Water and bromide in the active center of vanadate-dependent haloperoxidases |
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Authors: | Rehder D Schulzke C Dau H Meinke C Hanss J Epple M |
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Affiliation: | Institut für Anorganische und Angewandte Chemie, Universit?t Hamburg, Germany. rehder@xray.chemie.uni-hamburg.de |
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Abstract: | Two aqua-oxovanadium complexes, viz. [A-VO(H2O)(sal-L-Leu)] (1) and [VO(H2O)2(5-Br-sal-Gly)] x H2O(2 x H2O), containing the water ligands in cis- and trans-positions to the oxo group at V-OH2 distances ranging from 2.008 to 2.228 A, have been structurally characterized in order to model the apical electron density feature found in the structures of fungal and algal vanadate-dependent peroxidases. Br K-edge XAS of bromide-treated bromoperoxidase from Ascophyllum nodosum and model compounds (including 2 x H2O) has been used to show that the substrate bromide does not bind to active site vanadium but to a light atom, possibly carbon, in its vicinity. |
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