| pubmed-article:20346515 | pubmed:abstractText | Vanadium K-edge X-ray Absorption Spectra have been recorded for the native and peroxo-forms of vanadium chloroperoxidase from Curvularia inaequalis at pH 6.0. The Extended X-ray Absorption Fine Structure (EXAFS) regions provide a refinement of previously reported crystallographic data; one short V=O bond (1.54A) is present in both forms. For the native enzyme, the vanadium is coordinated to two other oxygen atoms at 1.69A, another oxygen atom at 1.93A and the nitrogen of an imidazole group at 2.02A. In the peroxo-form, the vanadium is coordinated to two other oxygen atoms at 1.67A, another oxygen atom at 1.88A and the nitrogen of an imidazole group at 1.93A. When combined with the available crystallographic and kinetic data, a likely interpretation of the EXAFS distances is a side-on bound peroxide involving V-O bonds of 1.67 and 1.88A; thus, the latter oxygen would be 'activated' for transfer. The shorter V-N bond observed in the peroxo-form is in line with the previously reported stronger binding of the cofactor in this form of the enzyme. Reduction of the enzyme with dithionite has a clear influence on the spectrum, showing a change from vanadium(V) to vanadium(IV). | lld:pubmed |
