Iron core mineralisation in prokaryotic ferritins

Biochimica et Biophysica Acta - General Subjects

Volumn 1800, Issue 8, 2010, Pages 732-744

  Le Brun, Nick E ^a   Crow, Allister ^a   Murphy, Michael E P ^b   Mauk, A Grant ^b   Moore, Geoffrey R ^a  

^a UNIVERSITY OF EAST ANGLIA   (United Kingdom)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Bacterioferritin; Diiron centre; Ferroxidase; Ftn; Heme; Iron; Mineralisation

Indexed keywords

BACTERIOFERRITIN; CERULOPLASMIN; FERRIC OXIDE; FERRITIN; IRON;

ARCHAEBACTERIUM; BIOAVAILABILITY; CATALYSIS; KINETICS; MINERALIZATION; NANOPORE; NONHUMAN; OXIDATION; PRIORITY JOURNAL; PROKARYOTE; REVIEW; SPECTROSCOPY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATALYTIC DOMAIN; FERRIC COMPOUNDS; FERRITINS; IRON; MINERALS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROKARYOTIC CELLS; SEQUENCE HOMOLOGY, AMINO ACID;

ARCHAEA; BACTERIA (MICROORGANISMS); PROKARYOTA;

EID: 77953808958     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2010.04.002     Document Type: Review

References (113)

