Electron exchange between Fe(II)-horse spleen ferritin and Co(III)Mn(III) reconstituted horse spleen and Azotobacter vinelandii ferritins

Biochemistry

Volumn 45, Issue 18, 2006, Pages 5766-5774

  Zhang, Bo ^a   Harb, John N ^b   Davis, Robert C ^a   Choi, Sang ^c   Kim, Jae Woo ^c   Miller, Tim ^b   Chu, Sang Hyon ^c   Watt, Gerald D ^a  

^a N243 Eyring Science Center   (United States)

^b Department of Electrical and Computer Engineering   (United States)

^c NASA LANGLEY RESEARCH CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COBALT; FERRITES; MANGANESE; REACTION KINETICS; SYNTHESIS (CHEMICAL); VITAMINS;

AZOTOBACTER VINELANDII FERRITINS; FERRITIN; MOLECULAR INTERACTIONS; SPLEEN;

BACTERIOLOGY;

BACTERIOFERRITIN; CARBON MONOXIDE; COBALT; FERRITIN; GOLD; HYDROXIDE; MANGANESE; MINERAL; PARAQUAT; SILICON DIOXIDE; UNCLASSIFIED DRUG;

ARTICLE; AZOTOBACTER VINELANDII; BINDING SITE; CONDUCTANCE; ELECTRON TRANSPORT; HORSE; KINETICS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; REACTION ANALYSIS; REACTION TIME; REDUCTION; SPLEEN; SYNTHESIS;

ANIMALS; AZOTOBACTER VINELANDII; ELECTRON TRANSPORT; FERRITINS; GOLD; HORSES; KINETICS; SILICON DIOXIDE; SPLEEN;

AZOTOBACTER VINELANDII; EQUUS CABALLUS;

EID: 33646466461     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060164d     Document Type: Article

References (42)

