Vanadium containing bromoperoxidase--insights into the enzymatic mechanism using X-ray crystallography.
Garcia Rodriguez, E
Journal of Inorganic Biochemistry
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.
addresses: School of Biosciences, University of Exeter, Exeter, UK. J.A.Littlechild@exeter.ac.uk
types: Journal Article; Research Support, Non-U.S. Gov't
Copyright © 2009 Elsevier. NOTICE: this is the author’s version of a work that was accepted for publication in Journal of Inorganic Biochemistry. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Journal of Inorganic Biochemistry, 2009, Vol. 103, Issue 4, pp. 617 – 621 DOI: 10.1016/j.jinorgbio.2009.01.011
Journal of Inorganic Biochemistry, 2009, Vol. 103, Issue 4, pp. 617 - 621
Place of publication