Specifically, the scientists saw that naphthalene dioxygenase, a bacterial enzyme, can bind oxygen (to iron) in a side-on fashion and add it on to naphthalene, a hydrocarbon molecule. The discovery is a result of the first three-dimensional imaging of naphthalene dioxygenase, a member of the family of enzymes called Rieske dioxygenases. The findings could help lead to the development of microorganisms that can clean up toxic and cancer-causing waste in the environment and to the development of novel drugs. The research results appear in the Feb. 14 issue of Science.
"The more we know about how enzymes catalyze reactions, the better able we are to modify them -- to improve or stop reactions, as desired" said S. Ramaswamy, Ph.D., UI professor of biochemistry and one of the study's authors.
"The question was: how does the enzyme actually work at the molecular level?" said David Gibson, Ph.D., UI professor of microbiology and one of the study's authors, whose previous research led to the discovery of the Rieske dioxygenase family of enzymes.
That seemingly straightforward question required seven years of collaborative work between the UI and the researchers in Sweden, beginning in 1996, and included assistance from the UI Center for Biocatalysis and Bioprocessing.
Ramaswamy and Gibson began research related to this investigation when Ramaswamy was a faculty member in the molecular biology department at Swedish University of Agricultural Sciences in Uppsala, Sweden. The paper's lead author is Andreas Karlsson, who was a graduate student of Ramaswamy's at the Swedish University and currently works for Avent
Contact: Becky Soglin
University of Iowa