메뉴 건너뛰기




Volumn 27, Issue 3, 1997, Pages 385-394

The metal site of Pseudomonas aeruginosa azurin, revealed by a crystal structure determination of the Co(II) derivative and co-EPR spectroscopy

Author keywords

azurin; cobalt; EPR; Pseudomonas aeruginosa; x ray crystallography

Indexed keywords

AZURIN; BACTERIAL PROTEIN; COBALT; COPPER; NICKEL; ZINC;

EID: 1842376246     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199703)27:3<385::AID-PROT6>3.0.CO;2-C     Document Type: Article
Times cited : (52)

References (57)
  • 2
    • 0006487434 scopus 로고
    • Spectroscopic studies of ceruloplasmin: Electronic structures of the copper sites
    • Dawson, J.H., Dooley, D.M., Clark, R., Stephens, P.J., Gray, H.B. Spectroscopic studies of ceruloplasmin: Electronic structures of the copper sites. J. Am. Chem. Soc. 101:5046-5053, 1979.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 5046-5053
    • Dawson, J.H.1    Dooley, D.M.2    Clark, R.3    Stephens, P.J.4    Gray, H.B.5
  • 3
    • 0016861603 scopus 로고
    • Direct observation of sulfur coordination in bean plastocyanin by x-ray photoelectron spectroscopy
    • Solomon, E.I., Clendening, P.J., Gray, H.B. Direct observation of sulfur coordination in bean plastocyanin by x-ray photoelectron spectroscopy. J. Am. Chem. Soc. 97:3878-3879, 1975.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 3878-3879
    • Solomon, E.I.1    Clendening, P.J.2    Gray, H.B.3
  • 4
    • 0008121579 scopus 로고
    • Characterization of the blue copper site in oxidized azurin by extended x-ray absorption fine structure: Determination of a short Cu-S distance
    • Tullius, T.D., Frank, P., Hodgson, K.O. Characterization of the blue copper site in oxidized azurin by extended x-ray absorption fine structure: Determination of a short Cu-S distance. Proc. Natl. Acad. Sci. USA 75:4069-4073, 1978.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4069-4073
    • Tullius, T.D.1    Frank, P.2    Hodgson, K.O.3
  • 5
    • 0016686508 scopus 로고
    • The copper coordination group in "blue" copper proteins: Evidence from resonance raman spectra
    • Miskowski, V., Tang, S.-P.W., Spiro, T.G., Shapiro, E., Moss, T.H. The copper coordination group in "blue" copper proteins: Evidence from resonance raman spectra. Biochemistry 14:1244-1250, 1975.
    • (1975) Biochemistry , vol.14 , pp. 1244-1250
    • Miskowski, V.1    Tang, S.-P.W.2    Spiro, T.G.3    Shapiro, E.4    Moss, T.H.5
  • 6
    • 0017297879 scopus 로고
    • Resonance raman spectra of "blue" copper proteins and the nature of their copper sites
    • Siiman, O., Young, N.M., Carey, P.R. Resonance raman spectra of "blue" copper proteins and the nature of their copper sites. J. Am. Chem. Soc. 98:744-748, 1976.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 744-748
    • Siiman, O.1    Young, N.M.2    Carey, P.R.3
  • 9
    • 0021104996 scopus 로고
    • Structure of oxidized poplar plastocyanin at 1.6 Å resolution
    • Guss, J.M., Freeman, H.C. Structure of oxidized poplar plastocyanin at 1.6 Å resolution. J. Mol. Biol. 169:521-563, 1983.
    • (1983) J. Mol. Biol. , vol.169 , pp. 521-563
    • Guss, J.M.1    Freeman, H.C.2
  • 10
    • 0001743579 scopus 로고
    • Blue copper proteins: The copper site in azurin from Alcaligenes denitrifcans
    • Norris, G.E., Anderson, B.F., Baker, E.N. Blue copper proteins: The copper site in azurin from Alcaligenes denitrifcans. J. Am. Chem. Soc. 108:2784-2785, 1986.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 2784-2785
    • Norris, G.E.1    Anderson, B.F.2    Baker, E.N.3
  • 11
    • 33745343303 scopus 로고
    • Structural features of azurin at 2.7 Å resolution
    • Adman, E.T., Jensen, L.H. Structural features of azurin at 2.7 Å resolution. Isr. J. Chem. 21:8-12, 1981.
