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Papers In Press, published online ahead of print April 11, 2006
J. Biol. Chem, 10.1074/jbc.M601269200
Submitted on February 9, 2006
Revised on April 3, 2006
Accepted on April 11, 2006

Probes of the catalytic site of cysteine dioxygenase

Sergio C. Chai, John R. Bruyere, and Michael J. Maroney

Department of Chemistry, University of Massachusetts, Amherst, MA 01003

Corresponding Author: mmaroney{at}chemistry.umass.edu

The first major step of cysteine catabolism, the oxidation of cysteine to cysteine sulfinic acid (CSA), is catalyzed by cysteine dioxygenase (CDO). In the present work, we utilize recombinant rat liver CDO and cysteine derivatives to elucidate structural parameters involved in substrate recognition, and x-ray absorption spectroscopy to probe the interaction of the active site iron center with cysteine. Kinetic studies using cysteine structural analogs show that most are inhibitors and that a terminal functional group bearing a negative charge (e.g., a carboxlyate) is required for binding. The substrate-binding site has no stringent restrictions with respect to the size of the amino acid. Lack of the amino or carboxyl groups at the alpha-carbon does not prevent the molecules from interacting with the active site. In fact, cysteamine is shown to be a potent activator of the enzyme without being a substrate. CDO was also rendered inactive upon complexation with the metal-binding inhibitors azide and cyanide. Unlike many non-heme iron dioxygenases that employ alpha-keto acids as cofactors, CDO was shown to be the only dioxygenase known to be inhibited by alpha-ketoglutarate.


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