X-RAY-ABSORPTION STUDIES OF THE PURPLE ACID-PHOSPHATASE FROM RED KIDNEY BEANS (NATIVE ENZYME, METAL EXCHANGED FORM)

Authors
AHLERS F ZIPPEL F KLABUNDE T KREBS B LOCKE R WITZEL H NOLTING HF
Citation
F. Ahlers et al., X-RAY-ABSORPTION STUDIES OF THE PURPLE ACID-PHOSPHATASE FROM RED KIDNEY BEANS (NATIVE ENZYME, METAL EXCHANGED FORM), Physica. B, Condensed matter, 209(1-4), 1995, pp. 731-732
Citations number
8
Categorie Soggetti
Physics, Condensed Matter
Journal title
Physica. B, Condensed matter → ACNP
ISSN journal
09214526
Volume
209
Issue
1-4
Year of publication
1995
Pages
731 - 732
Database
ISI
SICI code
0921-4526(1995)209:1-4<731:XSOTPA>2.0.ZU;2-P
Abstract
Purple acid phosphatase from red kidney beans (KBP) catalyzes the hydr olysis of activated phosphoric acid monoesters and contains a heterodi nuclear Fe(III)-Zn(II) core in its active site. Iron K-edge X-ray abso rption data have been obtained for the native enzyme and for a metal e xchanged derivative, where Zn(II) was substituted by Fe(III). The envi ronment of the native enzyme consists of 2.5 O/N at 1.91 Angstrom, 3 O /N at 2.09 Angstrom, and 1 Zn at 4.05 Angstrom. For the metal exchange d form we obtained 2.5 O/N at 1.94 Angstrom;, 2.5 O/N at 2.09 Angstrom , and 1 Fe at 3.79 Angstrom.