    • (1981) Isr. J. Chem. , vol.21 , pp. 8-12
    • Adman, E.T.1    Jensen, L.H.2
  • 12
    • 0025953438 scopus 로고
    • Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and 9.0
    • Nar, H., Messerschmidt, A., Huber, R., van de Kamp, M., Canters, G.W. Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and 9.0. J. Mol. Biol. 221:765-772, 1991.
    • (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
  • 13
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P.J.J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946-950, 1991.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.J.1
  • 14
    • 4243375336 scopus 로고
    • On the relationship between protein-forced ligand fields and the properties of blue copper centers
    • Gray, H.B., Malmström, B.G. On the relationship between protein-forced ligand fields and the properties of blue copper centers. Comments Inorg. Chem. 2:203-209, 1983.
    • (1983) Comments Inorg. Chem. , vol.2 , pp. 203-209
    • Gray, H.B.1    Malmström, B.G.2
  • 17
    • 0014251790 scopus 로고
    • Metalloenzymes: The entatic nature of their active sites
    • Vallee, B.L., Williams, R.J.P. Metalloenzymes: The entatic nature of their active sites. Proc. Natl. Acad. Sci. USA 59:498-505, 1968.
    • (1968) Proc. Natl. Acad. Sci. USA , vol.59 , pp. 498-505
    • Vallee, B.L.1    Williams, R.J.P.2
  • 19
    • 0018225148 scopus 로고
    • Newly synthesized sulfhydryl- and imidazol-containing tripeptides with a specific copper-binding site
    • Sugiura, Y. Newly synthesized sulfhydryl- and imidazol-containing tripeptides with a specific copper-binding site. Inorg. Chem. 17:2176-2182, 1978.
    • (1978) Inorg. Chem. , vol.17 , pp. 2176-2182
    • Sugiura, Y.1
  • 20
    • 0025126890 scopus 로고
    • Tetrahedral copper(II) complexes supported by a hindered pyrazolylborate: Formation of the thiolato complex, which closely mimics the spectroscopic characteristics of blue copper proteins
    • Kitajima, N., Fujisawa, K., Moro-oka, Y. Tetrahedral copper(II) complexes supported by a hindered pyrazolylborate: Formation of the thiolato complex, which closely mimics the spectroscopic characteristics of blue copper proteins. J. Am. Chem. Soc. 112:3210-3212, 1990.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 3210-3212
    • Kitajima, N.1    Fujisawa, K.2    Moro-oka, Y.3
  • 21
    • 33749413911 scopus 로고
    • Synthetic approach to the structure and function of copper proteins
    • Kitajima, N. Synthetic approach to the structure and function of copper proteins. Adv. Inorg. Chem. 39:1-7, 1992.
    • (1992) Adv. Inorg. Chem. , vol.39 , pp. 1-7
    • Kitajima, N.1
  • 22
    • 0007313183 scopus 로고
    • Preparation and spectroscopic studies of cobalt(II)-stellacyanin
    • McMillin, D.R., Holwerda, R.A., Gray, H.B. Preparation and spectroscopic studies of cobalt(II)-stellacyanin. Proc. Natl. Acad. Sci. USA 71:1339-1341, 1974.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1339-1341
    • McMillin, D.R.1    Holwerda, R.A.2    Gray, H.B.3
  • 23
    • 0016361758 scopus 로고
    • Preparation and spectroscopic studies of cobalt(II) derivates of blue copper proteins
    • McMillin, D.R., Rosenberg, R.C., Gray, H.B. Preparation and spectroscopic studies of cobalt(II) derivates of blue copper proteins. Proc. Natl. Acad. Sci. USA 71:4760-4762, 1974.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4760-4762
    • McMillin, D.R.1    Rosenberg, R.C.2    Gray, H.B.3
  • 24
    • 0028980934 scopus 로고
    • 1H-NMR study of a cobalt-substituted blue copper protein: Pseudomonas aeruginosa Co(II)-azurin
    • 1H-NMR study of a cobalt-substituted blue copper protein: Pseudomonas aeruginosa Co(II)-azurin. Eur. J. Biochem. 231:358-369, 1995.
