A purple acid phosphatase from sweet potato contains an antiferromagnetically coupled binuclear Fe-Mn center

Schenk, Gerhard, Boutchard, Clare L., Carrington, Lyle E., Noble, Christopher J., Moubaraki, Boujemaa, Murray, Keith S., de Jersey, John, Hanson, Graeme R. and Hamilton, Susan (2001) A purple acid phosphatase from sweet potato contains an antiferromagnetically coupled binuclear Fe-Mn center. Journal of Biological Chemistry, 276 22: 19084-19088. doi:10.1074/jbc.M009778200

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Author Schenk, Gerhard
Boutchard, Clare L.
Carrington, Lyle E.
Noble, Christopher J.
Moubaraki, Boujemaa
Murray, Keith S.
de Jersey, John
Hanson, Graeme R.
Hamilton, Susan
Title A purple acid phosphatase from sweet potato contains an antiferromagnetically coupled binuclear Fe-Mn center
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2001-01-01
Year available 2001
Sub-type Article (original research)
DOI 10.1074/jbc.M009778200
Open Access Status File (Publisher version)
Volume 276
Issue 22
Start page 19084
End page 19088
Total pages 5
Place of publication Bethesda
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Subject C1
270108 Enzymes
780105 Biological sciences
Abstract A purple acid phosphatase from sweet potato is the first reported example of a protein containing an enzymatically active binuclear Fe-Mn center. Multifield saturation magnetization data over a temperature range of 2 to 200 K indicates that this center is strongly antiferromagnetically coupled. Metal ion analysis shows an excess of iron over manganese. Low temperature EPR spectra reveal only resonances characteristic of high spin Fe(III) centers (Fe(III)-apo and Fe(III)-Zn(II)) and adventitious Cu(II) centers. There were no resonances from either Mn(II) or binuclear Fe-Mn centers. Together with a comparison of spectral properties and sequence homologies between known purple acid phosphatases, 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. Because of the strong antiferromagnetism it is likely that the metal ions in the sweet potato enzyme are linked via a mu -oxo bridge, in contrast to other known purple acid phosphatases in which a mu -hydroxo bridge is present. Differences in metal ion composition and bridging may affect substrate specificities leading to the biological function of different purple acid phosphatases.
Keyword Biochemistry & Molecular Biology
Pig Allantoic Fluid
Bovine Spleen
Spectroscopic Characterization
Fluoride Complex
Q-Index Code C1
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Faculty of Science Publications
Centre for Advanced Imaging Publications
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Created: Wed, 15 Aug 2007, 01:55:52 EST