Electrochemical Properties of the Diiron Core of Uteroferrin and Its Anion Complexes

Authors

Dan Li Wang, University of Minnesota - Twin Cities
Richard C. Holz, Marquette UniversityFollow
Sheila S. David, University of Minnesota - Twin Cities
Lawrence Que Jr, University of Minnesota - Twin CitiesFollow
Marian T. Stankovich, University of Minnesota - Twin Cities

Document Type

Article

Publication Date

1991

Source Publication

Biochemistry

Source ISSN

0006-2960

Abstract

The reduction potentials (E_m) 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 consisten with a µ-oxo-bridge in Uf_o. 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-reducing process. This process was assigned to the protonation of a terminally bound hydroxide ligand at the Fe(II) center upon reduction of Uf_o. 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 consisten 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 Uf_r [David, S. S. & Que, L., Jr. (1990) J. Am. Chem. Soc. 112, 6455-6463].

Comments

BIochemistry, Vol. 30, No. 33 (1991): 8187-8194. DOI.

Richard Holz was affiliated with the University of Minnesota at the time of publication.

Recommended Citation

Wang, Dan Li; Holz, Richard C.; David, Sheila S.; Que, Lawrence Jr; and Stankovich, Marian T., "Electrochemical Properties of the Diiron Core of Uteroferrin and Its Anion Complexes" (1991). Chemistry Faculty Research and Publications. 328.
https://epublications.marquette.edu/chem_fac/328