Abstract

This proposal has three specific aims. The first two are the same in intent but refer two different Ftn, a mammalian Ftn, horse spleen ferritin (HoSF) and a bacterial one, from Azobacter vinelandii (AVBF).
This aim i s to use microcoulometric methods to quantitatively link the flux of H(+) and e(-) to the amount of iron deposition and release from Ftn. Individual H and L chaims and site-directed mutant proteins will be used to localize the protein domains and residues associated with Fe binding and ferroxidase activity. Mossbauer spectroscopy will be used to quantitate the redox distribution of Fe that is incorporated into the Ftn.
The third aim i s to determine the relationship between phosphate in the Ftn core, the deposition of Fe in the core and the reactivity of the Fe in the core and to determine whether the modulation of these properties by phosphate is unique to this anion.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
2R01DK036799-06A4
Application #
2139871
Study Section
Metallobiochemistry Study Section (BMT)
Program Officer
Laughlin, Maren R
Project Start
1988-07-01
Project End
1998-06-30
Budget Start
1995-07-01
Budget End
1996-06-30
Support Year
6
Fiscal Year
1995
Total Cost
Indirect Cost

  Institution

Name
Brigham Young University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
City
Provo
State
UT
Country
United States
Zip Code
84602

  Publications

Lindsay, Stuart; Brosnahan, David; Lowery Jr, Thomas J et al. (2003) Kinetic studies of iron deposition in horse spleen ferritin using O2 as oxidant. Biochim Biophys Acta 1621:57-66
Lindsay, S; Brosnahan, D; Watt, G D (2001) Hydrogen peroxide formation during iron deposition in horse spleen ferritin using O2 as an oxidant. Biochemistry 40:3340-7
Johnson, J L; Norcross, D C; Arosio, P et al. (1999) Redox reactivity of animal apoferritins and apoheteropolymers assembled from recombinant heavy and light human chain ferritins. Biochemistry 38:4089-96
Johnson, J L; Cannon, M; Watt, R K et al. (1999) Forming the phosphate layer in reconstituted horse spleen ferritin and the role of phosphate in promoting core surface redox reactions. Biochemistry 38:6706-13
Richards, T D; Pitts, K R; Watt, G D (1996) A kinetic study of iron release from Azotobacter vinelandii bacterial ferritin. J Inorg Biochem 61:1-13
Pead, S; Durrant, E; Webb, B et al. (1995) Metal ion binding to apo, holo, and reconstituted horse spleen ferritin. J Inorg Biochem 59:15-27
Webb, B; Frame, J; Zhao, Z et al. (1994) Molecular entrapment of small molecules within the interior of horse spleen ferritin. Arch Biochem Biophys 309:178-83
Hilty, S; Webb, B; Frankel, R B et al. (1994) Iron core formation in horse spleen ferritin: magnetic susceptibility, pH, and compositional studies. J Inorg Biochem 56:173-85
Zhao, Z; Malik, A; Lee, M L et al. (1994) A capillary electrophoresis method for studying apo, holo, recombinant, and subunit dissociated ferritins. Anal Biochem 218:47-54
Heqing, H; Watt, R K; Frankel, R B et al. (1993) Role of phosphate in Fe2+ binding to horse spleen holoferritin. Biochemistry 32:1681-7

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