메뉴 건너뛰기




Volumn 22, Issue 9, 2003, Pages 1959-1968

Ferritins, iron uptake and storage from the bacterioferritin viewpoint

Author keywords

Bacterioferritins; Ferroxidase activity; Iron storage; Native di iron centres; Specific iron channel

Indexed keywords

BACTERIOFERRITIN; CERULOPLASMIN; FERRITIN; FERROUS ION; HEME; ION CHANNEL; IRON; OXYGEN; PROTEIN SUBUNIT; RADICAL; TYROSINE; UNCLASSIFIED DRUG;

EID: 0038219647     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg215     Document Type: Review
Times cited : (243)

References (60)
  • 1
    • 0031763106 scopus 로고    scopus 로고
    • Iron storage in bacteria
    • Andrews, S.C. (1998) Iron storage in bacteria. Adv. Microb. Physiol., 40, 281-351.
    • (1998) Adv. Microb. Physiol. , vol.40 , pp. 281-351
    • Andrews, S.C.1
  • 2
    • 0037101879 scopus 로고    scopus 로고
    • Ferritin, iron homeostasis, and oxidative damage
    • Arosio, P. and Levi, S. (2002) Ferritin, iron homeostasis, and oxidative damage. Free Rad. Biol. Med., 33, 457-463.
    • (2002) Free Rad. Biol. Med. , vol.33 , pp. 457-463
    • Arosio, P.1    Levi, S.2
  • 3
    • 0017803865 scopus 로고
    • Electron density map of apoferritin at 2.8 A resolution
    • Banyard, S.H., Stammers, D.K. and Harrison, P.M. (1978) Electron density map of apoferritin at 2.8 A resolution. Nature, 271, 282-284.
    • (1978) Nature , vol.271 , pp. 282-284
    • Banyard, S.H.1    Stammers, D.K.2    Harrison, P.M.3
  • 4
    • 84957665033 scopus 로고    scopus 로고
    • An object-oriented programming suite for electrostatic effects in biological molecules
    • Springer, Berlin, Germany
    • Bashford, D. (1997) An object-oriented programming suite for electrostatic effects in biological molecules. In Scientific Computing in Object-Oriented Parallel Environments. Vol. 1343. Springer, Berlin, Germany, pp. 233-240.
    • (1997) Scientific Computing in Object-Oriented Parallel Environments , vol.1343 , pp. 233-240
    • Bashford, D.1
  • 5
    • 0027748181 scopus 로고
    • Iron (II) oxidation and early intermediates of iron-core formation in recombinant human H-chain ferritin
    • Bauminger, E.R., Harrison, P.M., Hechel, D., Hodson, N.W., Nowik, I., Treffry, A. and Yewdall, S.J. (1993) Iron (II) oxidation and early intermediates of iron-core formation in recombinant human H-chain ferritin. Biochem. J., 296, 709-719.
    • (1993) Biochem. J. , vol.296 , pp. 709-719
    • Bauminger, E.R.1    Harrison, P.M.2    Hechel, D.3    Hodson, N.W.4    Nowik, I.5    Treffry, A.6    Yewdall, S.J.7
  • 6
    • 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, 37064-37069.
    • (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
  • 7
    • 0033617958 scopus 로고    scopus 로고
    • Mineralization in ferritin: An efficient means of iron storage
    • Chasteen, N.D. and Harrison, P.M. (1999) Mineralization in ferritin: an efficient means of iron storage. J. Struct. Biol., 126, 182-194.
    • (1999) J. Struct. Biol. , vol.126 , pp. 182-194
    • Chasteen, N.D.1    Harrison, P.M.2
  • 8
    • 0036006679 scopus 로고    scopus 로고
    • The 2.6 A 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 A resolution structure of Rhodobacter capsulatus bacterioferritin with metal-free dinuclear site and heme iron in a crystallographic 'special position'. Acta Crystallogr. D, 58, 29-38.
    • (2002) Acta Crystallogr. D , vol.58 , pp. 29-38
    • Cobessi, D.1    Huang, L.S.2    Ban, M.3    Pon, N.G.4    Daldal, F.5    Berry, E.A.6
  • 10
    • 0017823433 scopus 로고
    • Novel mechanism for ferritin iron oxidation and deposition
    • Crichton, R.R. and Roman, F. (1978) Novel mechanism for ferritin iron oxidation and deposition. J. Mol. Catal., 4, 75-82.
    • (1978) J. Mol. Catal. , vol.4 , pp. 75-82
    • Crichton, R.R.1    Roman, F.2
  • 12
    • 0029949340 scopus 로고    scopus 로고
    • The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains
