메뉴 건너뛰기




Volumn 42, Issue 13, 2003, Pages 3701-3707

Investigation of the mechanism of iron release from the C-lobe of human serum transferrin: Mutational analysis of the role of a pH sensitive triad

Author keywords

[No Author keywords available]

Indexed keywords

IRON; PH EFFECTS; PROTEINS;

EID: 0037426355     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi027071q     Document Type: Article
Times cited : (58)

References (33)
  • 1
    • 0000242640 scopus 로고
    • The evolution of transferrin
    • Williams, J. (1982) The evolution of transferrin, TIBS 7, 394-397.
    • (1982) TIBS , vol.7 , pp. 394-397
    • Williams, J.1
  • 6
    • 0344492012 scopus 로고
    • Difference between the two iron-binding sites of transferrin
    • Princiotto, J. V., and Zapolski, E. J. (1975) Difference between the two iron-binding sites of transferrin, J. Biol. Chem. 253, 1930-1937.
    • (1975) J. Biol. Chem. , vol.253 , pp. 1930-1937
    • Princiotto, J.V.1    Zapolski, E.J.2
  • 7
    • 0017230087 scopus 로고
    • The effect of pH upon human transferrin: Selective labeling of the two iron-binding sites
    • Lestas, A. N. (1976) The effect of pH upon human transferrin: selective labeling of the two iron-binding sites, Br. J. Haematol. 32, 341-350.
    • (1976) Br. J. Haematol. , vol.32 , pp. 341-350
    • Lestas, A.N.1
  • 8
    • 0020385854 scopus 로고
    • The effect of pH on the kinetics of iron release from human transferrin
    • Baldwin, D. A., De Sousa, D. M. R., and Von Wandruszka, R. M. A. (1982) The Effect of pH on the Kinetics of Iron Release from Human Transferrin, Biochim. Biophys. Acta 719, 140-146.
    • (1982) Biochim. Biophys. Acta , vol.719 , pp. 140-146
    • Baldwin, D.A.1    De Sousa, D.M.R.2    Von Wandruszka, R.M.A.3
  • 9
    • 0002148929 scopus 로고    scopus 로고
    • Molecular aspects of release of iron from transferrins
    • Templeton, D. M., Ed., Marcel Dekker, Inc., New York
    • He, Q.-Y., and Mason, A. B. (2002) Molecular aspects of release of iron from transferrins, in Molecular and Cellular Iron Transport (Templeton, D. M., Ed.) pp 95-123, Marcel Dekker, Inc., New York.
    • (2002) Molecular and Cellular Iron Transport , pp. 95-123
    • He, Q.-Y.1    Mason, A.B.2
  • 10
    • 0033609501 scopus 로고    scopus 로고
    • Dual role of Lys206-Lys296 interaction in human transferrin N-lobe: Iron-release trigger and anion-binding site
    • He, Q.-Y., Mason, A. B., Tam, B. M., MacGillivray, R. T. A., and Woodworth, R. C. (1999) Dual role of Lys206-Lys296 interaction in human transferrin N-lobe: Iron-release trigger and anion-binding site, Biochemistry 38, 9704-9711.
    • (1999) Biochemistry , vol.38 , pp. 9704-9711
    • He, Q.-Y.1    Mason, A.B.2    Tam, B.M.3    MacGillivray, R.T.A.4    Woodworth, R.C.5
  • 11
    • 0035852806 scopus 로고    scopus 로고
    • Crystal structures and iron release properties of mutants (K206A and K296A) that abolish the dilysine interaction in the N-lobe of human transferrin
    • Nurizzo, D., Baker, H. M., He, Q.-Y., MacGillivray, R. T. A., Mason, A. B., Woodworth, R. C., and Baker, E. N. (2001) Crystal structures and iron release properties of mutants (K206A and K296A) that abolish the dilysine interaction in the N-lobe of human transferrin, Biochemistry 40, 1616-1623.
    • (2001) Biochemistry , vol.40 , pp. 1616-1623
    • Nurizzo, D.1    Baker, H.M.2    He, Q.-Y.3    MacGillivray, R.T.A.4    Mason, A.B.5    Woodworth, R.C.6    Baker, E.N.7
  • 12
    • 0032578428 scopus 로고    scopus 로고
    • Iron release is reduced by mutations of lysine 206 and 296 in recombinant N-terminal half-transferrin
    • Steinlein, L. M., Ligman, C. M., Kessler, S., and Ikeda, R. A. (1998) Iron release is reduced by mutations of lysine 206 and 296 in recombinant N-terminal half-transferrin, Biochemistry 37, 13696-13703.
