메뉴 건너뛰기




Volumn 114, Issue 2-3, 2005, Pages 235-244

Kinetic studies of iron deposition catalyzed by recombinant human liver heavy, and light ferritins and Azotobacter vinelandii bacterioferritin using O2 and H2O2 as oxidants

Author keywords

Bacterioferritin; Human liver ferritin; Hydrogen peroxide; Iron deposition; Kinetics; Recombinant ferritins

Indexed keywords

BACTERIAL PROTEIN; BACTERIOFERRITIN; CERULOPLASMIN; FERRITIN; FERROUS ION; HYDROGEN PEROXIDE; IRON; LIVER PROTEIN; OXIDIZING AGENT; OXYGEN; PROTEIN SUBUNIT; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 20244386979     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2004.11.008     Document Type: Article
Times cited : (19)

References (37)
  • 1
    • 0029468457 scopus 로고
    • Molecular aspects of iron uptake and storage in ferritin
    • P.M. Proulx-Curry, and N.D. Chasteen Molecular aspects of iron uptake and storage in ferritin Coord. Chem. Rev. 144 1995 347 368
    • (1995) Coord. Chem. Rev. , vol.144 , pp. 347-368
    • Proulx-Curry, P.M.1    Chasteen, N.D.2
  • 2
    • 0002840502 scopus 로고    scopus 로고
    • Ferritin and iron biomineralization
    • K.S. Suslick Pergamon Press Oxford, U.K.
    • G.S. Waldo, and E.C. Theil Ferritin and iron biomineralization K.S. Suslick Comprehensive Supramolecular Chemistry vol. 5 1996 Pergamon Press Oxford, U.K. 65 89
    • (1996) Comprehensive Supramolecular Chemistry , vol.5 , pp. 65-89
    • Waldo, G.S.1    Theil, E.C.2
  • 3
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • P.M. Harrison, and P. Arosio The 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
  • 4
    • 0023067301 scopus 로고
    • Ferritin structure gene regulation and cellular functionin animals, plants and microorganisms
    • E.C. Theil Ferritin structure gene regulation and cellular functionin animals, plants and microorganisms Annu. Rev. Biochem. 56 1987 289 316
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 289-316
    • Theil, E.C.1
  • 5
    • 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
  • 6
    • 0017812024 scopus 로고
    • Incorporation and release of inorganic phosphate in horse spleen ferritin
    • A. Treffry, and P.M. Harrison Incorporation and release of inorganic phosphate in horse spleen ferritin Biochem. J. 171 1978 313 320
    • (1978) Biochem. J. , vol.171 , pp. 313-320
    • Treffry, A.1    Harrison, P.M.2
  • 7
    • 0033580643 scopus 로고    scopus 로고
    • Forming the phosphate layer in reconstituted horse spleen ferritin and the role of phosphate in promoting core surface redox reactions
    • J.L. Johnson, M. Cannon, R.K. Watt, R.B. Frankel, and G.D. Watt Forming the phosphate layer in reconstituted horse spleen ferritin and the role of phosphate in promoting core surface redox reactions Biochemistry 38 1999 6706 6713
    • (1999) Biochemistry , vol.38 , pp. 6706-6713
    • Johnson, J.L.1    Cannon, M.2    Watt, R.K.3    Frankel, R.B.4    Watt, G.D.5
  • 9
    • 0025139929 scopus 로고
    • Iron environment in ferritin with large amounts of phosphate from Azotobacter vinelandii and horse spleen, analyzed using extended X-ray absorption fine structure (EXAFS)
    • J.S. Rohrer, Q.T. Islam, G.D. Watt, D.E. Sayers, and E.C. Theil Iron environment in ferritin with large amounts of phosphate from Azotobacter vinelandii and horse spleen, analyzed using extended X-ray absorption fine structure (EXAFS) Biochemistry 29 1990 259 264
    • (1990) Biochemistry , vol.29 , pp. 259-264
    • Rohrer, J.S.1    Islam, Q.T.2    Watt, G.D.3    Sayers, D.E.4    Theil, E.C.5
  • 10
    • 0031763106 scopus 로고    scopus 로고
    • Iron storage in bacteria
    • S. Andrews Iron storage in bacteria Adv. Microb. Physiol. 40 1998 282351
    • (1998) Adv. Microb. Physiol. , vol.40 , pp. 282351
    • Andrews, S.1
  • 13
    • 0024245282 scopus 로고
    • Mechanism of ferritin iron uptake: Activity of the H-chain and deletion mapping of the ferro-oxidase site
    • S. Levi, A. Luzzago, G. Cesareni, A. Cozzi, F. Franceschenelli, A. Albertini, and P. Arosio Mechanism of ferritin iron uptake: activity of the H-chain and deletion mapping of the ferro-oxidase site 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    Franceschenelli, F.5    Albertini, A.6    Arosio, P.7
  • 14
    • 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 Biol. Chem. 266 1991 19965 19970
    • (1991) Biol. Chem. , vol.266 , pp. 19965-19970
