Benjamin/Cummings Publishing Company, Inc., London, Amsterdam, Ontario, Sydney.
  • 49
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 50
    • 2442604589 scopus 로고    scopus 로고
    • Side-on copper-nitrosyl coordination by nitrite reductase
    • Tocheva E.I., Rosell F.I., Mauk A.G., and Murphy M.E.P. Side-on copper-nitrosyl coordination by nitrite reductase. Science 304 (2004) 867-870
    • (2004) Science , vol.304 , pp. 867-870
    • Tocheva, E.I.1    Rosell, F.I.2    Mauk, A.G.3    Murphy, M.E.P.4
  • 51
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallog. 53 (1997) 240-255
    • (1997) Acta Crystallog. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.2    Dodson, E.J.3
  • 52
    • 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. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26 (1993) 283-291
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 53
    • 33646109199 scopus 로고    scopus 로고
    • Fersht, A. (1985). Conformational change and allosteric regulation. In Enzyme Structure and Mechanism, p. 256, W.H. Freeman and Company, New York.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.