Structure Of Enzyme Against Chemical Warfare Agents Determined

January 29, 2009 at 2:00 pm Leave a comment


The enzyme DFPase from the squid Loligo vulgaris, is able to rapidly and efficiently detoxify chemical warfare agents such as Sarin, which was used in the Tokyo subway attacks in 1995. A detailed understanding of the mechanism by which enzymes catalyze chemical reactions is necessary for efforts aiming to improve their properties. A group of researchers at the University of Frankfurt, the Bundeswehr Institute for Pharmacology and Toxicology in Munich, and Los Alamos National Laboratory in New Mexico, USA, have successfully determined the structure of DFPase using neutron diffraction. They report their findings in the 20 January 2009 issue of the journal Proceedings of the National Academy of Sciences (106(3), 713-718).





The team used the neutron source at Los Alamos National Laboratory, one of only three sources worldwide equipped for protein crystallography. In contrast to structure determination using X-rays, neutrons are able to locate the positions of hydrogen atoms, which make up half of all atoms in proteins, and are crucial for chemical reactions. As X-rays interact with the electron cloud around an atomic nucleus, so heavier elements are more easily seen, while neutrons interact with the atomic nuclei, and atoms in proteins such as hydrogen, oxygen, nitrogen, carbon, and sulfur, all scatter neutrons in a similar manner. Yet despite being so widespread, hydrogen atoms in proteins are quite elusive. As X-rays interact with the electron cloud around an atomic nucleus, hydrogen atoms, with only one electron, are normally invisible in structures. In contrast, neutrons interact with the atomic nuclei, such that atoms in proteins, hydrogen, oxygen, nitrogen, carbon, and sulfur, all scatter neutrons in a similar manner. The two techniques therefore yield complementary information about a protein structure. This information about hydrogen atoms is therefore essential for a basic understanding of the reaction mechanism of DFPase.





Neutron structures of proteins are quite rare and technically demanding, requiring large crystals and long measurement times. Though the first neutron structure of a protein was reported 40 years ago, in 1969, to date only about 20 unique structures have been solved, out of 50000 entries in the Protein Data Bank. ” The effort has been absolutely worth it, ” says Junior-Prof. Julian Chen, who published this work together with Dr. Marc-Michael Blum and Prof. Heinz Rueterjans. ” Based on the results of this study, we can now create targeted changes to DFPase to augment the activity, as well as diversify the substrate range of the enzyme.”





—————————-

Article adapted by Medical News Today from original press release.

—————————-





This release is available in German.





Source: Julian Chen


Goethe University Frankfurt

[Via http://www.medicalnewstoday.com]

Advertisements

Entry filed under: Uncategorized.

Urinary Incontinence Reduced By Weight Loss In Overweight And Obese Women Weight Loss Reduced Incontinence In Overweight And Obese Women

Leave a Reply

Fill in your details below or click an icon to log in:

WordPress.com Logo

You are commenting using your WordPress.com account. Log Out / Change )

Twitter picture

You are commenting using your Twitter account. Log Out / Change )

Facebook photo

You are commenting using your Facebook account. Log Out / Change )

Google+ photo

You are commenting using your Google+ account. Log Out / Change )

Connecting to %s

Trackback this post  |  Subscribe to the comments via RSS Feed


Archives

Top Clicks

  • None

Blog Stats

  • 15,556 hits

%d bloggers like this: