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Volumn 352, Issue 2, 2005, Pages 467-477

μ-1,2-peroxo diferric complex formation in horse spleen ferritin. A mixed H/L-subunit heteropolymer

Author keywords

Horse spleen ferritin; Iron mineralization; Peroxo intermediate; Stopped flow kinetics

Indexed keywords

CERULOPLASMIN; FERRITIN; FERROUS ION; IRON COMPLEX;

EID: 23944512213     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.07.039     Document Type: Article
Times cited : (30)

References (35)
  • 1
    • 0030608152 scopus 로고    scopus 로고
    • Ferritins: Molecular properties, iron storage function and cellular regulation
    • P.M. Harrison, and P. Arosio Ferritins: molecular properties, iron storage function and cellular regulation Biochim. Biophys. Acta Bio-Energ. 1275 1996 161 203
    • (1996) Biochim. Biophys. Acta Bio-Energ. , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 2
    • 0033617958 scopus 로고    scopus 로고
    • Mineralization in ferritin: An efficient means of iron storage
    • N.D. Chasteen, and P.M. Harrison Mineralization in ferritin: an efficient means of iron storage J. Struct. Biol. 126 1999 182 194
    • (1999) J. Struct. Biol. , vol.126 , pp. 182-194
    • Chasteen, N.D.1    Harrison, P.M.2
  • 3
    • 0037151089 scopus 로고    scopus 로고
    • Human mitochondrial ferritin expressed in HeLa cells incorporates iron and affects cellular iron metabolism
    • B. Corsi, A. Cozzi, P. Arosio, J. Drysdale, P. Santambrogio, and A. Campanella Human mitochondrial ferritin expressed in HeLa cells incorporates iron and affects cellular iron metabolism J. Biol. Chem. 277 2002 22430 22437
    • (2002) J. Biol. Chem. , vol.277 , pp. 22430-22437
    • Corsi, B.1    Cozzi, A.2    Arosio, P.3    Drysdale, J.4    Santambrogio, P.5    Campanella, A.6
  • 4
    • 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
    • A.S. Pereira, W. Small, C. Krebs, P. Tavares, D.E. Edmondson, E.C. Theil, and B.H. Huynh Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization Biochemistry 37 1998 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
  • 6
    • 0031605490 scopus 로고    scopus 로고
    • Ferritin. Uptake, storage, and release of iron
    • A. Sigel H. Sigel Dekker New York
    • N.D. Chasteen Ferritin. Uptake, storage, and release of iron A. Sigel H. Sigel Metal Ions in Biological Systems vol. 35 1998 Dekker New York 479 514
    • (1998) Metal Ions in Biological Systems , vol.35 , pp. 479-514
    • Chasteen, N.D.1
  • 7
    • 0000823059 scopus 로고    scopus 로고
    • Identification of catalytic residues involved in iron uptake by L-chain ferritins
    • R.R. Crichton, A. Herbas, O. Chavez-Alba, and F. Roland Identification of catalytic residues involved in iron uptake by L-chain ferritins J. Biol. Inorg. Chem. 1 1996 567 574
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 567-574
    • Crichton, R.R.1    Herbas, A.2    Chavez-Alba, O.3    Roland, F.4
  • 9
    • 0034614666 scopus 로고    scopus 로고
    • A short Fe-Fe distance in peroxodiferric ferritin: Control of Fe substrate versus cofactor decay?
    • J. Hwang, C. Krebs, B.H. Huynh, D.E. Edmondson, E.C. Theil, and J.E. Penner-Hahn A short Fe-Fe distance in peroxodiferric ferritin: control of Fe substrate versus cofactor decay? Science 287 2000 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
  • 12
    • 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
