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Volumn 1794, Issue 7, 2009, Pages 995-1000

Active site loop dictates the thermodynamics of reduction and ligand protonation in cupredoxins

Author keywords

Conformational transition; Cupredoxin; Electrochemistry; Electron transfer; Reduction potential; Thermodynamic parameters

Indexed keywords

AMICYANIN; AZURIN; COPPER; COPPER PROTEIN; CYSTEINE; HISTIDINE; METHIONINE; PLASTOCYANIN; PROTON; SCAFFOLD PROTEIN;

EID: 67349108661     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.02.001     Document Type: Article
Times cited : (7)

References (39)
  • 1
    • 0542365212 scopus 로고
    • Active-site properties of the blue copper proteins
    • Sykes A.G. Active-site properties of the blue copper proteins. Adv. Inorg. Chem. 36 (1991) 377-408
    • (1991) Adv. Inorg. Chem. , vol.36 , pp. 377-408
    • Sykes, A.G.1
  • 2
    • 0001826594 scopus 로고    scopus 로고
    • Metal sites in small blue copper proteins, blue copper oxidases and vanadium-containing enzymes
    • Messerschmidt A. Metal sites in small blue copper proteins, blue copper oxidases and vanadium-containing enzymes. Struct. Bond. 90 (1998) 37-68
    • (1998) Struct. Bond. , vol.90 , pp. 37-68
    • Messerschmidt, A.1
  • 3
    • 0026411154 scopus 로고
    • Copper protein structures
    • Adman E.T. Copper protein structures. Adv. Protein Chem. 42 (1991) 145-197
    • (1991) Adv. Protein Chem. , vol.42 , pp. 145-197
    • Adman, E.T.1
  • 4
    • 27844457050 scopus 로고    scopus 로고
    • Investigating the structure and function of cupredoxins
    • Dennison C. Investigating the structure and function of cupredoxins. Coord. Chem. Rev. 249 (2005) 3025-3054
    • (2005) Coord. Chem. Rev. , vol.249 , pp. 3025-3054
    • Dennison, C.1
  • 7
    • 38849140251 scopus 로고    scopus 로고
    • The role of ligand-containing loops at copper sites in proteins
    • Dennison C. The role of ligand-containing loops at copper sites in proteins. Nat. Prod. Rep. 25 (2008) 15-24
    • (2008) Nat. Prod. Rep. , vol.25 , pp. 15-24
    • Dennison, C.1
  • 8
    • 0036185564 scopus 로고    scopus 로고
    • An outer-sphere hydrogen-bond network constrains copper coordination in blue proteins
    • Machczynski C.M., Gray H.B., and Richards J.H. An outer-sphere hydrogen-bond network constrains copper coordination in blue proteins. J. Inorg. Biochem. 88 (2002) 375-380
    • (2002) J. Inorg. Biochem. , vol.88 , pp. 375-380
    • Machczynski, C.M.1    Gray, H.B.2    Richards, J.H.3
  • 10
    • 0028236692 scopus 로고
    • The crystal structures of reduced pseudoazurin from Alcaligenes faecalis S-6 at two pH values
    • Vakoufari E., Wilson K.S., and Petratos K. The crystal structures of reduced pseudoazurin from Alcaligenes faecalis S-6 at two pH values. FEBS Lett. 347 (1994) 203-206
    • (1994) FEBS Lett. , vol.347 , pp. 203-206
    • Vakoufari, E.1    Wilson, K.S.2    Petratos, K.3
  • 12
    • 0039521296 scopus 로고
    • Reversible active site protonation and electron-transfer properties of Achromobacter cycloclastes pseudoazurin: comparisons with other type 1 copper proteins
    • Dennison C., Kohzuma T., McFarlane W., Suzuki S., and Sykes A.G. Reversible active site protonation and electron-transfer properties of Achromobacter cycloclastes pseudoazurin: comparisons with other type 1 copper proteins. Chem. Commun. (1994) 581-582
    • (1994) Chem. Commun. , pp. 581-582
    • Dennison, C.1    Kohzuma, T.2    McFarlane, W.3    Suzuki, S.4    Sykes, A.G.5
  • 13
    • 0034043603 scopus 로고    scopus 로고
    • Protonation of the copper(I) form of the blue copper proteins plastocyanin and amicyanin - a molecular dynamics study
    • Buning C., and Comba P. Protonation of the copper(I) form of the blue copper proteins plastocyanin and amicyanin - a molecular dynamics study. Eur. J. Inorg. Chem. (2000) 1267-1273
