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This release is available in German.
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
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| Contact: Julian Chen chen@chemie.uni-frankfurt.de 49-697-982-9641 Goethe University Frankfurt Source:Eurekalert |
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