Magnetization and electron paramagnetic resonance studies of reduced uteroferrin and its 'EPR-silent' phosphate complex

E. P. Day, S. S. David, J. Peterson, W. R. Dunham, J. J. Bonvoisin, R. H. Sands, L. Que

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Abstract

The exchange coupling of reduced uteroferrin has been measured (19.8(5) cm-1 S1·S2) using recently developed techniques for studying metalloprotein magnetization. A spin Hamiltonian describing the coupled binuclear Fe(II)·Fe(III) center has been used to fit the low and high field magnetization data, the EPR g values, and the highly anisotropic effective hyperfine tensor of the ferric site. The exchange coupling of the phosphate complex of reduced uteroferrin has also been measured (6.0(5) cm-1 S1·S2) using the same techniques. The smaller exchange coupling of the phosphate complex is comparable with the zero field splittings of the iron sites. This results in increased sensitivity of the system g values (found by calculation from the spin Hamiltonian) to variations of the zero field splitting parameters arising from heterogeneities in the protein microenvironment. Consequently, there is a very significant (9-fold) increase in the 'effective g strain' of the system compared to the situation in the absence of phosphate. This, together with the larger g anisotropy (g = (1.06, 1.51, 2.27)), gives rise to an EPR signal for the phosphate complex of reduced uteroferrin which is extremely broad and difficult to detect but which has now been identified for the first time.

Original languageEnglish (US)
Pages (from-to)15561-15567
Number of pages7
JournalJournal of Biological Chemistry
Volume263
Issue number30
StatePublished - 1988
Externally publishedYes

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Electron Spin Resonance Spectroscopy
Exchange coupling
Paramagnetic resonance
Magnetization
Phosphates
Hamiltonians
Metalloproteins
Anisotropy
Tensors
Iron
Tartrate-Resistant Acid Phosphatase
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Day, E. P., David, S. S., Peterson, J., Dunham, W. R., Bonvoisin, J. J., Sands, R. H., & Que, L. (1988). Magnetization and electron paramagnetic resonance studies of reduced uteroferrin and its 'EPR-silent' phosphate complex. Journal of Biological Chemistry, 263(30), 15561-15567.

Magnetization and electron paramagnetic resonance studies of reduced uteroferrin and its 'EPR-silent' phosphate complex. / Day, E. P.; David, S. S.; Peterson, J.; Dunham, W. R.; Bonvoisin, J. J.; Sands, R. H.; Que, L.

In: Journal of Biological Chemistry, Vol. 263, No. 30, 1988, p. 15561-15567.

Research output: Contribution to journalArticle

Day, EP, David, SS, Peterson, J, Dunham, WR, Bonvoisin, JJ, Sands, RH & Que, L 1988, 'Magnetization and electron paramagnetic resonance studies of reduced uteroferrin and its 'EPR-silent' phosphate complex', Journal of Biological Chemistry, vol. 263, no. 30, pp. 15561-15567.
Day EP, David SS, Peterson J, Dunham WR, Bonvoisin JJ, Sands RH et al. Magnetization and electron paramagnetic resonance studies of reduced uteroferrin and its 'EPR-silent' phosphate complex. Journal of Biological Chemistry. 1988;263(30):15561-15567.
Day, E. P. ; David, S. S. ; Peterson, J. ; Dunham, W. R. ; Bonvoisin, J. J. ; Sands, R. H. ; Que, L. / Magnetization and electron paramagnetic resonance studies of reduced uteroferrin and its 'EPR-silent' phosphate complex. In: Journal of Biological Chemistry. 1988 ; Vol. 263, No. 30. pp. 15561-15567.
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