X-ray absorption studies of the purple acid phosphatase from beef spleen

S. M. Kauzlarich, B. K. Teo, T. Zirino, S. Burman, J. C. Davis, B. A. Averill

Research output: Contribution to journalArticle

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Abstract

Iron K-edge near-edge (XANES) and extended X-ray absorption fine structure (EXAFS) spectra have been measured for the purple acid phosphatase from beef spleen and for several oxo-bridged model complexes. The XANES show a shift of the absorption edge to lower energy by 2.0 eV upon reduction of the purple form of the enzyme to the pink form, consistent with reduction of one of the iron atoms. Fourier transforms of the EXAFS data of the purple form of the enzyme show three peaks, assigned to Fe-O(N) (first shell), Fe-Fe and Fe-P or Fe-C (second shell), and Fe-C(N) (imidazole, third shell) scatterers, in order of increasing distance. Best fits of the individually back-transformed peaks using theoretical functions are consistent with the indicated assignments. The Fe- -Fe distance of 3.00 Å is consistent with a bridged binuclear iron center in the enzyme. Due to the presence of short Fe-O(tyrosine) linkages at 1.8-1.9 Å, direct evidence for a bridging oxo group at ca. 1.8 Å could not be obtained. The observed Fe-P distance of 3.06 Å is most consistent with the presence of a phosphate as a monodentate ligand to one iron atom in the purple (oxidized) form of the enzyme.

Original languageEnglish (US)
Pages (from-to)2781-2785
Number of pages5
JournalInorganic Chemistry
Volume25
Issue number16
StatePublished - 1986
Externally publishedYes

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Beef
phosphatases
spleen
X ray absorption
enzymes
Iron
iron
acids
Enzymes
x rays
fine structure
Atoms
tyrosine
imidazoles
linkages
Tyrosine
atoms
Fourier transforms
phosphates
Phosphates

ASJC Scopus subject areas

  • Inorganic Chemistry

Cite this

Kauzlarich, S. M., Teo, B. K., Zirino, T., Burman, S., Davis, J. C., & Averill, B. A. (1986). X-ray absorption studies of the purple acid phosphatase from beef spleen. Inorganic Chemistry, 25(16), 2781-2785.

X-ray absorption studies of the purple acid phosphatase from beef spleen. / Kauzlarich, S. M.; Teo, B. K.; Zirino, T.; Burman, S.; Davis, J. C.; Averill, B. A.

In: Inorganic Chemistry, Vol. 25, No. 16, 1986, p. 2781-2785.

Research output: Contribution to journalArticle

Kauzlarich, SM, Teo, BK, Zirino, T, Burman, S, Davis, JC & Averill, BA 1986, 'X-ray absorption studies of the purple acid phosphatase from beef spleen', Inorganic Chemistry, vol. 25, no. 16, pp. 2781-2785.
Kauzlarich SM, Teo BK, Zirino T, Burman S, Davis JC, Averill BA. X-ray absorption studies of the purple acid phosphatase from beef spleen. Inorganic Chemistry. 1986;25(16):2781-2785.
Kauzlarich, S. M. ; Teo, B. K. ; Zirino, T. ; Burman, S. ; Davis, J. C. ; Averill, B. A. / X-ray absorption studies of the purple acid phosphatase from beef spleen. In: Inorganic Chemistry. 1986 ; Vol. 25, No. 16. pp. 2781-2785.
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AB - Iron K-edge near-edge (XANES) and extended X-ray absorption fine structure (EXAFS) spectra have been measured for the purple acid phosphatase from beef spleen and for several oxo-bridged model complexes. The XANES show a shift of the absorption edge to lower energy by 2.0 eV upon reduction of the purple form of the enzyme to the pink form, consistent with reduction of one of the iron atoms. Fourier transforms of the EXAFS data of the purple form of the enzyme show three peaks, assigned to Fe-O(N) (first shell), Fe-Fe and Fe-P or Fe-C (second shell), and Fe-C(N) (imidazole, third shell) scatterers, in order of increasing distance. Best fits of the individually back-transformed peaks using theoretical functions are consistent with the indicated assignments. The Fe- -Fe distance of 3.00 Å is consistent with a bridged binuclear iron center in the enzyme. Due to the presence of short Fe-O(tyrosine) linkages at 1.8-1.9 Å, direct evidence for a bridging oxo group at ca. 1.8 Å could not be obtained. The observed Fe-P distance of 3.06 Å is most consistent with the presence of a phosphate as a monodentate ligand to one iron atom in the purple (oxidized) form of the enzyme.

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