INOR 767 |
| Cysteine dioxygenase (CDO) is a non-heme iron enzyme that can be found in mammalian tissue. It is mainly localized in the liver but is also present in the brain, kidney, and adipose tissue. CDO converts cysteine to cysteine sulfinic acid, which is the first step in cysteine metabolism in the human body. CDO contains a novel covalent linkage located near the metal binding site that is present in another enzyme, galactose oxidase, where it is essential to functional enzyme. This suggests that the linkage may play an important role in CDO as well. Also the iron site was studied using XAS and crystallography revealing many different binding motifs containing varying numbers of ligands. CDO differs from the rest of the cupin super family in that it does not contain a 2-his-1-carboxylate binding motif but rather the carboxylate is replaced with another histidine. The covalent linkage and metal binding site were studied using site directed mutagenesis and XAS.
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Bioinorganic Chemistry: Enzymes and Coenzymes
7:00 PM-10:00 PM, Tuesday, August 21, 2007 BCEC -- Exhibit Hall - B2, Poster
Sci-Mix
Division of Inorganic Chemistry |
