Literature DB >> 1653614

Reactivation of vanadium bromoperoxidase; inhibition by metallofluoric compounds.

M Tromp1, T T Van, R Wever.   

Abstract

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.

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Year:  1991        PMID: 1653614     DOI: 10.1016/0167-4838(91)90023-s

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

1.  From phosphatases to vanadium peroxidases: a similar architecture of the active site.

Authors:  W Hemrika; R Renirie; H L Dekker; P Barnett; R Wever
Journal:  Proc Natl Acad Sci U S A       Date:  1997-03-18       Impact factor: 11.205

  1 in total

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