Abstract
Recent results on the structures and functions of purple acid phosphatases and catechol oxidases as well as on their model compounds are reviewed and discussed. Purple acid phosphatase from kidney beans (KBPAP) was crystallized in two modifications, and the structure is being refined at 2.8 E resolution by X-ray diffraction. The enzyme is a dimer of quasi-identical subunits connected by a disulfide bridge. The sequence could be determined using MALDI mass spectrometry. Structural and functional model complexes for Fe-Fe and Zn-Fe PAP’s were prepared with new dinucleating ligands, partly with bridging and terminal phosphate ligands. Some of them show considerable phosphatase activity and, like the enzyme itself, also appear to have oxygen-activating properties. EXAFS and XANES on KBPAP indicate rather long metal-metal distances as compared to the values proposed for uteroferrin. The rather weak antiferromagnetic coupling in the beef spleen phosphatase (as well as in the model compounds) and the X-ray diffraction data suggest hydroxo bridging of the metals in the enzyme rather than oxo bridging.
Two catechol oxidases with Cu(II)-Cu(II) active centers were isolated, purified, and characterized. Dinuclear and tetranuclear model complexes were synthesized with tri-, penta- and heptadentate dinucleating ligands containing bridging phenolate or alcoholate groups. Correlations are obtained between the coordination numbers, properties of the donor groups and catalytic activity, dinuclear Cu(II) complexes with tridentate ligands like 2,6-bis(morpholinyl-N-methyl)-4-methylphenol being the most active. Catechol oxidase as well as its biomimetic model complexes are investigated as possible active elements in bio- and chemosensors for the analysis of hormones and neurotransmitters like adrenaline in medical diagnosis. Molecular modeling methods are employed favourably during these investigations.
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Krebs, B. (1995). Purple Acid Phosphatases and Catechol Oxidase and their Model Compounds. Crystal Structure Studies of Purple Acid Phosphatase from Red Kidney Beans. In: Kessissoglou, D.P. (eds) Bioinorganic Chemistry. NATO ASI Series, vol 459. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-0255-1_28
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DOI: https://doi.org/10.1007/978-94-011-0255-1_28
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