Reactivation of vanadium bromoperoxidase; inhibition by metallofluoric compounds.
The effect of phosphate analogs (pyrophosphate, aluminofluoride and beryllofluoride complexes) on the reactivation of apobromoperoxidase by vanadate was studied. P2O7(4-) inhibited the reactivation in the millimolar range. Of the different aluminofluoride complexes, only AlF4- was inhibitory. In addition, BeF4(2-) also appeared to bind with high affinity to the apobromoperoxidase, thus inhibiting the reactivation very strongly. The inhibition observed supports a mechanism in which the fluorometallic complexes act as analogs of vanadate and bind accordingly to the apobromoperoxidase.
Tromp
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M
E.C. Slater Institute for Biochemical Research, University of Amsterdam, The Netherlands.
Van
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Wever
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D000535:Aluminum / Q000494:pharmacology*; D017607:Aluminum Compounds; D001608:Beryllium / Q000494:pharmacology*; D011756:Diphosphates / Q000494:pharmacology*; D004789:Enzyme Activation; D005459:Fluorides / Q000494:pharmacology*; D010544:Peroxidases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000459:Phaeophyceae / Q000201:enzymology
D017607:Aluminum Compounds; D011756:Diphosphates; C035982:beryllium fluoride; D000535:Aluminum; D010544:Peroxidases; C026195:bromide peroxidase; D001608:Beryllium; D005459:Fluorides; C032311:aluminum fluoride