    • DeMaré, F., Kurtz, D.M. and Nordlund, P. (1996) The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains. Nat. Struct. Biol., 3, 539-546.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 539-546
    • DeMaré, F.1    Kurtz, D.M.2    Nordlund, P.3
  • 13
    • 0031808808 scopus 로고    scopus 로고
    • Calculated electrostatic gradients in recombinant human H-chain ferritin
    • Douglas, T. and Ripoll, D.R. (1998) Calculated electrostatic gradients in recombinant human H-chain ferritin. Protein Sci., 7, 1083-1091.
    • (1998) Protein Sci. , vol.7 , pp. 1083-1091
    • Douglas, T.1    Ripoll, D.R.2
  • 14
    • 0033767236 scopus 로고    scopus 로고
    • Structure of a dioxygen reduction enzyme from Desulfovibrio gigas
    • Frazão, C. et al. (2000) Structure of a dioxygen reduction enzyme from Desulfovibrio gigas. Nat. Struct. Biol., 7, 1041-1045.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1041-1045
    • Frazão, C.1
  • 15
    • 0004152433 scopus 로고    scopus 로고
    • 1 - Bacterioferritin
    • Messerschmidt, A.H.R., Poulos, K. and Weighardt, K. (eds). Wiley, Chichester, UK
    • 1 - bacterioferritin. In Messerschmidt, A.H.R., Poulos, K. and Weighardt, K. (eds), Handbook of Metalloproteins. Vol. 2. Wiley, Chichester, UK, pp. 782-790.
    • (2001) Handbook of Metalloproteins , vol.2 , pp. 782-790
    • Frolow, F.1    Kalb, A.J.2
  • 16
    • 0011945794 scopus 로고
    • Location of haem in bacterioferritin of E. coli
    • Frolow, F., Kalb, A.J. and Yariv, J. (1993) Location of haem in bacterioferritin of E. coli. Acta Crystallogr. D, 49, 597-600.
    • (1993) Acta Crystallogr. D , vol.49 , pp. 597-600
    • Frolow, F.1    Kalb, A.J.2    Yariv, J.3
  • 17
    • 0028467772 scopus 로고
    • Structure of a unique twofold symmetric haem-binding site
    • Frolow, F., Kalb, A.J. and Yariv, J. (1994) Structure of a unique twofold symmetric haem-binding site. Nat. Struct. Biol., 1, 453-460.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 453-460
    • Frolow, F.1    Kalb, A.J.2    Yariv, J.3
  • 18
    • 0030754031 scopus 로고    scopus 로고
    • X-ray structure of recombinant horse L chain apoferritin at 2.0 Å resolution: Implications for stability and function
    • Gallois, B. et al. (1997) X-ray structure of recombinant horse L chain apoferritin at 2.0 Å resolution: implications for stability and function. J. Biol. Inorg. Chem., 2, 360-367.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 360-367
    • Gallois, B.1
  • 19
    • 0035800902 scopus 로고    scopus 로고
    • Could a diiron-containing four-helix-bundle protein have been a primitive oxygen reductase?
    • Gomes, C.M., Le Gall, J., Xavier, A.V. and Teixeira, M. (2001) Could a diiron-containing four-helix-bundle protein have been a primitive oxygen reductase? Chembiochem. 2, 583-587.
    • (2001) Chembiochem , vol.2 , pp. 583-587
    • Gomes, C.M.1    Le Gall, J.2    Xavier, A.V.3    Teixeira, M.4
  • 22
    • 0031959912 scopus 로고    scopus 로고
    • The crystal structure of Dps, a ferritin homolog that binds and protects DNA
    • Grant, R.A., Filman, D.J., Finkel, S.E., Kolter, R. and Hogle, J.M. (1998) The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat. Struct. Biol., 5, 294-303.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 294-303
    • Grant, R.A.1    Filman, D.J.2    Finkel, S.E.3    Kolter, R.4    Hogle, J.M.5
  • 23
    • 0032793828 scopus 로고    scopus 로고
    • Crystal structure of bullfrog M ferritin at 2.8 Å resolution: Analysis of subunit interactions and the binuclear metal center
    • Ha, Y., Shi, D., Small, G.W., Theil, E.C. and Allewell, N.M. (1999) Crystal structure of bullfrog M ferritin at 2.8 Å resolution: analysis of subunit interactions and the binuclear metal center. J. Biol. Inorg. Chem., 4, 243-256.
    • (1999) J. Biol. Inorg. Chem. , vol.4 , pp. 243-256
    • Ha, Y.1    Shi, D.2    Small, G.W.3    Theil, E.C.4    Allewell, N.M.5
  • 24
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P.M. and Arosio, P. (1996) The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta, 1275, 161-203.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 29