1. Aisen P., Enns C., Wessling-Resnick M. Chemistry and biology of eukaryotic iron metabolism. Int. J. Biochem. Cell Biol. 2001, 33:940-959.
2. Kohanski M.A., Dwyer D.J., Hayete B., Lawrence C.A., Collins J.J. A common mechanism of cellular death induced by bactericidal antibiotics. Cell 2007, 130:797-810.
3. Andrews S.C., Robinson A.K., Rodriguez-Quinones F. Bacterial iron homeostasis. FEMS Microbiol. Rev. 2003, 27:215-237.
4. Chasteen N.D. Ferritin. Uptake, storage, and release of iron. Met. Ions Biol. Syst. 1998, Vol 35:479-514.
5. Lewin A., Moore G.R., Le Brun N.E. Formation of protein-coated iron minerals. Dalton Trans. 2005, 3597-3610.
6. Theil E.C., Matzapetakis M., Liu X.F. Ferritins: iron/oxygen biominerals in protein nanocages. J. Biol. Inorg. Chem. 2006, 11:803-810.
7. Harrison P.M., Arosio P. Ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta-Bioenerg. 1996, 1275:161-203.
8. Theil E.C. The ferritin family of iron storage proteins. Adv. Enzymol. Relat. Areas Mol. Biol. 1990, 63:421-449.
9. Grant R.A., Filman D.J., Finkel S.E., Kolter R., Hogle J.M. The crystal structure of Dps, a ferritin homolog that binds and protects DNA. Nat. Struct. Biol. 1998, 5:294-303.
10. Ilari A., Stefanini S., Chiancone E., Tsernoglou D. The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site. Nat. Struct. Biol. 2000, 7:38-43.
11. E. Chiancone, P. Ceci, The multifaceted actions of Dps proteins to combat bacterial stress conditions: detoxification of iron and hydrogen peroxide and DNA binding Biochim. Biophys. Acta this issue. doi:10.1016/j.bbagen.2010.01.013.
12. Johnson E., Cascio D., Sawaya M.R., Gingery M., Schroder I. Crystal structures of a tetrahedral open pore ferritin from the hyperthermophilic Archaeon Archaeoglobus fulgidus. Struct. Fold. Des. 2005, 13:637-648.
13. Tatur J., Hagen W.R., Matias P.M. Crystal structure of the ferritin from the hyperthermophilic archaeal anaerobe Pyrococcus furiosus. J. Biol. Inorg. Chem. 2007, 12:615-630.
14. S.C. Andrews, The ferritin superfamily: structure, function and evolution of the biological iron storeman, Biochim. Biophys. Acta submitted for publication.
15. Abdul-Tehrani H., Hudson A.J., Chang Y.S., Timms A.R., Hawkins C., Williams J.M., Harrison P.M., Guest J.R., Andrews S.C. Ferritin mutants of Escherichia coli are iron deficient and growth impaired, and fur mutants are iron deficient. J. Bacteriol. 1999, 181:1415-1428.
16. Velayudhan J., Castor M., Richardson A., Main-Hester K.L., Fang F.C. The role of ferritins in the physiology of Salmonella enterica sv. Typhimurium: a unique role for ferritin B in iron-sulphur cluster repair and virulence. Mol. Microbiol. 2007, 63:1495-1507.
17. Expert D., Boughammoura A., Franza T. Siderophore-controlled iron assimilation in the enterobacterium Erwinia chrysanthemi evidence for the involvement of bacterioferritin and the Suf iron-sulfur cluster assembly machinery. J. Biol. Chem. 2008, 283:36564-36572.
18. Waidner B., Greiner S., Odenbreit S., Kavermann H., Velayudhan J., Stahler F., Guhl J., Bisse E., van Vliet A.H.M., Andrews S.C., Kusters J.G., Kelly D.J., Haas R., Kist M., Bereswill S. Essential role of ferritin Pfr in Helicobacter pylori iron metabolism and gastric colonization. Infect. Immun. 2002, 70:3923-3929.
19. Wai S.N., Nakayama K., Umene K., Moriya T., Amako K. Construction of a ferritin-deficient mutant of Campylobacter jejuni: contribution of ferritin to iron storage and protection against oxidative stress. Mol. Microbiol. 1996, 20:1127-1134.
20. Edson R.R., Smith C.J. Transcriptional regulation of the Bacteroides fragilis ferritin gene (ftnA) by redox stress. Microbiology 2004, 150:2125-2134.
21. Shcolnick S., Summerfield T.C., Reytman L., Sherman L.A., Keren N. The mechanism of iron homeostasis in the unicellular cyanobacterium Synechocystis sp PCC 6803 and its relationship to oxidative stress. Plant Physiol. 2009, 150:2045-2056.
22. Chen C.Y., Morse S.A. Neisseria gonorrhoeae bacterioferritin: structural heterogeneity, involvement in iron storage and protection against oxidative stress. Microbiology 1999, 145:2967-2975.
23. 557.5 is a bacterioferritin. Nature 1979, 279:81-83.