    • (1995) Eur. J. Biochem. , vol.231 , pp. 358-369
    • Salgado, J.1    Jiménez, H.R.2    Donaire, A.3    Moratal, J.M.4
  • 26
    • 33845560348 scopus 로고
    • A detailed analysis of the charge-transfer bands of a blue copper protein: Studies of the nickel(II), manganese(II), and cobalt(II) derivates of azurin
    • Tennent, D.L., McMillin, D.R. A detailed analysis of the charge-transfer bands of a blue copper protein: Studies of the nickel(II), manganese(II), and cobalt(II) derivates of azurin. J. Am. Chem. Soc. 101:2307-2311, 1979.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 2307-2311
    • Tennent, D.L.1    McMillin, D.R.2
  • 27
    • 84908717417 scopus 로고
    • Electronic spectroscopic studies of Ni(II)-substituted blue copper proteins
    • Lum, V., Gray, H.B. Electronic spectroscopic studies of Ni(II)-substituted blue copper proteins. Isr. J. Chem. 21:23-25, 1981.
    • (1981) Isr. J. Chem. , vol.21 , pp. 23-25
    • Lum, V.1    Gray, H.B.2
  • 28
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry, R., Eyring, H. Conformation changes of proteins. J. Phys. Chem. 58:110-120, 1954.
    • (1954) J. Phys. Chem. , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 29
    • 0000191704 scopus 로고
    • Metal binding and catalytic activity in bovine carbonic anhydrase
    • Lindskog, R., Malmström, B.G. Metal binding and catalytic activity in bovine carbonic anhydrase. J. Biol. Chem. 237:1129-1137, 1962.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1129-1137
    • Lindskog, R.1    Malmström, B.G.2
  • 30
    • 0027998885 scopus 로고
    • Rack-induced bonding in blue-copper proteins
    • Malmström, B.G. Rack-induced bonding in blue-copper proteins. Eur. J. Biochem. 223:711-718, 1994.
    • (1994) Eur. J. Biochem. , vol.223 , pp. 711-718
    • Malmström, B.G.1
  • 32
    • 0000140532 scopus 로고
    • Connection between structure, electronic spectrum, and electron-transfer properties of blue copper proteins
    • Larsson, S., Broo, A., Sjölin, L. Connection between structure, electronic spectrum, and electron-transfer properties of blue copper proteins. J. Phys. Chem. 99:4860-4865, 1995.
    • (1995) J. Phys. Chem. , vol.99 , pp. 4860-4865
    • Larsson, S.1    Broo, A.2    Sjölin, L.3
  • 33
    • 0026557819 scopus 로고
    • Characterization and crystal structure of zinc azurin, a by-product of heterologous expression in Escherichia coli of Pseudomonas aeruginosa copper azurin
    • Nar, H., Huber, R., Messerschmidt, A., Filipou, A.C., Barth, M., Jaquinod, M., van de Kamp, M., Canters, G.W. Characterization and crystal structure of zinc azurin, a by-product of heterologous expression in Escherichia coli of Pseudomonas aeruginosa copper azurin. Eur. J. Biochem. 205:1123-1129, 1992.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 1123-1129
    • Nar, H.1    Huber, R.2    Messerschmidt, A.3    Filipou, A.C.4    Barth, M.5    Jaquinod, M.6    Van De Kamp, M.7    Canters, G.W.8
  • 37
    • 0024517882 scopus 로고
    • The azurin gene from Pseudomonas aeruginosa: Cloning and characterization
    • Arviddsson, R.H.A., Nordling, M., Lundberg, L.G. The azurin gene from Pseudomonas aeruginosa: Cloning and characterization. Eur. J. Biochem. 179:195-200, 1989.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 195-200
    • Arviddsson, R.H.A.1    Nordling, M.2    Lundberg, L.G.3
  • 38
    • 0024511736 scopus 로고
    • Expression of the blue copper protein azurin from Pseudomonas aeruginosa in Escherichia coli
    • Karlsson, B.C., Pascher, T., Nordling, M., Arvidsson, R.H.A., Lundberg, L.G. Expression of the blue copper protein azurin from Pseudomonas aeruginosa in Escherichia coli. FEBS Lett. 246:211-217, 1989.
