Vanadate-dependent peroxidases,

A similiar approach was performed by van de Velde (1999), using incorporation of vanadate into an acid phosphatase (phytase) to create a semi-synthetic peroxidase similar to the heme-dependent chloroperoxidase. The latter is a useful enzyme for the asymmetric epoxidation of olefins, but less stable due to oxidation of the porphyrin ring and difficult to express outside the native fungal host. The authors exploited the structural similarity of active sites from vanadate-dependent halo-peroxidases and acid phosphatases and have shown the useful application as an enantioselective catalyst for the synthesis of chiral sulfoxides (van de Velde, 1999). 

Table 4.5 Selected bond lengths (in A) for vanadate-dependent peroxidases from single crystal X-ray diffraction analysis (XRD) and X-ray absoption spectroscopy (XAS). See Figure 4.16a-d for structure representations and numbering of the amino acids.

VANADIUM ENZYMES/MODELS Vanadate-Dependent Peroxidases... 

Fig. 4. Model reactions and catalysts for vanadate-dependent peroxidases. See the text for details.

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