24. Andrews S.C. Iron storage in bacteria. Adv. Microb. Physiol. 1998, 40:281-351.
25. Romao C.V., da Costa P.N., Macedo S., Mitchell E., Matias P.M., Melo E., Liu M.Y., Xavier A.V., Lindley P., LeGall J., Carrondo M.A., Saraiva L.M., Teixeira M. A bacterioferritin from the sulphate reducing bacterium Desulfovibrio desulfuricans ATCC 27774, with a novel haem cofactor. J. Inorg. Biochem. 2001, 86:405-405.
26. Frolow F., Kalb A.J., Yariv J. Structure of a unique twofold symmetrical heme-binding site. Nat. Struct. Biol. 1994, 1:453-460.
27. Cobessi D., Huang L.S., Ban M., Pon N.G., Daldal F., Berry E.A. The 2.6 angstrom resolution structure of Rhodobacter capsulatus bacterioferritin with metal-free dinuclear site and heme iron in a crystallographic 'special position'. Acta Crystallogr. D Biol. Crystallogr. 2002, 58:29-38.
28. Macedo S., Romao C.V., Mitchell E., Matias P.M., Liu M.Y., Xavier A.V., LeGall J., Teixeira M., Lindley P., Carrondo M.A. The nature of the di-iron site in the bacterioferritin from Desulfovibrio desulfuricans. Nat. Struct. Biol. 2003, 10:285-290.
29. Liu H.L., Zhou H.N., Xing W.M., Zhao H.F., Li S.X., Huang J.F., Bi R.C. 2.6 angstrom resolution crystal structure of the bacterioferritin from Azotobacter vinelandii. FEBS Lett. 2004, 573:93-98.
30. Swartz L., Kuchinskas M., Li H.Y., Poulos T.L., Lanzilotta W.N. Redox-dependent structural changes in the Azotobacter vinelandii bacterioferritin: new insights into the ferroxidase and iron transport mechanism. Biochemistry 2006, 45:4421-4428.
31. van Eerde A., Wolternik-van Loo S., van der Oost J., Dijkstra B.W. Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form. Acta Crystallogr. Sect. F Struct. Biol. Cryst.Commun. 2006, 62:1061-1066.
32. Gupta V., Gupta R.K., Khare G., Salunke D.M., Tyagi A.K. Crystal structure of BfrA from Mycobacterium tuberculosis: incorporation of selenomethionine results in cleavage and demetallation of haem. Plos One 2009, 4.
33. Moore G.R., Kadir F.H.A., Almassad F.K., Le Brun N.E., Thomson A.J., Greenwood C., Keen J.N., Findlay J.B.C. Structural heterogeneity of Pseudomonas aeruginosa bacterioferritin. Biochem. J. 1994, 304:493-497.
34. Miller C.D., Kim Y.C., Walsh M.K., Anderson A.J. Characterization and expression of the Pseudomonas putida bacterioferritin alpha subunit gene. Gene 2000, 247:199-207.
35. Keren N., Aurora R., Pakrasi H.B. Critical roles of bacterioferritins in iron storage and proliferation of cyanobacteria. Plant Physiol. 2004, 135:1666-1673.
36. Carrondo M.A. Ferritins, iron uptake and storage from the bacterioferritin viewpoint. EMBO J. 2003, 22:1959-1968.
37. Hudson A.J., Andrews S.C., Hawkins C., Williams J.M., Izuhara M., Meldrum F.C., Mann S., Harrison P.M., Guest J.R. Overproduction, purification and characterization of the Escherichia coli ferritin. Eur. J. Biochem. 1993, 218:985-995.
38. Clerte S., Dautant A., d'Estaintot B.L., Gallois B., Mizunoe Y., Wai S.N., Precigoux G. Expression, purification, crystallization and preliminary X-ray diffraction results from Campylobacter jejuni ferritin. Acta Crystallogr. D Biol. Crystallogr. 1999, 55:299-301.
39. Ratnayake D.B., Wai S.N., Shi Y.X., Amako K., Nakayama H., Nakayama K. Ferritin from the obligate anaerobe Porphyromonas gingivalis: purification, gene cloning and mutant studies. Microbiology 2000, 146:1119-1127.
40. Treffry A., Zhao Z.W., Quail M.A., Guest J.R., Harrison P.M. The use of zinc(II) to probe iron binding and oxidation by the ferritin (EcFtnA) of Escherichia coli. J. Biol. Inorg. Chem. 1998, 3:682-688.
41. Bauminger E.R., Treffry A., Quail M.A., Zhao Z.W., Nowik I., Harrison P.M. Stages in iron storage in the ferritin of Escherichia coli (EcFtnA): analysis of Mössbauer spectra reveals a new intermediate. Biochemistry 1999, 38:7791-7802.
42. 2+ derivatives. J. Mol. Biol. 2001, 307:587-603.
43. Bou-Abdallah F., Woodhall M.R., Velazquez-Campoy A., Andrews S.C., Chasteen N.D. Thermodynamic analysis of ferrous ion binding to Escherichia coli ferritin EcFtnA. Biochemistry 2005, 44:13837-13846.
44. Cho K.J., Shin H.J., Lee J.H., Kim K.J., Park S.S., Lee Y., Lee C., Kim K.H. The crystal structure of ferritin from Helicobacter pylori reveals unusual conformational changes for iron uptake. J. Mol. Biol. 2009, 390:83-98.
