The universal mechanism for iron translocation to the ferroxidase site in ferritin, which is mediated by the well conserved transit site

Biochemical and Biophysical Research Communications

Volumn 400, Issue 1, 2010, Pages 94-99

  Masuda, Taro ^a   Goto, Fumiyuki ^b   Yoshihara, Toshihiro ^b   Mikami, Bunzo ^a  

^a KYOTO UNIVERSITY   (Japan)

^b CENTRAL RESEARCH INSTITUTE OF ELECTRIC POWER INDUSTRY   (Japan)

Author keywords

Ferritin; Ferroxidase site; Metal sequestration; Transit site

Indexed keywords

CERULOPLASMIN; FERRITIN; FTH1 PROTEIN, HUMAN; IRON;

ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HUMAN; HYDROGEN BOND; IRON TRANSPORT; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; CHEMISTRY; GENETICS; METABOLISM; OXIDATION REDUCTION REACTION; PROTEIN CONFORMATION;

CERULOPLASMIN; FERRITINS; HUMANS; IRON; OXIDATION-REDUCTION; PROTEIN CONFORMATION;

VERTEBRATA;

EID: 79956187524     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.08.017     Document Type: Article

References (21)

1. Harrison P.M., Arosio P. The ferritins: molecular properties iron storage function and cellular regulation. Biochim. Biophys. Acta 1996, 1275:161-203.
2. Theil E.C. Ferrit structure, gene regulation, and cellular function in animals, plants and microorganisms. Ann. Rev. Biochem. 1987, 56:289-315.
3. Yablonski M.J., Theil E.C. A possible role for the conserved trimer interface of ferritin in iron incorporation. Biochemistry 1992, 31:9680-9684.
4. Lawson D.M., Artymiuk P.J., Yewdall S.J., Smith J.M.A., Livingstone J.C., Treffry A., Luzzago A., Levi S., Arosio P., Cesareni G., Thomas C.D., Shaw W.V., Harrison P.M. Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. Nature 1991, 349:541-544.
5. Sun S., Arosio P., Levi S., Chasteen N.D. Ferroxidase kinetics of human liver recombinant apoferritin H-chain apoferritin and site-directed mutants. Biochemistry 1993, 32:9362-9369.
6. Yang X., Chen-Barrett Y., Arosio P., Chasteen N.D. Reaction paths of iron oxidation and hydrolysis in horse spleen and recombinant human ferritins. Biochemistry 1998, 37:9743-9750.
7. Jameson G.N., Jin W., Krebs C., Perreira A.S., Tavares P., Liu X., Theil E.C., Huynh B.H. 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 2002, 41:13435-13443.
8. Liu X., Theil E.C. Ferritin reactions: direct identification of the site for the diferric peroxide reaction intermediate. Proc. Natl. Acad. Sci. USA 2004, 101:8557-8562.
9. Turanoa P., Lallia D., Fellia I.C., Theil E.C., Bertini I. NMR reveals pathway for ferric mineral precursors to the central cavity of ferritin. Proc. Natl. Acad. Sci. USA 2010, 107:545-550.
10. Masuda T., Goto F., Yoshihara T., Mikami B. Crystal structure of plant ferritin reveals a novel metal binding site that functions as a transit site for metal transfer in ferritin. J. Biol. Chem. 2010, 285:4049-4059.
11. Santambrogio P., Cozzi A., Levi S., Rovida E., Magni F., Albertini A., Arosio P. Functional and immunological analysis of recombinant mouse H- and L-ferritins from Escherichia coli. Protein Expression Purif. 2000, 19:212-218.
12. Masuda T., Goto F., Yoshihara T., Ezure T., Suzuki T., Kobayashi S., Shikata M., Utsumi S. Construction of homo- and heteropolymers of plant ferritin subunits using an in vitro protein expression system. Protein Expression Purif. 2007, 56:237-246.
13. Chasteen N.D., Theil E.C. Iron binding by horse spleen apoferritin. a vanadyl(IV) EPR spin probe study. J. Biol. Chem. 1982, 257:7672-7677.
14. Pace C.N., Vajdos F., Fee L., Grimsley G., Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 1995, 4:2411-2423.
15. Otwinowski Z., Minor W. Processing of X-ray crystallographic data collected in oscillation mode. Methods Enzymol. 1997, 276:307-326.
16. Murshudov G.N., Vagin A.A., Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr., Sect. D: Biol. Crystallogr. 1997, 53:240-255.
17. Adams P.D., Grosse-Kunstleve R.W., Hung L.W., Ioerger T.R., McCoy A.J., Moriarty N.W., Read R.J., Sacchettini J.C., Sauter N.K., Terwilliger T.C. PHENIX: building new software for automated crystallographic structure determination. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2002, 58:1948-1954.
18. Emsley P., Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2004, 60:2126-2132.
19. Toussaint L., Bertrand L., Hue L., Crichton R.R., Declercq J.P. High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites. J. Mol. Biol. 2007, 365:440-452.
20. Bou-Abdallah F., Zhao G., Biasiotto G., Poli M., Arosio P., Chasteen N.D. Facilitated diffusion of iron(II) and dioxygen substrates into human H-chain ferritin. A fluorescence and absorbance study employing the ferroxidase center substitution Y34W. J. Am. Chem. Soc. 2008, 130:17801-17811.
21. Ueno T., Abe M., Hirata K., Abe S., Suzuki M., Shimizu N., Yamamoto M., Takata M., Watanabe Y. Process of accumulation of metal ions on the interior surface of apo-ferritin: crystal structures of a series of apo-ferritins containing variable quantities of Pd(II) ions. J. Am. Chem. Soc. 2009, 131:5094-5100.