    • 0034614666 scopus 로고    scopus 로고
    • A short Fe-Fe distance in peroxodiferric ferritin: Control of Fe substrate versus cofactor decay?
    • Hwang, J., Krebs, C., Huynh, B.H., Edmondson, D.E., Theil, E.C. and Penner-Hahn, J.E. (2000) A short Fe-Fe distance in peroxodiferric ferritin: control of Fe substrate versus cofactor decay? Science, 287, 122-125.
    • (2000) Science , vol.287 , pp. 122-125
    • Hwang, J.1    Krebs, C.2    Huynh, B.H.3    Edmondson, D.E.4    Theil, E.C.5    Penner-Hahn, J.E.6
  • 30
    • 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 Tsemoglou, 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    Tsemoglou, D.4
  • 31
    • 0033119386 scopus 로고    scopus 로고
    • Software for handling macromolecular envelopes
    • Kleywegt, G.J. and Jones, T.A. (1999) Software for handling macromolecular envelopes. Acta Crystallogr. D, 55, 941-944.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 941-944
    • Kleywegt, G.J.1    Jones, T.A.2
  • 32
    • 12644273812 scopus 로고    scopus 로고
    • Structural similarity and functional diversity in diiron-oxo proteins
    • Kurtz, J.D.M. (1997) Structural similarity and functional diversity in diiron-oxo proteins. J. Biol. Inorg. Chem., 2, 159-167.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 159-167
    • Kurtz, J.D.M.1
  • 34
    • 0026059720 scopus 로고
    • Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts
    • Lawson, D.M. et al. (1991) Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. Nature, 349, 541-544.
    • (1991) Nature , vol.349 , pp. 541-544
    • Lawson, D.M.1
  • 35
    • 0027430148 scopus 로고
    • Kinetic and structural characterization of an intermediate in the biomineralization of bacterioferritin
    • Le Brun, N.E., Wilson, M.T., Andrews, S.C., Guest, J.R., Harrison, P.M., Thomson, A.J. and Moore, G.R. (1993) Kinetic and structural characterization of an intermediate in the biomineralization of bacterioferritin. FEBS Lett., 333, 197-202.
    • (1993) FEBS Lett. , vol.333 , pp. 197-202
    • Le Brun, N.E.1    Wilson, M.T.2    Andrews, S.C.3    Guest, J.R.4    Harrison, P.M.5    Thomson, A.J.6    Moore, G.R.7
  • 38
    • 0037389839 scopus 로고    scopus 로고
    • The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans
    • Macedo, S. et al. (2003) The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans. Nat. Struct. Biol., 10, 285-290.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 285-290
    • Macedo, S.1
  • 42
    • 0032516447 scopus 로고    scopus 로고
    • Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization
    • Pereira, A.S., Small, W., Krebs, C., Tavares, P., Edmondson, D.E., Theil, E.C. and Huynh, B.H. (1998) Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization. Biochemistry, 37, 9871-9876.
    • (1998) Biochemistry , vol.37 , pp. 9871-9876
    • Pereira, A.S.1    Small, W.2    Krebs, C.3    Tavares, P.4    Edmondson, D.E.5    Theil, E.C.6    Huynh, B.H.7
  • 45
    • 0034284575 scopus 로고    scopus 로고
    • Iron-coproporphyrin III is a natural cofactor in bacterioferritin from the anaerobic bacterium Desulfovibrio desulfuricans
    • Romão, C.V., Louro, R., Timkovich, R., Lubben, M., Liu, M.Y., LeGall, J., Xavier, A.V. and Teixeira, M. (2000a) Iron-coproporphyrin III is a natural cofactor in bacterioferritin from the anaerobic bacterium Desulfovibrio desulfuricans. FEBS Lett., 480, 213-216.
    • (2000) FEBS Lett. , vol.480 , pp. 213-216
    • Romão, C.V.1    Louro, R.2    Timkovich, R.3    Lubben, M.4    Liu, M.Y.5    LeGall, J.6    Xavier, A.V.7    Teixeira, M.8
  • 46
    • 0034643893 scopus 로고    scopus 로고
    • A bacterioferritin from the strict anaerobe Desulfovibrio desulfuricans ATCC 27774
    • Romão, C.V., Regalla, M., Xavier, A.V., Teixeira, M., Liu, M.Y. and Le Gall, J. (2000b) A bacterioferritin from the strict anaerobe Desulfovibrio desulfuricans. ATCC 27774. Biochemistry, 39, 6841-6849.
