메뉴 건너뛰기




Volumn 347, Issue 3, 2005, Pages 543-554

Unique iron binding and oxidation properties of human mitochondrial ferritin: A comparative analysis with human H-chain ferritin

Author keywords

Ferritin; Iron toxicity; Mineralization; Mitochondria; Oxidative stress

Indexed keywords

CERULOPLASMIN; FERRITIN;

EID: 14744304889     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.007     Document Type: Article
Times cited : (81)

References (46)
  • 2
    • 0000171802 scopus 로고    scopus 로고
    • Ferritin
    • A. Messerschmidt R. Huber T. Poulos K. Wieghardt John Wiley and Sons Chichester
    • E.C. Theil Ferritin A. Messerschmidt R. Huber T. Poulos K. Wieghardt Handbook of Metalloproteins 2001 John Wiley and Sons Chichester 771 781
    • (2001) Handbook of Metalloproteins , pp. 771-781
    • Theil, E.C.1
  • 3
    • 0033954991 scopus 로고    scopus 로고
    • Oxidative stress and Alzheimer disease
    • Y. Christen Oxidative stress and Alzheimer disease Am. J. Clin. Nutr. 71 2000 621S 629S
    • (2000) Am. J. Clin. Nutr. , vol.71
    • Christen, Y.1
  • 4
    • 0029266160 scopus 로고
    • Iron species in iron homeostasis and toxicity
    • R.R. Crichton, and R.J. Ward Iron species in iron homeostasis and toxicity Analyst 120 1995 693 697
    • (1995) Analyst , vol.120 , pp. 693-697
    • Crichton, R.R.1    Ward, R.J.2
  • 5
    • 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 1275 1996 161 203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 6
    • 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
  • 7
    • 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.A. 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.A.4    Livingstone, J.C.5    Treffry, A.6
  • 8
    • 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
  • 9
    • 0028276960 scopus 로고
    • The role of the L-chain in ferritin iron incorporation. Studies of homo- and heteropolymers
    • S. Levi, P. Santambrogio, A. Cozzi, E. Rovida, B. Corsi, and E. Tamborini The role of the L-chain in ferritin iron incorporation. Studies of homo- and heteropolymers J. Mol. Biol. 238 1994 649 654
    • (1994) J. Mol. Biol. , vol.238 , pp. 649-654
    • Levi, S.1    Santambrogio, P.2    Cozzi, A.3    Rovida, E.4    Corsi, B.5    Tamborini, E.6
  • 10
    • 0027198736 scopus 로고
    • Production and characterization of recombinant heteropolymers of human ferritin H and L chains
    • P. Santambrogio, S. Levi, A. Cozzi, E. Rovida, A. Albertini, and P. Arosio Production and characterization of recombinant heteropolymers of human ferritin H and L chains J. Biol. Chem. 268 1993 12744 12748
    • (1993) J. Biol. Chem. , vol.268 , pp. 12744-12748
    • Santambrogio, P.1    Levi, S.2    Cozzi, A.3    Rovida, E.4    Albertini, A.5    Arosio, P.6
  • 12
    • 0033986734 scopus 로고    scopus 로고
    • The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site
    • A. Ilari, S. Stefanini, E. Chiancone, and D. Tsermoglou The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site Nature Struct. Biol. 7 2000 38 43
    • (2000) Nature Struct. Biol. , vol.7 , pp. 38-43
    • Ilari, A.1    Stefanini, S.2    Chiancone, E.3    Tsermoglou, D.4
  • 13
    • 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
    • G. Zhao, P. Ceci, A. Ilari, L. Giangiacomo, T.M. Laue, E. Chiancone, and N.D. Chasteen 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 2002 27689 27696
    • (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
  • 14
    • 0036830474 scopus 로고    scopus 로고
    • Mitochondrial function and dysfunction in the cell: Its relevance to aging and aging-related disease
    • D.G. Nicholls Mitochondrial function and dysfunction in the cell: its relevance to aging and aging-related disease Int. J. Biochem. Cell. Biol. 34 2002 1372 1381
    • (2002) Int. J. Biochem. Cell. Biol. , vol.34 , pp. 1372-1381
    • Nicholls, D.G.1
  • 15
    • 0030608677 scopus 로고    scopus 로고
    • The ABC transporter Atm1p is required for mitochondrial iron homeostasis
    • G. Kispal, P. Csere, B. Guiard, and R. Lill The ABC transporter Atm1p is required for mitochondrial iron homeostasis FEBS Letters 418 1997 346 350
    • (1997) FEBS Letters , vol.418 , pp. 346-350
    • Kispal, G.1    Csere, P.2    Guiard, B.3    Lill, R.4