    • (1989) FEBS Lett. , vol.246 , pp. 211-217
    • Karlsson, B.C.1    Pascher, T.2    Nordling, M.3    Arvidsson, R.H.A.4    Lundberg, L.G.5
  • 40
    • 1842349349 scopus 로고    scopus 로고
    • SMART SIA, Madison, Wisconsin, 1994
    • SMART SIA, Madison, Wisconsin, 1994.
  • 41
  • 42
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones, T.A. A graphics model building and refinement system for macromolecules. J. Appl. Crystallogr. 11:268-272, 1978.
    • (1978) J. Appl. Crystallogr. , vol.11 , pp. 268-272
    • Jones, T.A.1
  • 43
    • 0024293340 scopus 로고
    • Structure of azurin from Alcaligenes denitrifcans refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules
    • Baker, E.N. Structure of azurin from Alcaligenes denitrifcans refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules. J. Mol. Biol. 203:1071-1095, 1988.
    • (1988) J. Mol. Biol. , vol.203 , pp. 1071-1095
    • Baker, E.N.1
  • 46
    • 0008434175 scopus 로고
    • Electronic absorption spectra of M(II) (Met121X) azurins (M = Co, Ni, Cu; X = Leu, Gly, Asp, Glu): Charge transfer energies and reduction potentials
    • Di Bilio, A.J., Chang, T.K., Gray, H.G., Karlsson, B.C., Nordling, M., Pascher, T., Lundberg, L.G. Electronic absorption spectra of M(II) (Met121X) azurins (M = Co, Ni, Cu; X = Leu, Gly, Asp, Glu): Charge transfer energies and reduction potentials. Inorg. Chim. Acta 198:145-149, 1992.
    • (1992) Inorg. Chim. Acta , vol.198 , pp. 145-149
    • Di Bilio, A.J.1    Chang, T.K.2    Gray, H.G.3    Karlsson, B.C.4    Nordling, M.5    Pascher, T.6    Lundberg, L.G.7
  • 47
    • 0000595820 scopus 로고
    • Magnetic circular dichroism and electron paramagnetic resonance studies of cobalt-substituted horse liver alcohol dehydrogenase
    • Werth, M.T., Tang, S.-F., Formicka, G., Zeppezauer, M., Johnson, M.K. Magnetic circular dichroism and electron paramagnetic resonance studies of cobalt-substituted horse liver alcohol dehydrogenase. Inorg. Chem. 34:218-228, 1995.
    • (1995) Inorg. Chem. , vol.34 , pp. 218-228
    • Werth, M.T.1    Tang, S.-F.2    Formicka, G.3    Zeppezauer, M.4    Johnson, M.K.5
  • 48
    • 2542494507 scopus 로고    scopus 로고
    • EPR and magnetic susceptibility studies of cobalt(II) and nickel(II)-substituted azurins from Pseudomonas aeruginosa: Electronic structure of the active sites
    • Jiménez, H.R., Salgado, J., Moratal, J.M., Morgenstern-Badarau, I. EPR and magnetic susceptibility studies of cobalt(II) and nickel(II)-substituted azurins from Pseudomonas aeruginosa: Electronic structure of the active sites. Inorg. Chem. 35:2737-2741, 1996.