    • (2000) Eur. J. Inorg. Chem. , pp. 1267-1273
    • Buning, C.1    Comba, P.2
  • 14
    • 37249081125 scopus 로고    scopus 로고
    • Kinetics and mechanism of the acid transition of the active site in plastocyanin
    • Hass M.A.S., Christensen H.E.M., Zhang J., and Led J.J. Kinetics and mechanism of the acid transition of the active site in plastocyanin. Biochemistry 46 (2007) 14619-14628
    • (2007) Biochemistry , vol.46 , pp. 14619-14628
    • Hass, M.A.S.1    Christensen, H.E.M.2    Zhang, J.3    Led, J.J.4
  • 15
    • 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
  • 18
    • 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.Ph., Camba R., McEvoy J.P., Armstrong F.A., 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.Ph.3    Camba, R.4    McEvoy, J.P.5    Armstrong, F.A.6    Canters, G.W.7
  • 19
    • 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.W., Durley R.C.E., Mathews F.S., and Davidson V.L. Molecular basis for interprotein complex-dependent effects on the redox properties of amicyanin. Biochemistry 37 (1998) 17128-17136
    • (1998) Biochemistry , vol.37 , pp. 17128-17136
    • Zhu, Z.1    Cunane, L.M.2    Chen, Z.W.3    Durley, R.C.E.4    Mathews, F.S.5    Davidson, V.L.6
  • 20
    • 0002426686 scopus 로고
    • Electron transfer in "blue" copper proteins
    • Freeman H.C. Electron transfer in "blue" copper proteins. Coord. Chem. 21 (1981) 29-51
    • (1981) Coord. Chem. , vol.21 , pp. 29-51
    • Freeman, H.C.1
  • 21
    • 10044272401 scopus 로고    scopus 로고
    • Loop-contraction mutagenesis of type 1 copper sites
    • Yanagisawa S., and Dennison C. Loop-contraction mutagenesis of type 1 copper sites. J. Am Chem. Soc. 126 (2004) 15711-15719
    • (2004) J. Am Chem. Soc. , vol.126 , pp. 15711-15719
    • Yanagisawa, S.1    Dennison, C.2
  • 23
    • 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. Engineering copper sites in proteins: loops confer native structures and properties to chimeric cupredoxins. J. Am. Chem. Soc. 129 (2007) 709-718
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 709-718
    • Li, C.1    Banfield, M.J.2    Dennison, C.3
  • 24
    • 53849105752 scopus 로고    scopus 로고
    • The importance of the long type 1 copper-binding loop of nitrite reductase for structure and function
    • Sato K., Firbank S.J., Li C., Banfield M.J., and Dennison C. The importance of the long type 1 copper-binding loop of nitrite reductase for structure and function. Chem. Eur. J. 14 (2008) 5820-5828
    • (2008) Chem. Eur. J. , vol.14 , pp. 5820-5828
    • Sato, K.1    Firbank, S.J.2    Li, C.3    Banfield, M.J.4    Dennison, C.5
  • 25
    • 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.J.C., Melter M., and Sanders-Loehr J. 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 (2000) 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.J.C.5    Melter, M.6    Sanders-Loehr, J.7
  • 26
    • 0034856809 scopus 로고    scopus 로고
    • An amicyanin C-terminal loop mutant where the active-site histidine donor cannot be protonated
    • Remenyi R., Jeuken L.J.C., Comba P., and Canters G.W. An amicyanin C-terminal loop mutant where the active-site histidine donor cannot be protonated. J. Biol. Inorg. Chem. 6 (2001) 23-26
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 23-26
    • Remenyi, R.1    Jeuken, L.J.C.2    Comba, P.3    Canters, G.W.4
  • 29
    • 0035849513 scopus 로고    scopus 로고
    • Enthalpic and entropic contributions to the mutational changes in the reduction potential of azurin
    • Battistuzzi G., Borsari M., Canters G.W., de Waal E., Loschi L., Warmerdam G., and Sola M. Enthalpic and entropic contributions to the mutational changes in the reduction potential of azurin. Biochemistry 40 (2001) 6707-6712
