Interdisciplinary Biotechnology Program in Environmental DehalogenationEPA Grant Number: R827612E02
Title: Interdisciplinary Biotechnology Program in Environmental Dehalogenation
Investigators: Marton, Laszlo , Chen, Yung-Pin , Czako, Mihaly , Dawson, John , Leiboda, Lukasz , Lincoln, David E. , Lovell, Charles R. , Morris, James T. , Woodin, Sarah A. , Yoch, Duane
Current Investigators: Sawyer, Roger , Chen, Yung-Pin , Czako, Mihaly , Dawson, John , Leiboda, Lukasz , Lincoln, David E. , Little, T. Scott , Lovell, Charles R. , Marton, Laszlo , Morris, James T. , Woodin, Sarah A. , Yoch, Duane
Institution: University of South Carolina at Columbia
EPA Project Officer: Chung, Serena
Project Period: June 1, 1999 through May 30, 2002
Project Amount: $246,999
RFA: EPSCoR (Experimental Program to Stimulate Competitive Research) (1998) RFA Text | Recipients Lists
Research Category: EPSCoR (The Experimental Program to Stimulate Competitive Research)
The objectives of this project are to: 1) optimize the catalytic properties of the dehaloperoxidase from the polychaete sea worm Amphitrite ornata; 2) characterize the dehaloperoxidases from the plant Spartina alterniflora and a bacterial isolate: determine substrate range, gene and protein sequence; optimize the purification procedures, and characterize the enzymes using kinetics, spectroscopy and X-ray crystallography; 3) determine consensus sequences and regions important for function and substrate specificity; 4) tailor the nucleotide sequence of the dehaloperoxidase gene that shows greatest stability to fit the consensus sequence required for broader substrate specificity determined by careful analysis of the three-dimensional structure to create a single biocatalyst of superior qualities; 5) improve human resources and physical infrastructure and hire a new tenure-track faculty.
The overall design is to go from individual enzymatic activities and protein N-terminal sequence data from organisms of different types, to protein structure deduced from nucleotide sequences, to delineation of a consensus structure. This project will significantly improve our understanding of how phylogenetically distant organisms have developed solutions to deal with diverse natural halogenated organic "contaminants" in sediments and waters and how dehaloperoxidases can be tailored to our needs in dealing with anthropogenic halogenated organic contaminants in the environment.
Specific results: 1) the detailed structure of dehaloperoxidases, a novel class of enzymes of great remediation potential; 2) identification of the conserved regions and structural themes common to dehaloperoxidases from different organisms, as well as determination of regions important for dehaloperoxidase function and substrate specificity; 3) data on how and to what extent dehaloperoxidase enzymes can be modified to suit our needs to deal with anthropogenic halogenated organic contaminants; 4) cloned wild-type and chimeric dehaloperoxidase genes and the corresponding transgenic organisms that can potentially be used in remediation technologies (with special consideration in phytoremeditaion); 5) improved human resources and physical infrastructure.