The di-iron core of mammalian purple acid phosphatases has been reproduced in the plant enzyme from kidney bean (Mr 111000) upon insertion of an Fe(II) ion in place of the native zinc(II) in the dinuclear Fe(III)Zn(II) core. The shortening of the electronic relaxation time of the metal centre allows detection of hyperfine-shifted 1H NMR resonances, although severe broadening due to Curie relaxation prevents independent signal assignment. Nevertheless, comparison of the spectral features of the structurally characterized plant enzyme with those of the mammalian species, which were previously extensively assigned, is consistent with a close similarity of the metal-binding sites, also suggested by previous sequence-alignment studies. Some differences appear to be mainly localized at the M(II) site. Spectral comparison was also carried out on the Fe(III)Co(II) derivatives.
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Research Article|
May 01 1997
Evidence for a conserved binding motif of the dinuclear metal site in mammalian and plant purple acid phosphatases: 1H NMR studies of the di-iron derivative of the Fe(III)Zn(II) enzyme from kidney bean
Gianantonio BATTISTUZZI;
Gianantonio BATTISTUZZI
‡
*Department of Chemistry, University of Modena, Via Campi 183, 41100 Modena, Italy
‡To whom correspondence should be addressed.
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Markus DIETRICH;
Markus DIETRICH
†Institute of Biochemistry, Westfälische Wilhelms-Universität, Wilhelm-Klemm Str. 2, D-48149 Münster, Germany
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Renate LÖCKE;
Renate LÖCKE
†Institute of Biochemistry, Westfälische Wilhelms-Universität, Wilhelm-Klemm Str. 2, D-48149 Münster, Germany
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Herbert WITZEL
Herbert WITZEL
§
†Institute of Biochemistry, Westfälische Wilhelms-Universität, Wilhelm-Klemm Str. 2, D-48149 Münster, Germany
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Publisher: Portland Press Ltd
Received:
January 29 1997
Revision Received:
February 25 1997
Accepted:
February 28 1997
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1997
1997
Biochem J (1997) 323 (3): 593–596.
Article history
Received:
January 29 1997
Revision Received:
February 25 1997
Accepted:
February 28 1997
Citation
Gianantonio BATTISTUZZI, Markus DIETRICH, Renate LÖCKE, Herbert WITZEL; Evidence for a conserved binding motif of the dinuclear metal site in mammalian and plant purple acid phosphatases: 1H NMR studies of the di-iron derivative of the Fe(III)Zn(II) enzyme from kidney bean. Biochem J 1 May 1997; 323 (3): 593–596. doi: https://doi.org/10.1042/bj3230593
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