메뉴 건너뛰기




Volumn 91, Issue 2, 2009, Pages 230-239

Two different H-type subunits from pea seed (Pisum sativum) ferritin that are responsible for fast Fe(II) oxidation

Author keywords

Ferritin; Ferroxidase site; Iron oxidation; MALDI TOF MS; Pea seed

Indexed keywords

AMINO ACID SEQUENCE; DATABASES, FACTUAL; FERRITINS; IRON; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; OXIDATION-REDUCTION; PEAS; PEPTIDE MAPPING; PROTEIN SUBUNITS; SEEDS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TANDEM MASS SPECTROMETRY;

EID: 58849146095     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2008.09.008     Document Type: Article
Times cited : (41)

References (27)
  • 1
    • 0030608152 scopus 로고    scopus 로고
    • Ferritins: molecular properties, iron storage function and cellular regulation
    • Harrison P.M., and Arosio P. 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
    • Chasteen N.D., and Harrison P.M. 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
    • 15244339209 scopus 로고    scopus 로고
    • Ferritins: dynamic management of biological iron and oxygen chemistry
    • Liu X., and Theil E.C. Ferritins: dynamic management of biological iron and oxygen chemistry. Acc. Chem. Res. 38 (2005) 167-175
    • (2005) Acc. Chem. Res. , vol.38 , pp. 167-175
    • Liu, X.1    Theil, E.C.2
  • 5
    • 0037452863 scopus 로고    scopus 로고
    • Multiple pathways for mineral core formation in mammalian apoferritin. The role of hydrogen peroxide
    • Zhao G., Bou-Abdallah F., Arosio P., Levi S., Janus-Chandler C., and Chasteen N.D. 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
  • 6
    • 0000823059 scopus 로고    scopus 로고
    • Identification of catalytic residues involved in iron uptake by L-chain ferritins
    • Crichton R.R., Herbas A., Chavez-Alba O., and Roland F. 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
  • 7
    • 0029410771 scopus 로고
    • Formation of the ferritin iron mineral occurs in plastids: an X-ray absorption spectroscopy (EXAFS) study
    • Waldo G.S., Wright E., Wang Z.-H., Briat J.-F., Theil E.C., and Sayers D.E. Formation of the ferritin iron mineral occurs in plastids: an X-ray absorption spectroscopy (EXAFS) study. Plant Physiol 109 (1995) 797-802
    • (1995) Plant Physiol , vol.109 , pp. 797-802
    • Waldo, G.S.1    Wright, E.2    Wang, Z.-H.3    Briat, J.-F.4    Theil, E.C.5    Sayers, D.E.6
  • 8
    • 0027056014 scopus 로고
    • Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin
    • Lobréaux S., Yewdall S.J., Briat J.-F., and Harrison P.M. Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin. Biochem. J. 288 (1992) 931-939
    • (1992) Biochem. J. , vol.288 , pp. 931-939
    • Lobréaux, S.1    Yewdall, S.J.2    Briat, J.-F.3    Harrison, P.M.4
  • 9
    • 0028854811 scopus 로고
    • Purification and characterization of recombinant pea-seed ferritins expressed in Escherichia coli: influence of N-terminus deletions on protein solubility and core formation in vitro
    • van Wuytswinkel O., Savino G., and Briat J.F. Purification and characterization of recombinant pea-seed ferritins expressed in Escherichia coli: influence of N-terminus deletions on protein solubility and core formation in vitro. Biochem. J. 305 (1995) 253-261
    • (1995) Biochem. J. , vol.305 , pp. 253-261
    • van Wuytswinkel, O.1    Savino, G.2    Briat, J.F.3
  • 10
    • 0025186372 scopus 로고
    • Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean
    • Ragland M., Briat J.F., Gagnon J., Laulhere J.P., Massenet O., and Theil E.C. Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean. J. Biol. Chem. 265 (1990) 18339-18344