45. Cheesman M.R., Thomson A.J., Greenwood C., Moore G.R., Kadir F. Bis-methionine axial ligation of heme in bacterioferritin from Pseudomonas aeruginosa. Nature 1990, 346:771-773.
46. George G.N., Richards T., Bare R.E., Gea Y.J., Prince R.C., Stiefel E.I., Watt G.D. Direct observation of bis-sulfur ligation to the heme of bacterioferritin. J. Am. Chem. Soc. 1993, 115:7716-7718.
47. Aranda R., Worley C.E., Liu M., Bitto E., Cates M.S., Olson J.S., Lei B., Phillips G.N. Bis-methionyl coordination in the crystal structure of the heme-binding domain of the streptococcal cell surface protein Shp. J. Mol. Biol. 2007, 374:374-383.
48. Andrews S.C., Le Brun N.E., Barynin V., Thomson A.J., Moore G.R., Guest J.R., Harrison P.M. Site-directed replacement of the coaxial heme ligands of bacterioferritin generates heme-free variants. J. Biol. Chem. 1995, 270:23268-23274.
49. Weeratunga S.K., Gee C.E., Lovell S., Zeng Y.H., Woodin C.L., Rivera M. Binding of Pseudomonas aeruginosa apobacterioferritin-associated ferredoxin to bacterioferritin B promotes heme mediation of electron delivery and mobilization of core mineral iron. Biochemistry 2009, 48:7420-7431.
50. Banyard S.H., Stammers D.K., Harrison P.M. Electron-density map of apoferritin at 2.8 Å resolution. Nature 1978, 271:282-284.
51. 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.
52. 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.
53. Lawson D.M., Treffry A., Artymiuk P.J., Harrison P.M., Yewdall S.J., Luzzago A., Cesareni G., Levi S., Arosio P. Identification of the ferroxidase center in ferritin. FEBS Lett. 1989, 254:207-210.
54. d'Estaintot B.L., Paolo S., Granier T., Gallois B., Chevalier J.M., Precigoux G., Levi S., Arosio P. Crystal structure and biochemical properties of the human mitochondrial ferritin and its mutant Ser144Ala. J. Mol. Biol. 2004, 340:277-293.
55. Crow A., Lawson T.L., Lewin A., Moore G.R., Le Brun N.E. Structural basis for iron mineralisation by bacterioferritin. J. Am. Chem. Soc. 2009, 131:6808-6813.
56. Nordlund P., Sjoberg B.M., Eklund H. 3-Dimensional structure of the free-radical protein of ribonucleotide reductase. Nature 1990, 345:593-598.
57. Rosenzweig A.C., Frederick C.A., Lippard S.J., Nordlund P. Crystal structure of a bacterial nonheme iron hydroxylase that catalyzes the biological oxidation of methane. Nature 1993, 366:537-543.
58. Weeratunga S.K., Lovell S., Yao H., Battaile K.P., Fischer C.J., Gee C.E., Rivera M. Structural studies of bacterioferritin B from Pseudomonas aeruginosa suggest a gating mechanism for iron uptake via the ferroxidase center. Biochemistry 2010, 10.1021/bi9015204.
59. Aberg A., Nordlund P., Eklund H. Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase. Nature 1993, 361:276-278.
60. + release associated with cobalt(II) and zinc(II) binding at dinuclear metal sites. FEBS Lett. 1996, 397:159-163.
61. Wong S.G., Tom-Yew S.A.L., Lewin A., Le Brun N.E., Moore G.R., Murphy M.E.P., Mauk A.G. Structural and mechanistic studies of a stabilized subunit dimer variant of Escherichia coli bacterioferritin identify residues required for core formation. J. Biol. Chem. 2009, 284:18873-18881.
62. 1-bacterioferritins 2001, 782-790. Handbook of Metalloproteins Wiley, New York. A. Messerschmidt (Ed.).
63. Lindqvist Y., Johansson E., Kaija H., Vihko P., Schneider G. Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 Å resolution with a mu-(hydr)oxo bridged di-iron center. J. Mol. Biol. 1999, 291:135-147.
64. Strater N., Klabunde T., Tucker P., Witzel H., Krebs B. Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site. Science 1995, 268:1489-1492.
65. Holmes M.A., Letrong I., Turley S., Sieker L.C., Stenkamp R.E. Structures of deoxy and oxy hemerythrin at 2.0 Å resolution. J. Mol. Biol. 1991, 218:583-593.
66. Le Brun N.E., Wilson M.T., Andrews S.C., Guest J.R., Harrison P.M., Thomson A.J., Moore G.R. Kinetic and structural characterization of an intermediate in the biomineralization of Bacterioferritin. FEBS Lett. 1993, 333:197-202.
67. Yang X., Le Brun N.E., Thomson A.J., Moore C.R., Chasteen N.D. The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin. Biochemistry 2000, 39:4915-4923.