    • (1996) Inorg. Chem. , vol.35 , pp. 2737-2741
    • Jiménez, H.R.1    Salgado, J.2    Moratal, J.M.3    Morgenstern-Badarau, I.4
  • 49
    • 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 and Asp) mutants
    • Bonander, N., Karlsson, E.G., Vänngård, T. Environment of copper in Pseudomonas aeruginosa azurin probed by binding of exogenous ligands to Met121X (X = Gly, Ala, Val, Leu and Asp) mutants. Biochemistry 35:2429-2436, 1996.
    • (1996) Biochemistry , vol.35 , pp. 2429-2436
    • Bonander, N.1    Karlsson, E.G.2    Vänngård, T.3
  • 50
    • 0030512439 scopus 로고    scopus 로고
    • Mutant Met121Ala of Pseudomonas aeruginosa azurin and its azide derivative crystal structures and spectral properties
    • Tsai, L.-C., Bonander, N., Harata, K., Karlsson, B.G., Vänngård, T., Langer, V., Sjölin, L. Mutant Met121Ala of Pseudomonas aeruginosa azurin and its azide derivative crystal structures and spectral properties. Acta Crystallogr. 052:952-958, 1996.
    • (1996) Acta Crystallogr. , vol.52 , pp. 952-958
    • Tsai, L.-C.1    Bonander, N.2    Harata, K.3    Karlsson, B.G.4    Vänngård, T.5    Langer, V.6    Sjölin, L.7
  • 52
    • 0017301812 scopus 로고
    • Infrared and visible circular dichroism and magnetic circular dichroism studies on cobalt(II)-substituted blue copper proteins
    • Solomon, E.I., Rawlings, J., McMillin, D.R., Stephens, P.J., Gray, H.B. Infrared and visible circular dichroism and magnetic circular dichroism studies on cobalt(II)-substituted blue copper proteins. J. Am. Chem. Soc. 98:8046-8048, 1976.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 8046-8048
    • Solomon, E.I.1    Rawlings, J.2    McMillin, D.R.3    Stephens, P.J.4    Gray, H.B.5
  • 53
    • 0008876117 scopus 로고
    • ESR spectra of low-symmetry high-spin cobalt(II) complexes. 2. Pseudotetrahedral dichlorobis(triphenylphosphine oxide) cobalt(II)
    • Bencini, A., Benelli, D., Gatteschi, D., Zanchini, C. ESR spectra of low-symmetry high-spin cobalt(II) complexes. 2. Pseudotetrahedral dichlorobis(triphenylphosphine oxide) cobalt(II). Inorg. Chem. 18:2137-2140, 1979.
    • (1979) Inorg. Chem. , vol.18 , pp. 2137-2140
    • Bencini, A.1    Benelli, D.2    Gatteschi, D.3    Zanchini, C.4
  • 55
    • 0024503685 scopus 로고
    • Characterization of the inhibitor complexes of cobalt carboxypeptidase A by electron paramagnetic resonance spectroscopy
    • Martinelli, R.A., Hanson, G.R., Thompson, J.S., Holmquist, B., Pilbrow, J.R., Auld, D.S., Vallee, B.L. Characterization of the inhibitor complexes of cobalt carboxypeptidase A by electron paramagnetic resonance spectroscopy. Biochemistry 28:2251-2258, 1989.
    • (1989) Biochemistry , vol.28 , pp. 2251-2258
    • Martinelli, R.A.1    Hanson, G.R.2    Thompson, J.S.3    Holmquist, B.4    Pilbrow, J.R.5    Auld, D.S.6    Vallee, B.L.7
  • 57
    • 0001000248 scopus 로고
    • Axial ligand bonding in blue copper proteins
    • Lowery, M.D., Solomon, E.I. Axial ligand bonding in blue copper proteins. Inorg. Chim. Acta. 198-200:233-243, 1992.
    • (1992) Inorg. Chim. Acta , vol.198-200 , pp. 233-243
    • Lowery, M.D.1    Solomon, E.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.