    • Xu, B.1    Chasteen, N.D.2
  • 15
    • 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
  • 16
    • 0027729455 scopus 로고
    • Formation of iron (III)-tyrosinate is the fastest reaction observed in ferritin
    • G.S. Waldo, and E.C. Theil Formation of iron (III)-tyrosinate is the fastest reaction observed in ferritin Biochemistry 32 1993 13262 13269
    • (1993) Biochemistry , vol.32 , pp. 13262-13269
    • Waldo, G.S.1    Theil, E.C.2
  • 17
    • 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
  • 18
    • 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
  • 19
    • 0034254215 scopus 로고    scopus 로고
    • Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua
    • X. Yang, E. Chiancone, S. Stefanini, A. Ilari, and N.D. Chasteen Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua Biochem. J. 349 2000 783 786
    • (2000) Biochem. J. , vol.349 , pp. 783-786
    • Yang, X.1    Chiancone, E.2    Stefanini, S.3    Ilari, A.4    Chasteen, N.D.5
  • 20
    • 0035916893 scopus 로고    scopus 로고
    • Hydrogen peroxide formation during iron deposition in horse spleen ferritin using O2 as an oxidant
    • S. Lindsay, D. Brosnahan, and G.D. Watt Hydrogen peroxide formation during iron deposition in horse spleen ferritin using O2 as an oxidant Biochemistry 40 2001 3340 3347
    • (2001) Biochemistry , vol.40 , pp. 3340-3347
    • Lindsay, S.1    Brosnahan, D.2    Watt, G.D.3
  • 21
    • 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
  • 23
    • 0037069409 scopus 로고    scopus 로고
    • Stoichiometric production of hydrogen peroxide and parallel formation of ferric multimers through decay of the diferric-peroxo complex, the first detectable intermediate in ferritin mineralization
    • G.N.L. Jameson, W. Jin, C. Krebs, A.S. Perreira, P. Tavares, X. Liu, E.C. Theil, and B.H. Huynh Stoichiometric production of hydrogen peroxide and parallel formation of ferric multimers through decay of the diferric-peroxo complex, the first detectable intermediate in ferritin mineralization Biochemistry 41 2002 13435 13443
    • (2002) Biochemistry , vol.41 , pp. 13435-13443
    • Jameson, G.N.L.1    Jin, W.2    Krebs, C.3    Perreira, A.S.4    Tavares, P.5    Liu, X.6    Theil, E.C.7    Huynh, B.H.8
  • 24
    • 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
  • 28
    • 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. Sevi, 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    Sevi, S.4    Janus-Chandler, C.5    Chasteen, N.D.6
  • 30
    • 0024384482 scopus 로고
    • Expression and structural and functional properties of human ferritin L-chain from Escherichia Coli
    • S. Levi, J. Salfeld, F. Franceschinelli, A. Cozzi, M.H. Dorner, and P. Arosio Expression and structural and functional properties of human ferritin L-chain from Escherichia Coli Biochemistry 28 1989 5179 5184
    • (1989) Biochemistry , vol.28 , pp. 5179-5184
    • Levi, S.1    Salfeld, J.2    Franceschinelli, F.3    Cozzi, A.4    Dorner, M.H.5    Arosio, P.6
  • 31
    • 0033616738 scopus 로고    scopus 로고
    • Redox reactivity of animal apoferritins and apoheteropolymers assembled from recombinant heavy and light human chain ferritins
    • J.l. Johnson, D.C. Norcross, P. Arosio, R.B. Frankel, and G.D. Watt Redox reactivity of animal apoferritins and apoheteropolymers assembled from recombinant heavy and light human chain ferritins Biochemistry 38 1999 4089 4096
    • (1999) Biochemistry , vol.38 , pp. 4089-4096
    • Johnson, J.L.1    Norcross, D.C.2    Arosio, P.3    Frankel, R.B.4    Watt, G.D.5
  • 32
  • 33
    • 0027363945 scopus 로고
    • Further characterization of the redox and spectroscopic properties of Azotobacter vinelandii ferritin
    • G.D. Watt, J.W. McDonald, C.-H. Chiu, and K.R.N. Reddy Further characterization of the redox and spectroscopic properties of Azotobacter vinelandii ferritin J. Inorg. Biochem. 5 1 1993 745 758
    • (1993) J. Inorg. Biochem. , vol.5 , Issue.1 , pp. 745-758
    • Watt, G.D.1    McDonald, J.W.2    Chiu, C.-H.3    Reddy, K.R.N.4
  • 35
    • 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. Pereira, W. Small, C. Krebs, P. Tavares, D. Edmondson, E. Theil, and B. 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.1    Small, W.2    Krebs, C.3    Tavares, P.4    Edmondson, D.5    Theil, E.6    Huynh, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.