    • (1998) Biochemistry , vol.37 , pp. 13696-13703
    • Steinlein, L.M.1    Ligman, C.M.2    Kessler, S.3    Ikeda, R.A.4
  • 13
    • 0032491165 scopus 로고    scopus 로고
    • Kinetic studies on the removal of iron and aluminum from recombinant and site-directed mutant N-lobe half transferrins
    • Li, Y. J., Harris, W. R., Maxwell, A., MacGillivray, R. T. A., and Brown, T. (1998) Kinetic studies on the removal of iron and aluminum from recombinant and site-directed mutant N-lobe half transferrins, Biochemistry 37, 14157-14166.
    • (1998) Biochemistry , vol.37 , pp. 14157-14166
    • Li, Y.J.1    Harris, W.R.2    Maxwell, A.3    MacGillivray, R.T.A.4    Brown, T.5
  • 14
    • 0027360843 scopus 로고
    • Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: Implications for transferrin iron release
    • Dewan, J. C., Mikami, B., Hirose, M., and Sacchettini, J. C. (1993) Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: Implications for transferrin iron release, Biochemistry 32, 11963-11968.
    • (1993) Biochemistry , vol.32 , pp. 11963-11968
    • Dewan, J.C.1    Mikami, B.2    Hirose, M.3    Sacchettini, J.C.4
  • 16
    • 0037022176 scopus 로고    scopus 로고
    • A new method for obtaining human transferrin C-lobe in the native conformation: Preparation and properties
    • Zak, O., and Aisen, P. (2002) A new method for obtaining human transferrin C-lobe in the native conformation: preparation and properties, Biochemistry 41, 1647-1653.
    • (2002) Biochemistry , vol.41 , pp. 1647-1653
    • Zak, O.1    Aisen, P.2
  • 18
    • 0034813966 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant nonglycosylated human serum transferrin containing a c-terminal hexahistidine tag
    • Mason, A. B., He, Q.-Y., Adams, T. E., Gumerov, D. R., Kaltashov, I. A., Nguyen, V., and MacGillivray, R. T. A. (2001) Expression, Purification, and Characterization of Recombinant Nonglycosylated Human Serum Transferrin Containing a c-terminal Hexahistidine Tag, Protein Expression Purif. 23, 142-150.
    • (2001) Protein Expression Purif. , vol.23 , pp. 142-150
    • Mason, A.B.1    He, Q.-Y.2    Adams, T.E.3    Gumerov, D.R.4    Kaltashov, I.A.5    Nguyen, V.6    MacGillivray, R.T.A.7
  • 19
    • 0034664990 scopus 로고    scopus 로고
    • The chloride effect is related to anion binding in determining the rate of iron release from the human transferrin N-lobe
    • He, Q. Y., Mason, A. B., Nguyen, V., MacGillivray, R. T. A., and Woodworth, R. C. (2000) The chloride effect is related to anion binding in determining the rate of iron release from the human transferrin N-lobe, Biochem. J. 350, 909-915.
    • (2000) Biochem. J. , vol.350 , pp. 909-915
    • He, Q.Y.1    Mason, A.B.2    Nguyen, V.3    MacGillivray, R.T.A.4    Woodworth, R.C.5
  • 20
    • 0034692904 scopus 로고    scopus 로고
    • Transferrins: Iron release from lactoferrin
    • Abdallah, F. B., and Chahine, J. M. E. (2000) Transferrins: Iron release from lactoferrin, J. Mol. Biol. 303, 255-266.
    • (2000) J. Mol. Biol. , vol.303 , pp. 255-266
    • Abdallah, F.B.1    Chahine, J.M.E.2
  • 22
    • 0000465641 scopus 로고
    • Mechanism of iron release from human serum c-terminal monoferric transferrin to pyrophosphate: Kinetic discrimination between alternative mechanisms
    • Egan, T. J., Ross, D. C., Purves, L. R., and Adams, P. A. (1992) Mechanism of Iron Release from Human Serum C-Terminal Monoferric Transferrin to Pyrophosphate: Kinetic Discrimination Between Alternative Mechanisms, Inorg. Chem. 31, 1994-1998.
    • (1992) Inorg. Chem. , vol.31 , pp. 1994-1998
    • Egan, T.J.1    Ross, D.C.2    Purves, L.R.3    Adams, P.A.4
  • 23
