메뉴 건너뛰기




Volumn 45, Issue 14, 2006, Pages 4421-4428

Redox-dependent structural changes in the Azotobacter vinelandii bacterioferritin: New insights into the ferroxidase and iron transport mechanism

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; ENZYME KINETICS; IRON; REDOX REACTIONS; TRANSPORT PROPERTIES; X RAY ANALYSIS;

EID: 33645690696     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060146w     Document Type: Article
Times cited : (47)

References (40)
  • 1
    • 15244339209 scopus 로고    scopus 로고
    • Ferritins: Dynamic management of biological iron and oxygen chemistry
    • Liu, X., and Theil, E. C. (2005) Ferritins: Dynamic management of biological iron and oxygen chemistry, Acc. Chem. Res. 38, 167-75.
    • (2005) Acc. Chem. Res. , vol.38 , pp. 167-175
    • Liu, X.1    Theil, E.C.2
  • 2
    • 0038219647 scopus 로고    scopus 로고
    • Ferritins, iron uptake and storage from the bacterioferritin viewpoint
    • Carrondo, M. A. (2003) Ferritins, iron uptake and storage from the bacterioferritin viewpoint, EMBO J. 22, 1959-68.
    • (2003) EMBO J. , vol.22 , pp. 1959-1968
    • Carrondo, M.A.1
  • 4
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli
    • Zhao, G., Ceci, P., Ilari, A., Giangiacomo, L., Laue, T. M., Chiancone, E., and Chasteen, N. D. (2002) Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritin-like DNA-binding protein of Escherichia coli, J. Biol. Chem. 277, 27689-96.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6    Chasteen, N.D.7
  • 5
    • 0033986734 scopus 로고    scopus 로고
    • The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site
    • Ilari, A., Stefanini, S., Chiancone, E., and Tsernoglou, D. (2000) The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site, Nat. Struct. Biol. 7, 38-43.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 38-43
    • Ilari, A.1    Stefanini, S.2    Chiancone, E.3    Tsernoglou, D.4
  • 7
    • 0037805747 scopus 로고    scopus 로고
    • The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: X-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties
    • Ceci, P., Ilari, A., Falvo, E., and Chiancone, E. (2003) The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: X-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties. J. Biol. Chem. 278, 20319-26.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20319-20326
    • Ceci, P.1    Ilari, A.2    Falvo, E.3    Chiancone, E.4
  • 8
    • 11144328882 scopus 로고    scopus 로고
    • Contribution of the Helicobacter pylori thiol peroxidase bacterioferritin comigratory protein to oxidative stress resistance and host colonization
    • Wang, G., Olczak, A. A., Walton, J. P., and Maier, R. J. (2005) Contribution of the Helicobacter pylori thiol peroxidase bacterioferritin comigratory protein to oxidative stress resistance and host colonization, Infect. Immun. 73, 378-84.
    • (2005) Infect. Immun. , vol.73 , pp. 378-384
    • Wang, G.1    Olczak, A.A.2    Walton, J.P.3    Maier, R.J.4
  • 9
    • 0035190269 scopus 로고    scopus 로고
    • Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: A novel oxidative stress protection system
    • Lumppio, H. L., Shenvi, N. V., Summers, A. O., Voordouw, G., and Kurtz, D. M., Jr. (2001) Rubrerythrin and rubredoxin oxidoreductase in Desulfovibrio vulgaris: A novel oxidative stress protection system, J. Bacteriol. 183, 101-8.
    • (2001) J. Bacteriol. , vol.183 , pp. 101-108
    • Lumppio, H.L.1    Shenvi, N.V.2    Summers, A.O.3    Voordouw, G.4    Kurtz Jr., D.M.5
  • 10
    • 0033289110 scopus 로고    scopus 로고
    • Oxygen-carrying proteins: Three solutions to a common problem
    • Kurtz, D. M., Jr. (1999) Oxygen-carrying proteins: Three solutions to a common problem, Essays Biochem. 34, 85-100.
    • (1999) Essays Biochem. , vol.34 , pp. 85-100
    • Kurtz Jr., D.M.1
  • 11
    • 0027729455 scopus 로고
    • Formation of iron(III)-tyrosinate is the fastest reaction observed in ferritin
    • Waldo, G. S., and Theil, E. C. (1993) Formation of iron(III)-tyrosinate is the fastest reaction observed in ferritin, Biochemistry 32, 13262-9.
    • (1993) Biochemistry , vol.32 , pp. 13262-13269
    • Waldo, G.S.1    Theil, E.C.2
  • 12
    • 0027398912 scopus 로고
    • Formation of an Fe(III)-tyrosinate complex during biomineralization of H-subunit ferritin
