title: Bromine K-edge EXAFS studies of bromide binding to bromoperoxidase from Ascophyllum nodosum.
abstract: Bromine K-edge EXAFS studies have been carried out for bromide/peroxidase samples in Tris buffer at pH 8. The results are compared with those of aqueous (Tris-buffered) bromide and vanadium model compounds containing Br-V, Br-C(aliphatic) and Br-C(aromatic) bonds. It is found that bromide does not coordinate to the vanadium centre. Rather, bromine binds covalently to carbon. A possible candidate is active site serine.
authors.affiliation: Fachbereich Biologie, Universität Marburg, D-35032, Marburg, Germany.
authors.forename: H
authors.initials: H
authors.lastname: Dau
authors.forename: J
authors.initials: J
authors.lastname: Dittmer
authors.forename: M
authors.initials: M
authors.lastname: Epple
authors.forename: J
authors.initials: J
authors.lastname: Hanss
authors.forename: E
authors.initials: E
authors.lastname: Kiss
authors.forename: D
authors.initials: D
authors.lastname: Rehder
authors.forename: C
authors.initials: C
authors.lastname: Schulzke
authors.forename: H
authors.initials: H
authors.lastname: Vilter
mesh_terms: D001965:Bromides / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D010545:Peroxides / Q000378:metabolism; D000459:Phaeophyceae / Q000201:enzymology*; D014639:Vanadium / Q000378:metabolism
chemical_list: D001965:Bromides; D010545:Peroxides; D014639:Vanadium; D010544:Peroxidases; C026195:bromide peroxidase