1. Theil, E. C. (1987) Ferritin structure gene regulation and cellular function in animals plants and microorganisms, Annu. Rev. Biochem. 56, 289-316.
2. Harrison, P. M., and Arosio, P. (1996) The ferritins: molecular properties, iron storage function and cellular regulation, Biochim. Biophys. Acta 1275, 161-203.
3. Bozzi, M., Mignogna, G., Stefanini, S., Barra, D., Longhi, C., Valenti, P., and Chiancone, E. (1997) A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua, J. Biol. Chem. 272, 3259-3265.
4. Meldrum, F. C., Wade, V. J., Nimmo, D. L., Heywood, B. R., and Mann, S. (1991) Synthesis of inorganic nanophase materials in supramolecular protein cages, Nature 349, 684-687.
5. Douglas, T., and Stark, V. T. (2000) Nanophase cobalt oxyhydroxide mineral synthesized within the protein cage of ferritin, Inorg. Chem. 39, 1828-1830.
6. Mackle, P., Charnock, J. M., Garner, C. D., Meldrum, F. C., and Mann, S. (1993) Characterization of the manganese core of reconstituted ferritin by X-ray absorption spectroscopy, J. Am. Chem. Soc. 115, 8471-8472.
7. Meldrum, F. C., Douglas, T., Levi, S., Arosio, P., and Mann, S. (1995) Reconstitution of manganese oxide cores in horse spleen and recombinant ferritins, J. Inorg. Biochem. 58, 59-68.
8. Meldrum, F. C., Heywood, B. R., and Mann, S. (1992) Magneto-ferritin in-vitro synthesis of a novel magnetic protein, Science (Washington, D.C.) 257, 522-523.
9. Okuda, M., Iwahori, K., Yamashita, I., and Yoshimura, H. (2003) Fabrication of nickel and chromium nanoparticles using the protein cage of apoferritin, Biotech. Bioeng. 84, 187-194.
10. Wong, K. K. W., and Mann, S. (1996) Biomimetic synthesis of cadmium sulfide- ferritin nanocomposites, Adv. Mater. (Weinheim, Ger.) 8, 928-932.
11. Watt, G. D., Jacobs, D., and Frankel, R. B. (1988) Redox reactivity of bacterial and mammalian ferritin: is reductant entry into the ferritin interior a necessary step for iron release, Proc. Natl. Acad. Sci. U.S.A. 85, 7457-7461.
12. Stuhrmann, H. B., Haas, J., Ibel, K., Koch, M. H. J., and Crichton, R. R. (1976) Low angle neutron scattering of ferritin studied by contrast variation, J. Mol. Biol. 100, 399-413.
13. May, M. E., Fish, W. W., Brown, E. B., Aisen, P., and Fielding, J. (1977) The restrictive nature of apoferritin channels as measured by passive diffusion. In Proteins of Iron Metabolism (Brown, E. J., Ed.) pp 31-38, Grune & Stratton, New York.
14. Webb, B., Frame, J., Zhao, Z., Lee, M. L., and Watt, G. D. (1994) Molecular entrapment of small molecules within the interior of horse spleen ferritin, Arch. Biochem. Biophys. 309, 178-183.
15. Yang, X., and Chasteen, N. D. (1996) Molecular diffusion into horse spleen ferritin: a nitroxide radical spin probe study, Biophys. J. 71, 1587-1595.
16. Watt, G. D., Frankel, R. B., Papaefthymiou, G. C., Spartalian, K., and Stiefel, E. I. (1986) Redox properties and Mössbauer spectroscopy of Azotobacter vinelandii bacterioferritin, Biochemistry 25, 4330-4336.
17. Andrews, S. C. (1998) Iron storage in bacteria, Adv. Microb. Physiol. 40, 282-351.
18. Richards, T. D., Pitts, K. R., and Watt, G. D. (1996) A kinetic study of iron release from Azotobacter vinelandii bacterial ferritin, J. Inorg. Biochem. 61, 1-13.
19. Stiefel, E. I., and Watt, G. D. (1979) Azotobacter cytochrome b557.5 is a bacterioferritin, Nature 279, 81-83.
20. Martin, T. D., Monheit, S. A., Niichel, R. J., Peterson, S. C., Campbell, C. H., and Zapien, D. C. (1997) Electron transfer of horse spleen ferritin at gold electrodes modified by self-assembled monolayers, J. Electroanal. Chem. 420, 279-290.
21. Zapien, D. C., and Johnson, M. A. (2000) Direct electron transfer of ferritin adsorbed at bare gold electrodes, J. Electroanal. Chem. 494, 114-120.
22. Huang, H. Q., Lin, Q. M., and Wang, T. L. (2002) Kinetics of iron release from pig spleen ferritin with bare platinum electrode reduction, Biophys. Chem. 97, 17-27.
23. Xu, D., Watt, G. D., Harb, J. N., and Davis, R. C. (2005) Electrical conductivity of ferritin proteins by conductive AFM, Nano Lett. 5, 571-577.
24. Zhang, B., Harb, J. N., Davis, R. C., Kim, J. W., Chu, S. H., Choi, S., Miller, T., and Watt, G. D. (2005) Kinetic and thermodynamic characterization of the Co(III) and Mn(III) mineral cores formed in horse spleen ferritin, Inorg. Chem. 44, 3738-3745.
25. Treffry, A., and Harrison, P. M. (1978) Incorporation and release of inorganic phosphate in horse spleen ferritin, Biochem. J. 171, 313-320.
26. Zhao, G., Bou-Abdallah, F., Yang, X., Arosio, P., and Chasteen, N. D. (2001) Is hydrogen peroxide produced during iron(II) oxidation in mammalian apoferritins? Biochemistry 40, 10832-10838.
27. 2 as oxidant, Biochim. Biophys. Acta 1621, 57-66.
28. Double, K. L., Maywald, M., Schmittel, M., Riederer, P., and Gerlach, M. (1998) In vitro studies of ferritin iron release and neurotoxicity, J. Neurochem. 70, 2492-2499.
29. Ensign, S. A., Bonam, D., and Ludden, P. W. (1989) Nickel is required for the transfer of electrons from carbon monoxide to the iron-sulfur center(s) of carbon monoxide dehydrogenase from Rhodospirillum rubrum, Biochemistry 28, 4968-4973.
30. Stephens, P. J., McKenna, M. C., Ensign, S. A., Bonam, D., and Ludden, P. W. (1989) Identification of a Ni- and Fe-containing cluster in Rhodospirillum rubrum carbon monoxide dehydrogenase, J. Biol. Chem. 264, 16347-16350.
31. Watt, G. D., McDonald, J. W., Chiu, C. H., and Reddy, K. R. N. (1993) Further characterization of the redox and spectroscopic properties of Azotobacter vinelandii ferritin, J. Inorg. Biochem. 51, 745-758.
32. Allen, M., Willits, D., Young, M., and Douglas, T. (2003) Constrained synthesis of cobalt oxide nanomaterials in the 12-subunit protein cage from Listeria innocua, Inorg. Chem. 42, 6300-6305.
33. Yang, X., Arosio, P., and Chasteen, N. D. (2000) Molecular diffusion into ferritin: pathways, temperature dependence, incubation time, and concentration effects, Biophys. J. 78, 2049-2059.
34. Caruso, F., Furlong, D. N., and Kingshott, P. (1997) Characterization of ferritin adsorption onto gold, J. Colloid Interface Sci. 186, 129-140.
35. Hook, F., Rodahl, M., Brzezinski, P., and Kasemo, B. (1998) Measurements using the quartz crystal microbalance technique of ferritin monolayers on methyl thiolated gold: dependence of energy dissipation and saturation coverage on salt concentration, J. Colloid Interface Sci. 208, 63-67.
36. Watt, R. K., Frankel, R. B., and Watt, G. D. (1992) Redox reactions of apo mammalian ferritin, Biochemistry 31, 9673-9679.
37. Johnson, J. L., Norcross, D. C., Arosio, P., Frankel, R. B., and Watt, G. D. (1999) Redox reactivity of animal apoferritins and apoheteropolymers assembled from recombinant and light human chain ferritins, Biochemistry 38, 4089-4096.
38. Yang, D., and Nagayama, K. (1995) Permeation of small molecules into the cavity of ferritin as revealed by proton nuclear magnetic resonance relaxation, Biochem. J. 307, 253-256.
39. Watt, G. D., Frankel, R. B., and Papaefthymiou, G. C. (1985) Reduction of mammalian ferritin, Proc. Natl. Acad. Sci. U.S.A. 82, 3640-3643.
40. 2+ binding to apo and holo mammalian ferritin, Biochemistry 28, 9216-9221.
41. Nygren, H. (1993) Nonlinear kinetics of ferritin adsorption, Biophys. J. 65, 1508-1512.
42. Frew, J. E., and Hill, H. A. O. (1988) Direct and indirect electron transfer between electrodes and redox proteins, Eur. J. Biochem. 172, 261-269.