Dehaloperoxidase (DHP) from the marine worm Amphitrite ornata, is a globin exhibiting significant peroxidase acitivity and is of environmental interest as it is involved in the oxidation of dehalogenation of trihalophenols.  The active site of this bifunctional enzyme is a heme center, coordinated by a histidine residue in the proximal position. This first M�ssbauer study will present the spectroscopic features of DHP in the resting states and the oxyferrous state. His 55 can close the active site in a 5-coordinated form (at low pH) or leave it open to coordinate a water ligand (high-pH). These two ferric forms coexist at all pH values and have different EPR signatures. DHP-A was studied at pH 7 and 5, in variable temperature and variable field conditions.   This study will ascertain the spin and oxidation states of the iron in the several catalytic states and will draw comparisons between DHP and other heme proteins.

Mössbauer studies of the dehaloperoxidase enzyme from <i>Amphitrite ornata</i>

244th National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.

Mössbauer studies of the dehaloperoxidase enzyme from Amphitrite ornata