    • Waldo, G. S., Ling, J., Sanders-Loehr, J., and Theil, E. C. (1993) Formation of an Fe(III)-tyrosinate complex during biomineralization of H-subunit ferritin, Science 259, 796-8.
    • (1993) Science , vol.259 , pp. 796-798
    • Waldo, G.S.1    Ling, J.2    Sanders-Loehr, J.3    Theil, E.C.4
  • 13
    • 0027522012 scopus 로고
    • Ferroxidase kinetics of human liver apoferritin, recombinant H-chain apoferritin, and site-directed mutants
    • Sun, S., Arosio, P., Levi, S., and Chasteen, N. D. (1993) Ferroxidase kinetics of human liver apoferritin, recombinant H-chain apoferritin, and site-directed mutants, Biochemistry 32, 9362-9.
    • (1993) Biochemistry , vol.32 , pp. 9362-9369
    • Sun, S.1    Arosio, P.2    Levi, S.3    Chasteen, N.D.4
  • 14
    • 0032493313 scopus 로고    scopus 로고
    • Reaction paths of iron oxidation and hydrolysis in horse spleen and recombinant human ferritins
    • Yang, X., Chen-Barrett, Y., Arosio, P., and Chasteen, N. D. (1998) Reaction paths of iron oxidation and hydrolysis in horse spleen and recombinant human ferritins, Biochemistry 37, 9743-50.
    • (1998) Biochemistry , vol.37 , pp. 9743-9750
    • Yang, X.1    Chen-Barrett, Y.2    Arosio, P.3    Chasteen, N.D.4
  • 16
    • 0025789986 scopus 로고
    • 2 stoichiometry during core formation
    • 2 stoichiometry during core formation, J. Biol. Chem. 266, 19965-70.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19965-19970
    • Xu, B.1    Chasteen, N.D.2
  • 17
    • 0034712683 scopus 로고    scopus 로고
    • The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin
    • Yang, X., Le Brun, N. E., Thomson, A. J., Moore, G. R., and Chasteen, N. D. (2000) The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin, Biochemistry 39, 4915-23.
    • (2000) Biochemistry , vol.39 , pp. 4915-4923
    • Yang, X.1    Le Brun, N.E.2    Thomson, A.J.3    Moore, G.R.4    Chasteen, N.D.5
  • 18
    • 0034254215 scopus 로고    scopus 로고
    • Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua
    • Yang, X., Chiancone, E., Stefanini, S., Ilari, A., and Chasteen, N. D. (2000) Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua, Biochem. J. 349 (Part 3), 783-6.
    • (2000) Biochem. J. , vol.349 , Issue.PART 3 , pp. 783-786
    • Yang, X.1    Chiancone, E.2    Stefanini, S.3    Ilari, A.4    Chasteen, N.D.5
  • 19
    • 0037020091 scopus 로고    scopus 로고
    • Iron detoxification properties of Escherichia coli bacterioferritin. Attenuation of oxyradical chemistry
    • Bou-Abdallah, F., Lewin, A. C., Le Brun, N. E., Moore, G. R., and Chasteen, N. D. (2002) Iron detoxification properties of Escherichia coli bacterioferritin. Attenuation of oxyradical chemistry, J. Biol. Chem. 277, 37064-9.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37064-37069
    • Bou-Abdallah, F.1    Lewin, A.C.2    Le Brun, N.E.3    Moore, G.R.4    Chasteen, N.D.5
  • 20
    • 0028467772 scopus 로고
    • Structure of a unique two-fold symmetric haem-bindinc site
    • Frolow, F., Kalb, A. J., and Yariv, J. (1994) Structure of a unique two-fold symmetric haem-bindinc site. Nat. Struct. Biol. 1, 453-60.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 453-460
    • Frolow, F.1    Kalb, A.J.2    Yariv, J.3
  • 22
    • 0036006679 scopus 로고    scopus 로고
    • The 2.6 Å resolution structure of Rhodobacter capsulatus bacterioferritin with metal-free dinuclear site and heme iron in a crystallographic 'special position'
    • Cobessi, D., Huang, L. S., Ban, M., Pon, N. G., Daldal, F., and Berry, E. A. (2002) The 2.6 Å resolution structure of Rhodobacter capsulatus bacterioferritin with metal-free dinuclear site and heme iron in a crystallographic 'special position', Acta Crystallogr. D58, 29-38.
    • (2002) Acta Crystallogr. , vol.D58 , pp. 29-38
    • Cobessi, D.1    Huang, L.S.2    Ban, M.3    Pon, N.G.4    Daldal, F.5    Berry, E.A.6
  • 24
    • 4344712784 scopus 로고    scopus 로고
    • 2.6 Å resolution crystal structure of the bacterioferritin from Azotobacter vinelandii
    • Liu, H. L., Zhou, H. N., Xing, W. M., Zhao, J. F., Li, S. X., Huang, J. F., and Bi, R. C. (2004) 2.6 Å resolution crystal structure of the bacterioferritin from Azotobacter vinelandii, FEBS Lett. 573, 93-8.
    • (2004) FEBS Lett. , vol.573 , pp. 93-98
