A (17)O NMR study of peroxide binding to the active centre of bromoperoxidase from Ascophyllum nodosum.
The (17)O NMR of bromoperoxidase in Tris buffer at pH 8 treated with (17)O-enriched H2O2 reveals direct binding of peroxide to active site vanadium both in the symmetric and asymmetric modes, the latter possibly due to hydroperoxide. In addition, non-active site HVO2(O2)2(2-) is detected. The results are counter-checked with NMR data on peroxovanadium model compounds.
Casný
M
M
Institut für Anorganische und Angewandte Chemie, Universität Hamburg, Germany.
Rehder
D
D
Schmidt
H
H
Vilter
H
H
Conte
V
V
D001665:Binding Sites; D009682:Magnetic Resonance Spectroscopy; D010103:Oxygen Isotopes / Q000032:analysis*; D010544:Peroxidases / Q000378:metabolism*; D010545:Peroxides / Q000378:metabolism*; D000459:Phaeophyceae / Q000201:enzymology*; D014639:Vanadium / Q000378:metabolism*; D014673:Vecuronium Bromide / Q000378:metabolism
D010103:Oxygen Isotopes; D010545:Peroxides; D014639:Vanadium; D014673:Vecuronium Bromide; D010544:Peroxidases; C026195:bromide peroxidase