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Vanadium containing bromoperoxidase - Insights into the enzymatic mechanism using X-ray crystallography
Littlechild, J.; Garcia Rodriguez, E.; Isupov, M. (2009). Vanadium containing bromoperoxidase - Insights into the enzymatic mechanism using X-ray crystallography. J. Inorg. Biochem. 103(4): 617-621.
In: Journal of Inorganic Biochemistry. Elsevier: New York,. ISSN 0162-0134, more
Peer reviewed article  

Available in  Authors 

Author keywords
    Vanadium bromoperoxidase enzyme; Corallina species; X-ray structuralstudies

Authors  Top 
  • Littlechild, J., more
  • Garcia Rodriguez, E.
  • Isupov, M.

    The X-ray crystal structure of the vanadium bromoperoxidase from the red algae Corallina pilulifera has been solved in the presence of the known substrates, phenol red and phloroglucinol. A putative substrate binding site has been observed in the active site channel of the enzyme. In addition bromide has been soaked into the crystals and it has been shown to bind unambiguously within the enzyme active site by using the technique of single anomalous dispersion. A specific leucine amino acid is seen to move towards the bromide ion in the wild-type enzyme to produce a hydrophobic environment within the active site. A mutant of the enzyme where arginine 397 has been changed to tryptophan, shows a different behaviour on bromide binding. These results have increased our understanding of the mechanism of the vanadium bromoperoxidases and have demonstrated that the substrate and bromide are specifically bound to the enzyme active site.

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