68. Wiedenheft B., Mosolf J., Willits D., Yeager M., Dryden K.A., Young M., Douglas T. An archaeal antioxidant: characterization of a Dps-like protein from Sulfolobus solfataricus. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:10551-10556.
69. Ramsay B., Wiedenheft B., Allen M., Gauss G.H., Lawrence C.M., Young M., Douglas T. Dps-like protein from the hyperthermophilic archaeon Pyrococcus furiosus. J. Inorg. Biochem. 2006, 100:1061-1068.
70. Gauss G.H., Benas P., Wiedenheft B., Young M., Douglas T., Lawrence C.M. Structure of the DPS-like protein from Sulfolobus solfataricus reveals a bacterioferritin-like dimetal binding site within a DPS-like dodecameric assembly. Biochemistry 2006, 45:10815-10827.
71. Granier T., d'Estaintot B.L., Gallois B., Chevalier J.M., Precigoux G., Santambrogio P., Arosio P. Structural description of the active sites of mouse L-chain ferritin at 1.2 Å resolution. J. Biol. Inorg. Chem. 2003, 8:105-111.
72. Hempstead P.D., Hudson A.J., Artymiuk P.J., Andrews S.C., Banfield M.J., Guest J.R., Harrison P.M. Direct observation of the iron-binding sites in a ferritin. FEBS Lett. 1994, 350:258-262.
73. Treffry A., Zhao Z.W., Quail M.A., Guest J.R., Harrison P.M. How the presence of three iron binding sites affects the iron storage function of the ferritin (EcFtnA) of Escherichia coli. FEBS Lett. 1998, 432:213-218.
74. Ford G.C., Harrison P.M., Rice D.W., Smith J.M.A., Treffry A., White J.L., Yariv J. Ferritin-design and formation of an iron-storage molecule. Philos. Trans. R. Soc. Lond. B Biol. Sci. 1984, 304:551-565.
75. Towe K.M., Bradley W.F. Mineralogical constitution of colloidal hydrous ferric oxides. J. Colloid Interface Sci. 1967, 24:384-392.
76. Michel F.M., Ehm L., Antao S.M., Lee P.L., Chupas P.J., Liu G., Strongin D.R., Schoonen M.A.A., Phillips B.L., Parise J.B. The structure of ferrihydrite, a nanocrystalline material. Science 2007, 316:1726-1729.
77. Harrison P.M., Fischbach F.A., Hoy T.G., Haggis G.H. Ferric oxyhydroxide core of ferritin. Nature 1967, 216:1188-1190.
78. Massover W.H., Cowley J.M. Ultrastructure of ferritin macromolecules-lattice structure of core crystallites. Proc. Natl. Acad. Sci. U. S. A. 1973, 70:3847-3851.
79. Galvez N., Fernandez B., Sanchez P., Cuesta R., Ceolin M., Clemente-Leon M., Trasobares S., Lopez-Haro M., Calvino J.J., Stephan O., Dominguez-Vera J.M. Comparative structural and chemical studies of ferritin cores with gradual removal of their iron contents. J. Am. Chem. Soc. 2008, 130:8062-8068.
80. 557 (bacterioferritin) from Pseudomonas aeruginosa. J. Inorg. Biochem. 1986, 28:329-336.
81. Rohrer J.S., Islam Q.T., Watt G.D., Sayers D.E., Theil E.C. 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 1990, 29:259-264.
82. Doig P., Austin J.W., Trust T.J. The Helicobacter pylori 19.6-kilodalton protein is an iron-containing protein resembling ferritin. J. Bacteriol. 1993, 175:557-560.
83. Baaghil S., Thomson A.J., Moore G.R., Le Brun N.E. Studies of copper(II)-binding to bacterioferritin and its effect on iron(II) oxidation. J. Chem. Soc.-Dalton Trans. 2002, 811-818.
84. Aitken-Rogers H., Singleton C., Lewin A., Taylor-Gee A., Moore G.R., Le Brun N.E. Effect of phosphate on bacterioferritin-catalysed iron(II) oxidation. J. Biol. Inorg. Chem. 2004, 9:161-170.
85. St Pierre T.G., Bell S.H., Dickson D.P.E., Mann S., Webb J., Moore G.R., Williams R.J.P. Mössbauer spectroscopic studies of the cores of human, limpet and bacterial ferritins. Biochim. Biophys. Acta 1986, 870:127-134.
86. Weir M.P., Peters T.J., Gibson J.F. Electron spin resonance studies of splenic ferritin and hemosiderin. Biochim. Biophys. Acta 1985, 828:298-305.
87. Deighton N., Aburaqabah A., Rowland I.J., Symons M.C.R., Peters T.J., Ward R.J. Electron paramagnetic resonance studies of a range of ferritins and haemosiderins. J. Chem. Soc.-Faraday Trans. 1991, 87:3193-3197.
88. Le Brun N.E., Moore G.R., Thomson A.J. Magnetic circular dichroism spectroscopy of the iron cores of ferritin and bacterioferritin. Mol. Phys. 1995, 85:1061-1068.
89. Mann S., Williams J.M., Treffry A., Harrison P.M. Reconstituted and native iron-cores of bacterioferritin and ferritin. J. Mol. Biol. 1987, 198:405-416.