    • (2000) Biochemistry , vol.39 , pp. 6841-6849
    • Romão, C.V.1    Regalla, M.2    Xavier, A.V.3    Teixeira, M.4    Liu, M.Y.5    Le Gall, J.6
  • 47
    • 0030885887 scopus 로고    scopus 로고
    • Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): Implications for substrate gating and component interactions
    • Rosenzweig, A.C., Brandstetter, H., Whittington, D.A., Nordlund, P., Lippard, S.J. and Frederick, C.A. (1997) Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions. Proteins, 29, 141-152.
    • (1997) Proteins , vol.29 , pp. 141-152
    • Rosenzweig, A.C.1    Brandstetter, H.2    Whittington, D.A.3    Nordlund, P.4    Lippard, S.J.5    Frederick, C.A.6
  • 48
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner, M.F., Spehner, J.C. and Olson, A.J. (1996) Reduced surface: an efficient way to compute molecular surfaces. Biopolymers, 38, 305-320.
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Spehner, J.C.2    Olson, A.J.3
  • 50
    • 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, 18685-18688.
    • (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
  • 51
    • 0000171802 scopus 로고    scopus 로고
    • Ferritin
    • Messerschmidt, A., Poulos, H.R. and Weighardt, K. (eds). Wiley, Chichester, UK
    • Theil, E.C. (2001) Ferritin. In Messerschmidt, A., Poulos, H.R. and Weighardt, K. (eds), Handbook of Metalloproteins. Vol. 2. Wiley, Chichester, UK, pp. 771-781.
    • (2001) Handbook of Metalloproteins , vol.2 , pp. 771-781
    • Theil, E.C.1
  • 53
    • 19244377006 scopus 로고    scopus 로고
    • Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography
    • Tong, W. et al. (1998) Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography. Biochemistry, 37, 5840-5848.
    • (1998) Biochemistry , vol.37 , pp. 5840-5848
    • Tong, W.1
  • 54
    • 0028825383 scopus 로고
    • Iron(II) oxidation by H chain ferritin: Evidence from site-directed mutagenesis that a transient blue species is formed at the dinuclear iron center
    • Treffry, A., Zhao, Z., Quail, M.A., Guest, J.R. and Harrison, P.M. (1995) Iron(II) oxidation by H chain ferritin: evidence from site-directed mutagenesis that a transient blue species is formed at the dinuclear iron center. Biochemistry, 34, 15204-15213.
    • (1995) Biochemistry , vol.34 , pp. 15204-15213
    • Treffry, A.1    Zhao, Z.2    Quail, M.A.3    Guest, J.R.4    Harrison, P.M.5
  • 56
    • 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, 13262-13269.
    • (1993) Biochemistry , vol.32 , pp. 13262-13269
    • Waldo, G.S.1    Theil, E.C.2
  • 57
    • 0027398912 scopus 로고
    • Formation of an Fe(III)-tyrosinate complex during biomineralization of Hsubunit ferritin
    • Waldo, G.S., Ling, J., Sanders-Loehr, J. and Theil, E.C. (1993) Formation of an Fe(III)-tyrosinate complex during biomineralization of Hsubunit ferritin. Science, 259, 796-798.
    • (1993) Science , vol.259 , pp. 796-798
    • Waldo, G.S.1    Ling, J.2    Sanders-Loehr, J.3    Theil, E.C.4
  • 58
    • 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, 9743-9750.
    • (1998) Biochemistry , vol.37 , pp. 9743-9750
    • Yang, X.1    Chen-Barrett, Y.2    Arosio, P.3    Chasteen, N.D.4
  • 59
    • 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, 4915-4923.
    • (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
  • 60
    • 33748504362 scopus 로고    scopus 로고
    • Catalytic iron (II) oxidation in the non-haem ferritin of Escherichia coli: The early intermediate is not an iron tyrosinate
    • Zhao, Z., Treffry, A., Quail, M.A., Guest, J.R. and Harrison, P.M. (1997) Catalytic iron (II) oxidation in the non-haem ferritin of Escherichia coli: the early intermediate is not an iron tyrosinate. J. Chem. Soc. Dalton Trans., 21, 3977-3978.
    • (1997) J. Chem. Soc. Dalton Trans. , vol.21 , pp. 3977-3978
    • Zhao, Z.1    Treffry, A.2    Quail, M.A.3    Guest, J.R.4    Harrison, P.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.