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Volumn 31, Issue 10, 1999, Pages 995-1000

Ferrochelatase

Author keywords

[No Author keywords available]

Indexed keywords

FERROCHELATASE; FERROUS ION; PORPHYRIN; PROTOPORPHYRIN;

EID: 0032832181     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(99)00066-7     Document Type: Article
Times cited : (53)

References (15)
  • 2
    • 0001979473 scopus 로고
    • Conversion of coproporphyrinogen to protoheme in higher eukaryotes and bacteria: Terminal three enzymes
    • H.A. Dailey. New York: McGraw-Hill
    • Dailey H.A. Conversion of coproporphyrinogen to protoheme in higher eukaryotes and bacteria: terminal three enzymes. Dailey H.A. Biosynthesis of Heme and Chlorophylls. 1990;123-161 McGraw-Hill, New York.
    • (1990) Biosynthesis of Heme and Chlorophylls , pp. 123-161
    • Dailey, H.A.1
  • 4
    • 0026576256 scopus 로고
    • Structure of the human ferrochelatase gene: Exon/intron gene organization and location of the gene to chromosome 18
    • Taketani S., Inazawa J., Nakahashi Y., Abe T., Tokunaga R. Structure of the human ferrochelatase gene: exon/intron gene organization and location of the gene to chromosome 18. Eur. J. Biochem. 205:1992;217-222.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 217-222
    • Taketani, S.1    Inazawa, J.2    Nakahashi, Y.3    Abe, T.4    Tokunaga, R.5
  • 6
    • 0028047783 scopus 로고
    • Human ferrochelatase is an iron-sulfur protein
    • Dailey H.A., Finnegan M.G., Johnson M.K. Human ferrochelatase is an iron-sulfur protein. Biochemistry. 33:1994;403-407.
    • (1994) Biochemistry , vol.33 , pp. 403-407
    • Dailey, H.A.1    Finnegan, M.G.2    Johnson, M.K.3
  • 7
    • 0031573454 scopus 로고    scopus 로고
    • Crystal structure of ferrochelatase: The terminal enzyme in heme biosynthesis
    • Al-Karadaghi S., Hansson M., Nikonov S., Jönsson B., Hederstedt L. Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis. Structure. 5:1997;1501-1510.
    • (1997) Structure , vol.5 , pp. 1501-1510
    • Al-Karadaghi, S.1    Hansson, M.2    Nikonov, S.3    Jönsson, B.4    Hederstedt, L.5
  • 8
    • 0029999490 scopus 로고    scopus 로고
    • Functional necessity and physicochemical characteristics of the [2Fe-2S] cluster in mammalian ferrochelatase
    • Lloyd S.G., Franco R., Moura J.J.G., Moura I., Ferreira G.C., Huynh B.H. Functional necessity and physicochemical characteristics of the [2Fe-2S] cluster in mammalian ferrochelatase. J. Am. Chem. Soc. 118:1996;9892-9900.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9892-9900
    • Lloyd, S.G.1    Franco, R.2    Moura, J.J.G.3    Moura, I.4    Ferreira, G.C.5    Huynh, B.H.6
  • 9
    • 0032575499 scopus 로고    scopus 로고
    • Evidence that the fourth ligand to the [2Fe-2S] cluster in animal ferrochelatase is a cysteine: Characterization of the enzyme from Drosophila melanogaster
    • Sellers V.M., Wang K.F., Johnson M.K., Dailey H.A. Evidence that the fourth ligand to the [2Fe-2S] cluster in animal ferrochelatase is a cysteine: characterization of the enzyme from Drosophila melanogaster. J. Biol. Chem. 273:1998;22311-22316.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22311-22316
    • Sellers, V.M.1    Wang, K.F.2    Johnson, M.K.3    Dailey, H.A.4
  • 10
    • 0028029512 scopus 로고
    • Site-directed mutagenesis of human ferrochelatase: Identification of histidine-263 as a binding site for metal ions
    • Kohno H., Okuda M., Furukawa T., Tokunaga R., Taketani S. Site-directed mutagenesis of human ferrochelatase: identification of histidine-263 as a binding site for metal ions. Biochim. Biophys. Acta. 1209:1994;95-100.
    • (1994) Biochim. Biophys. Acta , vol.1209 , pp. 95-100
    • Kohno, H.1    Okuda, M.2    Furukawa, T.3    Tokunaga, R.4    Taketani, S.5
  • 11
    • 0029974210 scopus 로고    scopus 로고
    • Probing the active-site site residues in Saccharomyces cerevisiae ferrochelatase by directed mutagenesis
    • Gora M., Grzybowska E., Rytka J., Labbe-Bois R. Probing the active-site site residues in Saccharomyces cerevisiae ferrochelatase by directed mutagenesis. J. Biol. Chem. 271:1996;11810-11816.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11810-11816
    • Gora, M.1    Grzybowska, E.2    Rytka, J.3    Labbe-Bois, R.4
  • 12
    • 0028840289 scopus 로고
    • Characterization of the iron-binding site in mammalian ferrochelatase by kinetic and Mössbauer methods
    • Franco R., Moura I., Moura J.J.G., Lloyd S., Huynh B.H., Forbes W.S., Ferreira G.C. Characterization of the iron-binding site in mammalian ferrochelatase by kinetic and Mössbauer methods. J. Biol. Chem. 270:1995;26352-26357.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26352-26357
    • Franco, R.1    Moura, I.2    Moura, J.J.G.3    Lloyd, S.4    Huynh, B.H.5    Forbes, W.S.6    Ferreira, G.C.7
  • 13
    • 0031979898 scopus 로고    scopus 로고
    • Iron and copper transport in yeast and its relevance to human disease
    • Askwith C., Kaplan J. Iron and copper transport in yeast and its relevance to human disease. Trends Biochem. Sci. 23:1998;135-138.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 135-138
    • Askwith, C.1    Kaplan, J.2
  • 14
    • 0345515979 scopus 로고    scopus 로고
    • Alternative modes of substrate distortion in enzyme and antibody catalyzed ferochelatase reactions
    • Blackwood M.E. Jr., Rush T.S. III, Romesberg F., Schultz P.G., Spiro T.G. Alternative modes of substrate distortion in enzyme and antibody catalyzed ferochelatase reactions. Biochemistry. 37:1998;779-782.
    • (1998) Biochemistry , vol.37 , pp. 779-782
    • Blackwood M.E., Jr.1    Rush T.S. III2    Romesberg, F.3    Schultz, P.G.4    Spiro, T.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.