Electrochemical properties of the diiron core of uteroferrin and its anion complexes

Dan Li Wang, Richard C. Holz, Sheila S. David, Lawrence Que, Marian T. Stankovich

Research output: Contribution to journalArticle

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Abstract

The reduction potentials (Em) of the purple acid phosphatase from porcine uterus, uteroferrin (Uf), and its phosphate, arsenate, and molybdate complexes were determined by coulometric methods at various pH values. The midpoint potential of Uf at the pH value for optimal enzyme activity (pH 5) was found to be +367 mV versus a normal hydrogen electrode (NHE), while at pH 6.01 Uf exhibits a reduction potential of +306 mV. At pH 6.01 molybdate was found to shift the potential of Uf more positive by 192 mV, while phosphate and arsenate shift the potential of Uf more negative by 193 and 89 mV, respectively. These shifts are consistent with the different susceptibilities of Uf to aerobic oxidation in the presence of these anions. Comparison of the reduction potential of Uf at pH 7.0 with those reported for other dinuclear non-heme iron enzymes and various (μ-oxo)diiron model complexes suggest that the potential of Uf is too positive to be consistent with a μ-oxo-bridge in Ufo. The pH dependence of the reduction potentials of Uf (60 mV/pH unit) and the fact that the electron transfer rate increases with decreasing pH indicate a concomitant participation of a proton during the oxidation-reduction process. This process was assigned to the protonation of a terminally bound hydroxide ligand at the Fe(II) center upon reduction of Ufo. Structural implications provided by the electrochemical data indicate that molybdate affects the dinuclear core in a manner that differs from that of phosphate and arsenate. This observation is consistent with previous spectroscopic and biochemical studies. Several possible anion binding modes are discussed and related to our recently proposed model for the interaction of anions with Ufr [David, S. S., & Que, L., Jr. (1990) J. Am. Chem. Soc. 112, 6455-6463].

Original languageEnglish (US)
Pages (from-to)8187-8194
Number of pages8
JournalBiochemistry
Volume30
Issue number33
StatePublished - 1991
Externally publishedYes

Fingerprint

Electrochemical properties
Anions
Phosphates
Protonation
Enzyme activity
Protons
Hydrogen
Iron
Tartrate-Resistant Acid Phosphatase
Ligands
Oxidation
Electrodes
Enzymes
Electrons
Uterus
Oxidation-Reduction
Swine
arsenic acid
molybdate

ASJC Scopus subject areas

  • Biochemistry

Cite this

Wang, D. L., Holz, R. C., David, S. S., Que, L., & Stankovich, M. T. (1991). Electrochemical properties of the diiron core of uteroferrin and its anion complexes. Biochemistry, 30(33), 8187-8194.

Electrochemical properties of the diiron core of uteroferrin and its anion complexes. / Wang, Dan Li; Holz, Richard C.; David, Sheila S.; Que, Lawrence; Stankovich, Marian T.

In: Biochemistry, Vol. 30, No. 33, 1991, p. 8187-8194.

Research output: Contribution to journalArticle

Wang, DL, Holz, RC, David, SS, Que, L & Stankovich, MT 1991, 'Electrochemical properties of the diiron core of uteroferrin and its anion complexes', Biochemistry, vol. 30, no. 33, pp. 8187-8194.
Wang DL, Holz RC, David SS, Que L, Stankovich MT. Electrochemical properties of the diiron core of uteroferrin and its anion complexes. Biochemistry. 1991;30(33):8187-8194.
Wang, Dan Li ; Holz, Richard C. ; David, Sheila S. ; Que, Lawrence ; Stankovich, Marian T. / Electrochemical properties of the diiron core of uteroferrin and its anion complexes. In: Biochemistry. 1991 ; Vol. 30, No. 33. pp. 8187-8194.
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