    • (2001) Biochemistry , vol.40 , pp. 6707-6712
    • Battistuzzi, G.1    Borsari, M.2    Canters, G.W.3    de Waal, E.4    Loschi, L.5    Warmerdam, G.6    Sola, M.7
  • 30
    • 0043166970 scopus 로고    scopus 로고
    • Control of metalloprotein reduction potential: compensation phenomena in the reduction thermodynamics of blue copper proteins
    • Battistuzzi G., Bellei M., Borsari M., Canters G.W., de Waal E., Jeuken L.J.C., Ranieri A., and Sola M. Control of metalloprotein reduction potential: compensation phenomena in the reduction thermodynamics of blue copper proteins. Biochemistry 42 (2003) 9214-9220
    • (2003) Biochemistry , vol.42 , pp. 9214-9220
    • Battistuzzi, G.1    Bellei, M.2    Borsari, M.3    Canters, G.W.4    de Waal, E.5    Jeuken, L.J.C.6    Ranieri, A.7    Sola, M.8
  • 32
    • 0025953438 scopus 로고
    • Crystal structure analysis of oxidised Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0
    • Nar H., Messerschmidt A., Huber R., van de Kamp M., and Canters G.W. Crystal structure analysis of oxidised Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. J. Mol. Biol. 221 (1991) 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
  • 33
    • 33845560299 scopus 로고
    • A survey of ligand effects upon the reaction entropies of some transition metal redox couples
    • Yee E.L., Cave R.J., Guyer K.L., Tyma P.D., and Weaver M.J. A survey of ligand effects upon the reaction entropies of some transition metal redox couples. J. Am. Chem. Soc. 101 (1979) 1131-1137
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 1131-1137
    • Yee, E.L.1    Cave, R.J.2    Guyer, K.L.3    Tyma, P.D.4    Weaver, M.J.5
  • 34
    • 0001218042 scopus 로고
    • Functional dependence upon ligand composition of the reaction entropies for some transition-metal redox couples containing mixed ligands
    • Yee E.L., and Weaver M.J. Functional dependence upon ligand composition of the reaction entropies for some transition-metal redox couples containing mixed ligands. Inorg. Chem. 19 (1980) 1077-1079
    • (1980) Inorg. Chem. , vol.19 , pp. 1077-1079
    • Yee, E.L.1    Weaver, M.J.2
  • 35
    • 0001049649 scopus 로고
    • Temperature and electrolyte effects on the electron-transfer reactions of cytochrome c
    • Koller K.B., and Hawkridge F.M. Temperature and electrolyte effects on the electron-transfer reactions of cytochrome c. J. Am. Chem. Soc. 107 (1985) 7412-7417
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 7412-7417
    • Koller, K.B.1    Hawkridge, F.M.2
  • 37
    • 0000357971 scopus 로고
    • Spectroelectrochemistry of blue copper proteins: pH and temperature dependences of the reduction potentials of five azurins
    • St. Clair C., Ellis W.R., and Gray H.B. Spectroelectrochemistry of blue copper proteins: pH and temperature dependences of the reduction potentials of five azurins. Inorg. Chim. Acta 191 (1992) 149-155
    • (1992) Inorg. Chim. Acta , vol.191 , pp. 149-155
    • St. Clair, C.1    Ellis, W.R.2    Gray, H.B.3
  • 38
    • 29144505214 scopus 로고    scopus 로고
    • Modulation of the free energy of reduction in metalloproteins
    • Sola M., Battistuzzi G., and Borsari M. Modulation of the free energy of reduction in metalloproteins. Chemtracts 18 (2005) 73-86
    • (2005) Chemtracts , vol.18 , pp. 73-86
    • Sola, M.1    Battistuzzi, G.2    Borsari, M.3
  • 39
    • 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., and Warshel A. Frozen density functional free energy simulations of redox proteins: computational studies of the reduction potential of plastocyanin and rusticyanin. J. Am. Chem. Soc. 125 (2003) 5025-5039
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5025-5039
    • Olsson, M.H.M.1    Hong, G.2    Warshel, A.3


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