  • 16
    • 0032540929 scopus 로고    scopus 로고
    • Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis
    • S.A.B. Knight, N.B.V. Sepuri, D. Pain, and A. Dancis Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis J. Biol. Chem. 273 1998 18389 18393
    • (1998) J. Biol. Chem. , vol.273 , pp. 18389-18393
    • Knight, S.A.B.1    Sepuri, N.B.V.2    Pain, D.3    Dancis, A.4
  • 17
    • 0033516467 scopus 로고    scopus 로고
    • Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria
    • H. Lange, G. Kispal, and R. Lill Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria J. Biol. Chem. 274 1999 18989 18996
    • (1999) J. Biol. Chem. , vol.274 , pp. 18989-18996
    • Lange, H.1    Kispal, G.2    Lill, R.3
  • 18
    • 0030296878 scopus 로고    scopus 로고
    • Friedreich's ataxia protein: Phylogenetic evidence for mitochondrial dysfunction
    • T.J. Gibson, E.V. Koonin, G. Musco, A. Pastore, and P. Bork Friedreich's ataxia protein: phylogenetic evidence for mitochondrial dysfunction Trends Neurosci. 19 1996 465 468
    • (1996) Trends Neurosci. , vol.19 , pp. 465-468
    • Gibson, T.J.1    Koonin, E.V.2    Musco, G.3    Pastore, A.4    Bork, P.5
  • 19
    • 0034641851 scopus 로고    scopus 로고
    • Human frataxin maintains mitochondrial iron homeostasis in Saccharomyces cerevisiae
    • P. Cavadini, C. Gellera, P.I. Patel, and G. Isaya Human frataxin maintains mitochondrial iron homeostasis in Saccharomyces cerevisiae Hum. Mol. Genet. 9 2000 2523 2530
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2523-2530
    • Cavadini, P.1    Gellera, C.2    Patel, P.I.3    Isaya, G.4
  • 20
    • 0642287902 scopus 로고    scopus 로고
    • Iron metabolism and mitochondrial abnormalities in Friedreich ataxia
    • M. Pandolfo Iron metabolism and mitochondrial abnormalities in Friedreich ataxia Blood Cells Mol. Dis. 29 2002 536 547
    • (2002) Blood Cells Mol. Dis. , vol.29 , pp. 536-547
    • Pandolfo, M.1
  • 22
    • 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
  • 23
    • 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
  • 25
    • 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
  • 26
    • 1842583828 scopus 로고    scopus 로고
    • The putative "nucleation site" in human H-chain ferritin is not required for mineralization of the iron core
    • F. Bou-Abdallah, G. Biasiotto, P. Arosio, and N.D. Chasteen The putative "nucleation site" in human H-chain ferritin is not required for mineralization of the iron core Biochemistry 43 2004 4332 4337
    • (2004) Biochemistry , vol.43 , pp. 4332-4337
    • Bou-Abdallah, F.1    Biasiotto, G.2    Arosio, P.3    Chasteen, N.D.4
  • 27
    • 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
  • 28
    • 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
  • 29
    • 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
  • 30
    • 0037125958 scopus 로고    scopus 로고
    • Ferrous ion binding to recombinant human H-chain ferritin. An isothermal titration calorimetry study
    • F. Bou-Abdallah, P. Arosio, P. Santambrogio, X. Yang, C. Janus-Chandler, and N.D. Chasteen Ferrous ion binding to recombinant human H-chain ferritin. An isothermal titration calorimetry study Biochemistry 41 2002 11184 11191
    • (2002) Biochemistry , vol.41 , pp. 11184-11191
    • Bou-Abdallah, F.1    Arosio, P.2    Santambrogio, P.3    Yang, X.4    Janus-Chandler, C.5    Chasteen, N.D.6
  • 31
    • 0037020091 scopus 로고    scopus 로고
    • Iron detoxification properties of Escherichia coli bacterioferritin. Attenuation of oxyradical chemistry
    • F. Bou-Abdallah, A.C. Lewin, N.E. Le Brun, G.R. Moore, and N.D. Chasteen Iron detoxification properties of Escherichia coli bacterioferritin. Attenuation of oxyradical chemistry J. Biol. Chem. 277 2002 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
  • 32
    • 0025789986 scopus 로고
    • Iron oxidation chemistry in ferritin. Increasing Fe/O2 stoichiometry during core formation
    • B. Xu, and N.D. Chasteen Iron oxidation chemistry in ferritin. Increasing Fe/O2 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
  • 33
    • 3342981572 scopus 로고    scopus 로고
    • Iron binding and oxidation properties of the bacterial frataxin CyaY of Escherichia coli