    • A. Treffry, Z. Zhao, M.A. Quail, J.R. Guest, and P.M. Harrison 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 1995 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
  • 13
    • 2942558543 scopus 로고    scopus 로고
    • Ferritin reaction: Direct identification of the site for the diferric peroxide reaction intermediate
    • X. Liu, and E.C. Theil Ferritin reaction: direct identification of the site for the diferric peroxide reaction intermediate Proc. Natl Acad. Sci. USA 101 2004 8557 8562
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 8557-8562
    • Liu, X.1    Theil, E.C.2
  • 14
    • 33748504362 scopus 로고    scopus 로고
    • Catalytic iron oxidation in the non-haem ferritin of Escherichia coli: The early intermediate is not an iron tyrosinate
    • Z. Zhao, A. Treffry, M.A. Quail, J.R. Guest, and P.M. Harrison Catalytic iron oxidation in the non-haem ferritin of Escherichia coli: the early intermediate is not an iron tyrosinate J. Chem. Soc. Dalton Trans. 1997 3977 3978
    • (1997) J. Chem. Soc. Dalton Trans. , pp. 3977-3978
    • Zhao, Z.1    Treffry, A.2    Quail, M.A.3    Guest, J.R.4    Harrison, P.M.5
  • 15
    • 0037452863 scopus 로고    scopus 로고
    • Multiple pathways for mineral core formation in mammalian apoferritin. the role of hydrogen peroxide
    • G. Zhao, F. Bou-Abdallah, P. Arosio, S. Levi, C. Janus-Chandler, and N.D. Chasteen Multiple pathways for mineral core formation in mammalian apoferritin. The role of hydrogen peroxide Biochemistry 42 2003 3142 3150
    • (2003) Biochemistry , vol.42 , pp. 3142-3150
    • Zhao, G.1    Bou-Abdallah, F.2    Arosio, P.3    Levi, S.4    Janus-Chandler, C.5    Chasteen, N.D.6
  • 16
    • 15744368011 scopus 로고    scopus 로고
    • Origin of the unusual kinetics of iron deposition in human H-chain ferritin
    • F. Bou-Abdallah, G. Zhao, H.R. Mayne, P. Arosio, and N.D. Chasteen Origin of the unusual kinetics of iron deposition in human H-chain ferritin J. Am. Chem. Soc. 127 2005 3885 3893
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 3885-3893
    • Bou-Abdallah, F.1    Zhao, G.2    Mayne, H.R.3    Arosio, P.4    Chasteen, N.D.5
  • 17
    • 0027522012 scopus 로고
    • Ferroxidase kinetics of human liver apoferritin, recombinant H-chain apoferritin, and site-directed mutants
    • S. Sun, P. Arosio, S. Levi, and N.D. Chasteen Ferroxidase kinetics of human liver apoferritin, recombinant H-chain apoferritin, and site-directed mutants Biochemistry 32 1993 9362 9369
    • (1993) Biochemistry , vol.32 , pp. 9362-9369
    • Sun, S.1    Arosio, P.2    Levi, S.3    Chasteen, N.D.4
  • 18
    • 0026469339 scopus 로고
    • Ferroxidase kinetics of horse spleen apoferritin
    • S. Sun, and N.D. Chasteen Ferroxidase kinetics of horse spleen apoferritin J. Biol. Chem. 267 1992 25160 25166
    • (1992) J. Biol. Chem. , vol.267 , pp. 25160-25166
    • Sun, S.1    Chasteen, N.D.2
  • 19
    • 0026475825 scopus 로고
    • Evidence of H- and L-chains have co-operative roles in the iron-uptake mechanism of human ferritin
    • S. Levi, S.J. Yewdall, P.M. Harrison, P. Santambrogio, A. Cozzi, and E. Rovida Evidence of H- and L-chains have co-operative roles in the iron-uptake mechanism of human ferritin Biochem. J. 288 1992 591 596
    • (1992) Biochem. J. , vol.288 , pp. 591-596
    • Levi, S.1    Yewdall, S.J.2    Harrison, P.M.3    Santambrogio, P.4    Cozzi, A.5    Rovida, E.6
  • 20
    • 0024245282 scopus 로고
