Bioremediation Using Dehaloperoxidase
Abstract
The project addresses the need to develop biological approaches to detoxifiy the environment. We have studied the first known hemoglobin that has a natural peroxidase function. The hemoglobin was first isolated from the marine worm (terebellid polychaete) Amphitrite ornata, but has been cloned and expressed in E. coli bacteria. During the grant period we discovered a principle of action of such peroxidases, namely internal inhibition by para-halophenols. This information permits further progress to be made in cloning and expressing bioremediation enzymes capable of degrading environmental pollutants such as 2,4-dichlorophenol, which is a byproduct of the insecticide 2,4-D and a precursor to highly toxic dioxins. We have published numerous X-ray crystal structures and nuclear magnetic resonance data to support the conclusions. We have carried out extensive enzymatic kinetic assays to demonstrate the utility of dehaloperoxidase for bioremediation applications.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 01, 2011
- Accession Number
- ADA545331
Entities
People
- Stefan Franzen
Organizations
- North Carolina State University