BIOL 250 |
| Halophenols are industrial pollutants that pose both environmental and health hazards. Herein, how a catalytic globin, dehaloperoxidase (DHP) from the marine worm Amphitrite ornata, has evolved to be bi-functional as an oxygen transport protein and a catalyst for halophenol detoxification is discussed. Cloning DHP demonstrates that dehaloperoxidase activity is inherent to the protein. Magnetic circular dichroism spectroscopy revealed the His-ligated active site is more similar to horse heart myoglobin than to horseradish peroxidase, the limiting examples of globin and peroxidase proteins. Rapid scan stopped-flow spectroscopy has been employed to examine the roles of high-valent heme intermediates during the oxidative dehalogenation of halophenols. Additionally, we demonstrate the use of the most versatile heme peroxidase, chloroperoxidase from Caldariomyces fumago, as a potential bioremediation catalyst for the breakdown of toxic haloaromatics. Furthermore, how halophenols interact with oxygen transport proteins, like myoglobin, under conditions of oxidative stress has been examined. |
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Enzymes
4:30 PM-6:30 PM, Wednesday, 13 September 2006 Moscone Center -- Hall D, Poster
Sci-Mix
Division of Biological Chemistry |