Bromine K-edge EXAFS studies of bromide binding to bromoperoxidase from Ascophyllum nodosum.
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.
Dau
H
H
Fachbereich Biologie, Universität Marburg, D-35032, Marburg, Germany.
Dittmer
J
J
Epple
M
M
Hanss
J
J
Kiss
E
E
Rehder
D
D
Schulzke
C
C
Vilter
H
H
D001965:Bromides / Q000378:metabolism*; D010544:Peroxidases / Q000378:metabolism*; D010545:Peroxides / Q000378:metabolism; D000459:Phaeophyceae / Q000201:enzymology*; D014639:Vanadium / Q000378:metabolism
D001965:Bromides; D010545:Peroxides; D014639:Vanadium; D010544:Peroxidases; C026195:bromide peroxidase