    • Mechanism of ferritin iron uptake: Activity of the H-chain and deletion mapping of the ferro-oxidase site. a study of iron uptake and ferro-oxidase activity of human liver, recombinant H-chain ferritins, and of two H-chain deletion mutants
    • S. Levi, A. Luzzago, G. Cesareni, A. Cozzi, F. Franceschinelli, A. Albertini, and P. Arosio Mechanism of ferritin iron uptake: activity of the H-chain and deletion mapping of the ferro-oxidase site. A study of iron uptake and ferro-oxidase activity of human liver, recombinant H-chain ferritins, and of two H-chain deletion mutants J. Biol. Chem. 263 1988 18086 18092
    • (1988) J. Biol. Chem. , vol.263 , pp. 18086-18092
    • Levi, S.1    Luzzago, A.2    Cesareni, G.3    Cozzi, A.4    Franceschinelli, F.5    Albertini, A.6    Arosio, P.7
  • 21
    • 0026059720 scopus 로고
    • Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts
    • D.M. Lawson, P.J. Artymiuk, S.J. Yewdall, J.M. Smith, J.C. Livingstone, and A. Treffry Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts Nature 349 1991 541 544
    • (1991) Nature , vol.349 , pp. 541-544
    • Lawson, D.M.1    Artymiuk, P.J.2    Yewdall, S.J.3    Smith, J.M.4    Livingstone, J.C.5    Treffry, A.6
  • 23
    • 0035845647 scopus 로고    scopus 로고
    • Is hydrogen peroxide produced during iron(II) oxidation in mammalian apoferritins?
    • G. Zhao, F. Bou-Abdallah, X. Yang, P. Arosio, and N.D. Chasteen Is hydrogen peroxide produced during iron(II) oxidation in mammalian apoferritins? Biochemistry 40 2001 10832 10838
    • (2001) Biochemistry , vol.40 , pp. 10832-10838
    • Zhao, G.1    Bou-Abdallah, F.2    Yang, X.3    Arosio, P.4    Chasteen, N.D.5
  • 24
    • 0032493313 scopus 로고    scopus 로고
    • Reaction paths of iron oxidation and hydrolysis in horse spleen and recombinant human ferritins
    • X. Yang, Y. Chen-Barrett, P. Arosio, and N.D. Chasteen Reaction paths of iron oxidation and hydrolysis in horse spleen and recombinant human ferritins Biochemistry 37 1998 9743 9750
    • (1998) Biochemistry , vol.37 , pp. 9743-9750
    • Yang, X.1    Chen-Barrett, Y.2    Arosio, P.3    Chasteen, N.D.4
  • 25
    • 0015270684 scopus 로고
    • The formation of ferritin from apoferritin. Kinetics and mechanism of iron uptake
    • I.G. Macara, T.G. Hoy, and P.M. Harrison The formation of ferritin from apoferritin. Kinetics and mechanism of iron uptake Biochem. J. 126 1972 151 162
    • (1972) Biochem. J. , vol.126 , pp. 151-162
    • MacAra, I.G.1    Hoy, T.G.2    Harrison, P.M.3
  • 26
    • 0015896975 scopus 로고
    • The formation of ferritin from apoferritin. Catalytic action of apoferritin
    • I.G. Macara, T.G. Hoy, and P.M. Harrison The formation of ferritin from apoferritin. Catalytic action of apoferritin Biochem. J. 135 1973 343 348
    • (1973) Biochem. J. , vol.135 , pp. 343-348
    • MacAra, I.G.1    Hoy, T.G.2    Harrison, P.M.3
  • 27
    • 0025789986 scopus 로고
    • 2 stoichiometry during core formation
    • 2 stoichiometry during core formation J. Biol. Chem. 266 1991 19965 19970
    • (1991) J. Biol. Chem. , vol.266 , pp. 19965-19970
    • Xu, B.1    Chasteen, N.D.2
  • 28
    • 0037086048 scopus 로고    scopus 로고
    • Characterization of the H- and L-subunit ratios of ferritins by sodium dodecyl sulfate-capillary gel electrophoresis
