| Literature DB >> 15301537 |
Paul V Bernhardt1, Gerhard Schenk, Gregory J Wilson.
Abstract
Cyclic voltammetry of the non-heme diiron enzyme porcine purple acid phosphatase (uteroferrin, Uf) has been reported for the first time. Totally reversible one-electron oxidation responses (FeIII-FeII --> FeII-FeIII) are seen both in the absence and in the presence of weak competitive inhibitors phosphate and arsenate, and dissociation constants of these oxoanion complexes formed with uteroferrin in its oxidized state (Uf(o)) have been determined. The effect of pH on the redox potentials has been investigated in the range 3 < pH < 6.5, enabling acid dissociation constants for Uf(o) and its phosphate and arsenate complexes to be calculated.Entities:
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Year: 2004 PMID: 15301537 DOI: 10.1021/bi0490338
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162