    • 0030774732 scopus 로고    scopus 로고
    • A kinetically active site in the C-lobe of human transferrin
    • Zak, O., Tam, B., MacGillivray, R. T. A., and Aisen, P. (1997) A kinetically active site in the C-lobe of human transferrin, Biochemistry 36, 11036-11043.
    • (1997) Biochemistry , vol.36 , pp. 11036-11043
    • Zak, O.1    Tam, B.2    MacGillivray, R.T.A.3    Aisen, P.4
  • 25
    • 0036006760 scopus 로고    scopus 로고
    • The crystal and molecular structures of diferric porcine and rabbit serum transferrins at resolutions of 2.15 and 2.60 A, respectively
    • Hall, D. R., Hadden, J. M., Leonard, G. A., Bailey, S., Neu, M., Winn, M., and Lindley, P. F. (2002) The crystal and molecular structures of diferric porcine and rabbit serum transferrins at resolutions of 2.15 and 2.60 A, respectively, Acta Crystallogr.., Sect. D 58, 70-80.
    • (2002) Acta Crystallogr., Sect. D. , vol.58 , pp. 70-80
    • Hall, D.R.1    Hadden, J.M.2    Leonard, G.A.3    Bailey, S.4    Neu, M.5    Winn, M.6    Lindley, P.F.7
  • 26
    • 0035839074 scopus 로고    scopus 로고
    • a that is elevated upon binding of sulphate
    • a that is elevated upon binding of sulphate, FEBS Lett. 503, 30-34.
    • (2001) FEBS Lett. , vol.503 , pp. 30-34
    • Clarkson, J.1    Smith, D.A.2
  • 27
    • 0000372669 scopus 로고
    • Kinetics of iron removal from human serum monoferric transferrins by citrate
    • Marques, H. M., Watson, D. L., and Egan, T. J. (1991) Kinetics of Iron Removal from Human Serum Monoferric Transferrins by Citrate, Inorg. Chem. 30, 3758-3762.
    • (1991) Inorg. Chem. , vol.30 , pp. 3758-3762
    • Marques, H.M.1    Watson, D.L.2    Egan, T.J.3
  • 28
    • 0028895477 scopus 로고
    • Release of iron from C-terminal monoferric transferrin to phosphate and pyrophosphate at pH 5.5 proceeds through two pathways
    • Marques, H. M., Walton, T., and Egan, T. J. (1995) Release of iron from C-terminal monoferric transferrin to phosphate and pyrophosphate at pH 5.5 proceeds through two pathways, J. Inorg. Biochem. 57, 11-21.
    • (1995) J. Inorg. Biochem. , vol.57 , pp. 11-21
    • Marques, H.M.1    Walton, T.2    Egan, T.J.3
  • 29
    • 0002511466 scopus 로고    scopus 로고
    • GeneDoc: Analysis and visualization of genetic variation
    • Nicholas, K. B., Nicholas, H. B., and Deerfield, D. W. I. (1997) GeneDoc: Analysis and Visualization of Genetic Variation, EMBNEW NEWS 4, 14.
    • (1997) EMBNEW News , vol.4 , pp. 14
    • Nicholas, K.B.1    Nicholas, H.B.2    Deerfield, D.W.I.3
  • 30
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of Molscript which includes greatly enhanced coloring capabilities
    • Esnouf, R. M. (1997) An extensively modified version of Molscript which includes greatly enhanced coloring capabilities, J. Mol. Graphics 15, 133-138.
    • (1997) J. Mol. Graphics , vol.15 , pp. 133-138
    • Esnouf, R.M.1
  • 31
    • 0026244229 scopus 로고
    • Molscript; A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P, (1991) Molscript; A program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 32
    • 0000913086 scopus 로고
    • A fast algorithm for rendering - Filling molecular pictures
    • Bacon, D. J., and Anderson, W. F. (1988) A fast algorithm for rendering - filling molecular pictures, J. Mol. Graphics 6, 219-220.
    • (1988) J. Mol. Graphics , vol.6 , pp. 219-220
    • Bacon, D.J.1    Anderson, W.F.2
  • 33
    • 0028057108 scopus 로고
    • Raster3D, version 2.0: A program for photorealistic molecular graphics
    • Merritt, E, A., and Murphy, M. E. P. (1994) Raster3D, version 2.0: A program for photorealistic molecular graphics, Acta Crystallogr., Sect. D 50, 869-873.
    • (1994) Acta Crystallogr., Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.