    • (1990) J. Biol. Chem. , vol.265 , pp. 18339-18344
    • Ragland, M.1    Briat, J.F.2    Gagnon, J.3    Laulhere, J.P.4    Massenet, O.5    Theil, E.C.6
  • 11
    • 0024977973 scopus 로고
    • Mechanism of the transition from plant ferritin to phytosiderin
    • Laulhere J.P., Laboure A.M., and Briat J.F. Mechanism of the transition from plant ferritin to phytosiderin. J. Biol. Chem. 264 (1989) 3629-3635
    • (1989) J. Biol. Chem. , vol.264 , pp. 3629-3635
    • Laulhere, J.P.1    Laboure, A.M.2    Briat, J.F.3
  • 12
    • 0035379652 scopus 로고    scopus 로고
    • A novel plant ferritin subunit from soybean that is related to a mechanism in iron release
    • Masuda T., Goto F., and Yoshihara T. A novel plant ferritin subunit from soybean that is related to a mechanism in iron release. J. Biol. Chem. 276 (2001) 19575-19579
    • (2001) J. Biol. Chem. , vol.276 , pp. 19575-19579
    • Masuda, T.1    Goto, F.2    Yoshihara, T.3
  • 14
    • 46449119266 scopus 로고    scopus 로고
    • Expression and purification of intact and functional soybean (Glycine max) seed ferritin complex in Escherichia coli
    • Dong X., Tang B., Li J., Xu Q., Fang S., and Hua Z. Expression and purification of intact and functional soybean (Glycine max) seed ferritin complex in Escherichia coli. J. Microbiol. Biotechnol 18 (2008) 299-307
    • (2008) J. Microbiol. Biotechnol , vol.18 , pp. 299-307
    • Dong, X.1    Tang, B.2    Li, J.3    Xu, Q.4    Fang, S.5    Hua, Z.6
  • 15
    • 0026535851 scopus 로고
    • Mechanism of catalysis of Fe(II) oxidation by ferritin H-chains
    • Treffry A., Hirzmann J., Yewdall S.J., and Harrison P.M. Mechanism of catalysis of Fe(II) oxidation by ferritin H-chains. FEBS Lett. 302 (1992) 108-112
    • (1992) FEBS Lett. , vol.302 , pp. 108-112
    • Treffry, A.1    Hirzmann, J.2    Yewdall, S.J.3    Harrison, P.M.4
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 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. 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
    • 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. 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
  • 20
    • 15744368011 scopus 로고    scopus 로고
    • Origin of the unusual kinetics of iron deposition in human H-chain ferritin
    • Bou-Abdallah F., Zhao G., Mayne H.R., Arosio P., and Chasteen N.D. 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
  • 22
    • 0000239991 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes containing binuclear non-heme iron clusters
    • Wallar B.J., and Lipscomb J.D. Dioxygen activation by enzymes containing binuclear non-heme iron clusters. Chem. Rev. 96 (1996) 2625-2658
    • (1996) Chem. Rev. , vol.96 , pp. 2625-2658
    • Wallar, B.J.1    Lipscomb, J.D.2
  • 23
    • 0026887039 scopus 로고
    • Iron induces ferritin synthesis in maize plantlets
    • Lobréaux S., Massenet O., and Briat J.F. Iron induces ferritin synthesis in maize plantlets. Plant Mol. Biol. 19 (1992) 563-575
    • (1992) Plant Mol. Biol. , vol.19 , pp. 563-575
    • Lobréaux, S.1    Massenet, O.2    Briat, J.F.3
  • 24
    • 0027267646 scopus 로고
    • Functional genes found for three different plant ferritin subunits in the legume, Vigna unguiculata
    • Wicks R.E., and Entsch B. Functional genes found for three different plant ferritin subunits in the legume, Vigna unguiculata. Biochem. Biophys. Res. Commun 192 (1993) 813-819
    • (1993) Biochem. Biophys. Res. Commun , vol.192 , pp. 813-819
    • Wicks, R.E.1    Entsch, B.2
  • 26
    • 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. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.