    • F. Bou-Abdallah, S. Adinolfi, A. Pastore, T.M. Laue, and N.D. Chasteen Iron binding and oxidation properties of the bacterial frataxin CyaY of Escherichia coli J. Mol. Biol. 341 2004 605 615
    • (2004) J. Mol. Biol. , vol.341 , pp. 605-615
    • Bou-Abdallah, F.1    Adinolfi, S.2    Pastore, A.3    Laue, T.M.4    Chasteen, N.D.5
  • 34
    • 0037613459 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins
    • T. Yoon, and J.A. Cowan Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins J. Am. Chem. Soc. 125 2003 6078 6084
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 35
    • 2942744572 scopus 로고    scopus 로고
    • Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis
    • T. Yoon, and J.A. Cowan Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis J. Biol. Chem. 279 2004 25943 25946
    • (2004) J. Biol. Chem. , vol.279 , pp. 25943-25946
    • Yoon, T.1    Cowan, J.A.2
  • 36
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • A.-L. Bulteau, H.A. O'Neill, M.C. Kennedy, M. Ikeda-Saito, G. Isaya, and L.I. Szweda Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity Science 305 2004 242 245
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.-L.1    O'Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 37
    • 0031718648 scopus 로고    scopus 로고
    • How the presence of three iron binding sites affects the iron storage function of the ferritin (EcFtnA) of Escherichia coli
    • A. Treffry, Z. Zhao, M.A. Quail, J.R. Guest, and P.M. Harrison How the presence of three iron binding sites affects the iron storage function of the ferritin (EcFtnA) of Escherichia coli FEBS Letters 432 1998 213 218
    • (1998) FEBS Letters , vol.432 , pp. 213-218
    • Treffry, A.1    Zhao, Z.2    Quail, M.A.3    Guest, J.R.4    Harrison, P.M.5
  • 38
    • 0034712683 scopus 로고    scopus 로고
    • The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin
    • X. Yang, N.E. Le Brun, A.J. Thomson, G.R. Moore, and N.D. Chasteen The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin Biochemistry 39 2000 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
  • 40
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • J. Gerber, U. Muehlenhoff, and R. Lill An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1 EMBO Rep. 4 2003 906 911
    • (2003) EMBO Rep. , vol.4 , pp. 906-911
    • Gerber, J.1    Muehlenhoff, U.2    Lill, R.3
  • 41
    • 0042232045 scopus 로고    scopus 로고
    • Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation
    • S. Park, O. Gakh, H.A. O'Neill, A. Mangravita, H. Nichol, J.C. Ferreira, and G. Isaya Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation J. Biol. Chem. 278 2003 31340 31351
    • (2003) J. Biol. Chem. , vol.278 , pp. 31340-31351
    • Park, S.1    Gakh, O.2    O'Neill, H.A.3    Mangravita, A.4    Nichol, H.5    Ferreira, J.C.6    Isaya, G.7
  • 42
    • 5444262935 scopus 로고    scopus 로고
    • The expression of human mitochondrial ferritin rescues respiratory function in frataxin-deficient yeast
    • A. Campanella, G. Isaya, H.A. O'Neill, P. Santambrogio, A. Cozzi, P. Arosio, and S. Levi The expression of human mitochondrial ferritin rescues respiratory function in frataxin-deficient yeast Hum. Mol. Genet. 13 2004 2279 2288
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2279-2288
    • Campanella, A.1    Isaya, G.2    O'Neill, H.A.3    Santambrogio, P.4    Cozzi, A.5    Arosio, P.6    Levi, S.7
  • 44
    • 0037372442 scopus 로고    scopus 로고
    • Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia
    • M. Cazzola, R. Invernizzi, G. Bergamaschi, S. Levi, B. Corsi, and E. Travaglino Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia Blood 101 2003 1996 2000
    • (2003) Blood , vol.101 , pp. 1996-2000
    • Cazzola, M.1    Invernizzi, R.2    Bergamaschi, G.3    Levi, S.4    Corsi, B.5    Travaglino, E.6
  • 46
    • 0029781087 scopus 로고    scopus 로고
    • Molecular diffusion into horse spleen ferritin: A nitroxide radical spin probe study
    • X. Yang, and N.D. Chasteen Molecular diffusion into horse spleen ferritin: a nitroxide radical spin probe study Biophys. J. 71 1996 1587 1595
    • (1996) Biophys. J. , vol.71 , pp. 1587-1595
    • Yang, X.1    Chasteen, N.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.