    • J.K. Grady, J. Zang, T.M. Laue, P. Arosio, and N.D. Chasteen Characterization of the H- and L-subunit ratios of ferritins by sodium dodecyl sulfate-capillary gel electrophoresis Anal. Biochem. 302 2002 263 268
    • (2002) Anal. Biochem. , vol.302 , pp. 263-268
    • Grady, J.K.1    Zang, J.2    Laue, T.M.3    Arosio, P.4    Chasteen, N.D.5
  • 29
    • 17244378120 scopus 로고    scopus 로고
    • Intermediates in the oxygenation of a nonheme diirion(II) complex, including first evidence for a bound superoxo species
    • X. Shan, and L. Que Jr Intermediates in the oxygenation of a nonheme diirion(II) complex, including first evidence for a bound superoxo species Proc. Natl Acad. Sci. USA 102 2005 5340 5345
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 5340-5345
    • Shan, X.1    Que Jr., L.2
  • 30
    • 12444296565 scopus 로고    scopus 로고
    • Structural and spectroscopic characterization of (μ-hydroxo or μ-oxo)(μ-peroxo)diiron(III) complexes: Models for peroxo intermediates of non-heme diiron proteins
    • X. Zhang, H. Furutachi, S. Fujinami, S. Nagtomo, Y. Maeda, and Y. Watanabe Structural and spectroscopic characterization of (μ-hydroxo or μ-oxo)(μ-peroxo)diiron(III) complexes: models for peroxo intermediates of non-heme diiron proteins J. Am. Chem. Soc. 127 2005 826 827
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 826-827
    • Zhang, X.1    Furutachi, H.2    Fujinami, S.3    Nagtomo, S.4    Maeda, Y.5    Watanabe, Y.6
  • 32
    • 0000016621 scopus 로고
    • The three dimensional structure of apoferritin: A framework controlling ferritin's iron storage and release
    • A.V. Xavier VCH Verlagsgesellschaft mbH Weinheim
    • P.M. Harrison, G.C. Ford, D.W. Rice, J.M.A. Smith, A. Treffry, and J.L. White The three dimensional structure of apoferritin: a framework controlling ferritin's iron storage and release A.V. Xavier Frontiers in Bioinorganic Chemistry 1986 VCH Verlagsgesellschaft mbH Weinheim 268 277
    • (1986) Frontiers in Bioinorganic Chemistry , pp. 268-277
    • Harrison, P.M.1    Ford, G.C.2    Rice, D.W.3    Smith, J.M.A.4    Treffry, A.5    White, J.L.6
  • 33
    • 0026535851 scopus 로고
    • Mechanism of catalysis of Fe(II) oxidation by ferritin H chains
    • A. Treffry, J. Hirzmann, S.J. Yewdall, and P.M. Harrison Mechanism of catalysis of Fe(II) oxidation by ferritin H chains FEBS Letters 302 1992 108 112
    • (1992) FEBS Letters , vol.302 , pp. 108-112
    • Treffry, A.1    Hirzmann, J.2    Yewdall, S.J.3    Harrison, P.M.4
  • 34
    • 0024473836 scopus 로고
    • Mössbauer spectroscopic study of the initial stages of iron-core formation in horse spleen apoferritin: Evidence for both isolated Fe(III) atoms and oxo-bridged Fe(III) dimers as early intermediates
    • E.R. Bauminger, P.M. Harrison, I. Nowik, and A. Treffry Mössbauer spectroscopic study of the initial stages of iron-core formation in horse spleen apoferritin: evidence for both isolated Fe(III) atoms and oxo-bridged Fe(III) dimers as early intermediates Biochemistry 28 1989 5486 5493
    • (1989) Biochemistry , vol.28 , pp. 5486-5493
    • Bauminger, E.R.1    Harrison, P.M.2    Nowik, I.3    Treffry, A.4
  • 35
    • 0019874117 scopus 로고
    • Amino acid sequence of horse spleen apoferritin
    • M. Heusterspreute, and R.R. Crichton Amino acid sequence of horse spleen apoferritin FEBS Letters 129 1981 322 327
    • (1981) FEBS Letters , vol.129 , pp. 322-327
    • Heusterspreute, M.1    Crichton, R.R.2


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