    • Liu, H.L.1    Zhou, H.N.2    Xing, W.M.3    Zhao, J.F.4    Li, S.X.5    Huang, J.F.6    Bi, R.C.7
  • 25
    • 0028942712 scopus 로고
    • Recombinant Desulfovibrio vulgaris rubrerythrin. Isolation and characterization of the diiron domain
    • Gupta, N., Bonomi, F., Kurtz, D. M., Jr., Ravi, N., Wang, D. L., and Huynh, B. H. (1995) Recombinant Desulfovibrio vulgaris rubrerythrin. Isolation and characterization of the diiron domain, Biochemistry 34, 3310-8.
    • (1995) Biochemistry , vol.34 , pp. 3310-3318
    • Gupta, N.1    Bonomi, F.2    Kurtz Jr., D.M.3    Ravi, N.4    Wang, D.L.5    Huynh, B.H.6
  • 26
    • 0000865399 scopus 로고
    • Redox Properties and Mossbauer Spectroscopy of Azotobacter vinelandii bacterioferritin
    • Watt, G. D., Frankel, R. B., Papaefthymiou, G. C., Spartalian, K., and Stiefel, E. I. (1986) Redox Properties and Mossbauer Spectroscopy of Azotobacter vinelandii bacterioferritin, Biochemistry 25, 4330-6.
    • (1986) Biochemistry , vol.25 , pp. 4330-4336
    • Watt, G.D.1    Frankel, R.B.2    Papaefthymiou, G.C.3    Spartalian, K.4    Stiefel, E.I.5
  • 27
  • 28
    • 0033896691 scopus 로고    scopus 로고
    • Maximum-likelihood density modification
    • Terwilliger, T. C. (2000) Maximum-likelihood density modification, Acta Crystallogr. D56 (Part 8), 965-72.
    • (2000) Acta Crystallogr. , vol.D56 , Issue.PART 8 , pp. 965-972
    • Terwilliger, T.C.1
  • 29
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger, T. C., and Berendzen, J. (1999) Automated MAD and MIR structure solution, Acta Crystallogr. D55 (Part 4), 849-61.
    • (1999) Acta Crystallogr. , vol.D55 , Issue.PART 4 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 30
    • 0022325950 scopus 로고
    • Resolution of phase ambiguity in macromolecular crystallography
    • Wang, B. C. (1985) Resolution of phase ambiguity in macromolecular crystallography, Methods Enzymol. 115, 90-112.
    • (1985) Methods Enzymol. , vol.115 , pp. 90-112
    • Wang, B.C.1
  • 31
    • 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. A47 (Part 2), 110-9.
    • (1991) Acta Crystallogr. , vol.A47 , Issue.PART 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 34
    • 0035954391 scopus 로고    scopus 로고
    • "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites
    • Jin, W., Takagi, H., Pancorbo, B., and Theil, E. C. (2001) "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites, Biochemistry 40, 7525-32.
    • (2001) Biochemistry , vol.40 , pp. 7525-7532
    • Jin, W.1    Takagi, H.2    Pancorbo, B.3    Theil, E.C.4
  • 35
    • 0032563119 scopus 로고    scopus 로고
    • Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release?
    • Takagi, H., Shi, D., Ha, Y., Allewell, N. M., and Theil, E. C. (1998) Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release? J. Biol. Chem. 273, 18685-8.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18685-18688
    • Takagi, H.1    Shi, D.2    Ha, Y.3    Allewell, N.M.4    Theil, E.C.5
  • 36
    • 4644286770 scopus 로고    scopus 로고
    • Iron-oxo clusters biomineralizing on protein surfaces: Structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states
    • Zeth, K., Offermann, S., Essen, L. O., and Oesterhelt, D. (2004) Iron-oxo clusters biomineralizing on protein surfaces: Structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states, Proc. Natl. Acad. Sci. U.S.A. 101, 13780-5.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13780-13785
    • Zeth, K.1    Offermann, S.2    Essen, L.O.3    Oesterhelt, D.4
  • 37
    • 21544434658 scopus 로고    scopus 로고
    • High-resolution crystal structures of Desulfovibrio vulgaris (Hildenborough) nigerythrin: Facile, redox-dependent iron movement, domain interface variability, and peroxidase activity in the rubrerythrins
    • Iyer, R. B., Silaghi-Dumitrescu, R., Kurtz, D. M., Jr., and Lanzilotta, W. N. (2005) High-resolution crystal structures of Desulfovibrio vulgaris (Hildenborough) nigerythrin: Facile, redox-dependent iron movement, domain interface variability, and peroxidase activity in the rubrerythrins, J. Biol. Inorg. Chem. 10, 407-16.
    • (2005) J. Biol. Inorg. Chem. , vol.10 , pp. 407-416
    • Iyer, R.B.1    Silaghi-Dumitrescu, R.2    Kurtz Jr., D.M.3    Lanzilotta, W.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.