90. Reid N.M.K., Dickson D.P.E., Greenwood C., Thompson A., Kadir F.H.A., Moore G.R. Evidence for Mössbauer spectroscopy for different forms of iron core in Pseudomonas aeruginosa bacterial ferritin. Biochem. J. 1990, 272:263-264.
91. Watt G.D., Frankel R.B., Papaefthymiou G.C., Spartalian K., Stiefel E.I. Redox properties and Mössbauer spectroscopy of Azotobacter vinelandii Bacterioferritin. Biochemistry 1986, 25:4330-4336.
92. Levi S., Luzzago A., Cesareni G., Cozzi A., Franceschinelli F., Albertini A., Arosio P. Mechanism of ferritin iron uptake-activity of the H-chain and deletion mapping of the ferro-oxidase site-a study of iron uptake and ferro-oxidase activity of human-liver, recombinant H-chain ferritins, and of 2 H-chain deletion mutants. J. Biol. Chem. 1988, 263:18086-18092.
93. Zhao G.H., Bou-Abdallah F., Arosio P., Levi S., Janus-Chandler C., Chasteen N.D. Multiple pathways for mineral core formation in mammalian apoferritin. The role of hydrogen peroxide. Biochemistry 2003, 42:3142-3150.
94. Jameson G.N.L., Jin W., Krebs C., Perreira A.S., Tavares P., Liu X.F., 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.
95. Waldo G.S., Theil E.C. Formation of iron(III)-tyrosinate is the fastest reaction observed in ferritin. Biochemistry 1993, 32:13262-13269.
96. Yang X.K., 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.
97. Bou-Abdallah F., Zhao G.H., Mayne H.R., Arosio P., Chasteen N.D. Origin of the unusual kinetics of iron deposition in human H-chain ferritin. J. Am. Chem. Soc. 2005, 127:3885-3893.
98. 2 Stoichiometry during core formation. J. Biol. Chem. 1991, 266:19965-19970.
99. Macara I.G., Harrison P.M., Hoy T.G. Formation of ferritin from apoferritin-kinetics and mechanism of iron uptake. Biochem. J. 1972, 126:151.
100. Macara I.G., Hoy T.G., Harrison P.M. Formation of ferritin from apoferritin-catalytic action of apoferritin. Biochem. J. 1973, 135:343-348.
101. Le Brun N.E., Andrews S.C., Guest J.R., Harrison P.M., Moore G.R., Thomson A.J. Identification of the ferroxidase centre of Escherichia coli bacterioferritin. Biochem. J. 1995, 312:385-392.
102. Bou-Abdallah F., Lewin A.C., Le Brun N.E., Moore G.R., Chasteen N.D. Iron detoxification properties of Escherichia coli bacterioferritin-attenuation of oxyradical chemistry. J. Biol. Chem. 2002, 277:37064-37069.
103. Baaghil S., Lewin A., Moore G.R., Le Brun N.E. Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center. Biochemistry 2003, 42:14047-14056.
104. Lawson T.L., Crow A., Lewin A., Yasmin S., Moore G.R., Le Brun N.E. Monitoring the iron status of the ferroxidase center of Escherichia coli bacterioferritin using fluorescence spectroscopy. Biochemistry 2009, 48:9031-9039.
105. 2+ and phosphate interactions in bacterial ferritin from Azotobacter vinelandii. Biochemistry 1992, 31:5672-5679.
106. Bauminger E.R., Treffry A., Quail M.A., Zhao Z.W., Nowik I., Harrison P.M. Metal binding at the active centre of the ferritin of Escherichia coli (EcFtnA). A Mössbauer spectroscopic study. Inorg. Chim. Acta 2000, 297:171-180.
107. Zhao Z.W., Treffry A., Quail M.A., Guest J.R., Harrison P.M. Catalytic iron(II) oxidation in the non-haem ferritin of Escherichia coli: the early intermediate is not an iron tyrosinate. J. Chem. Soc. Dalton Trans. 1997, 3977-3978.
108. Bou-Abdallah F., Papaefthymiou G.C., Scheswohl D.M., Stanga S.D., Arosio P., Chasteen N.D. mu-1, 2-peroxobridged di-iron(III) dimer formation in human H-chain ferritin. Biochem. J. 2002, 364:57-63.
109. Ebrahimi K.H., Hagedoorn P.L., Jongejan J.A., Hagen W.R. Catalysis of iron core formation in Pyrococcus furiosus ferritin. J. Biol. Inorg. Chem. 2009, 14:1265-1274.
110. Tatur J., Hagen W.R. The dinuclear iron-oxo ferroxidase center of Pyrococcus furiosus ferritin is a stable prosthetic group with unexpectedly high reduction potentials. FEBS Lett. 2005, 579:4729-4732.
111. Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 1994, 22:4673-4680.
112. Nicholas K.B., Nicholas H.B. Genedoc: A tool for editing and annotating multiple sequence alignments, distributed by the authors 1997.
113. DeLano W.L. The PyMOL Molecular Graphics System 2002, DeLano Scientific, San Carlos, USA.