Journal ArticleDOI
Magnetic susceptibility studies on the diiron forms of the metalloprotein purple acid phosphate from bovine spleen and kidney bean
Stefan Gehring,Peter Fleischhauer,M. Behlendorf,M. Hüber,Jürgen Lorösch,Wolfgang Haase,M. Dietrich,H. Witzel,R. Löcke,Bernt Krebs +9 more
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TLDR
In this paper, temperature dependent magnetic susceptibility measurements of the reduced and of the oxidized diiron forms of purple acid phosphatase from kidney bean (KBP) and from bovine spleen (BSP) have been carried out in the temperature range 4.2-220 K in order to detect the strength of the exchange coupling between the two metal centers in the active site.About:
This article is published in Inorganica Chimica Acta.The article was published on 1996-11-01. It has received 27 citations till now. The article focuses on the topics: Purple acid phosphatases.read more
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Journal ArticleDOI
The catalytic mechanisms of binuclear metallohydrolases.
TL;DR: An updated review of the current understanding of metallohydrolase-catalyzed reactions is presented, focusing on four systems, purple acid phosphatases, Ser/Thr protein phosph atases, PPs, 3′-5′ exonucleases, and 5′-nucleotidases, which have contributed to major advancement of the understanding of the catalytic mechanisms that operate in such enzymes.
Journal ArticleDOI
A Purple Acid Phosphatase from Sweet Potato Contains an Antiferromagnetically Coupled Binuclear Fe-Mn Center
Gerhard Schenk,Claire L Boutchard,Lyle E. Carrington,Christopher J. Noble,Boujemaa Moubaraki,Keith S Murray,John de Jersey,Graeme R. Hanson,Susan E. Hamilton +8 more
TL;DR: The enzymatic and spectroscopic data strongly indicate the presence of catalytic Fe(III)-Mn(II) centers in the active site of the sweet potato enzyme, which is the first reported example of a protein containing an enzymatically active binuclear Fe-Mn center.
Journal ArticleDOI
The active site of purple acid phosphatase from sweet potatoes (Ipomoea batatas) metal content and spectroscopic characterization.
Atila Durmus,Christoph Eicken,Bernd Horst Sift,Andreas Kratel,Reinhard Kappl,Jürgen Hüttermann,Bernt Krebs +6 more
TL;DR: It is shown that spPAP contains a Fe(III)-Zn(II) center in the active site as previously determined for the purple acid phosphatase from red kidney bean (kbPAP), and an alignment of the amino acid sequences suggests that the residues involved in metal-binding are identical in both plant PAPs.
Journal ArticleDOI
Magnetostructural correlations in exchange coupled phenoxo-, alkoxo-, and hydroxo-bridged dinuclear iron(III) compounds
TL;DR: In this article, a semi-empirical magnetostructural correlation for exchange coupled dinuclear asymmetrically phenoxo-, alkoxo, and hydroxo-bridged iron(III) complexes has been established.
Book ChapterDOI
The Dimetal Center in purple acid phosphatases
Thomas Klabunde,Bernt Krebse +1 more
TL;DR: In this paper, the dimetal center of PAPs has been studied using numerous spectroscopic methods such as Mossbauer spectroscopy, EPR, NMR, EXAFS, magnetic, electrochemical and resonance Raman studies characterizing most of the metal coordinating residues, the metal-metal separation and providing evidence of the similarity between enzymes from different sources.
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Journal ArticleDOI
Oxo- and hydroxo-bridged diiron complexes: a chemical perspective on a biological unit
Journal ArticleDOI
Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)-Zn(II) active site.
TL;DR: The active-site structure of the homodimeric 111-kilodalton KBPAP is consistent with previous proposals regarding the mechanism of phosphate ester hydrolysis involving nucleophilic attack on the phosphate group by an Fe(III)-coordinated hydroxide ion.
Journal ArticleDOI
Proteins containing oxo-bridged dinuclear iron centers: a bioinorganic perspective
John B. Vincent,Bruce A. Averill +1 more