Direct electrochemistry of porcine purple acid phosphatase (uteroferrin)


Autoria(s): Bernhardt, P. V.; Schenk, G.; Wilson, G. J.
Data(s)

01/01/2004

Resumo

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 (Fe-III-Fe-II --> Fe-III-Fe-III) 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.

Identificador

http://espace.library.uq.edu.au/view/UQ:71952

Idioma(s)

eng

Publicador

Amer Chemical Soc

Palavras-Chave #Biochemistry & Molecular Biology #Pig Allantoic Fluid #Soluble Methane Monooxygenase #Active-site #Reduced Uteroferrin #Crystal-structure #Anion Complexes #Hydroxo-bridge #Bovine Spleen #Sweet-potato #Fe-mn #C1 #250204 Bioinorganic Chemistry #780103 Chemical sciences
Tipo

Journal Article