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Abstract
X-ray absorption spectroscopy (XAS) was used to investigate structure, function, and mechanistic details of enzymatic catalysis in a variety of biological systems. Most significantly, these studies have resulted in the proposal for a mechanism for radical generation in the enzyme lysine aminomutase, as well as generating understanding about the active site and inhibiter-binding mode of methionyl aminopeptidase, an enzymatic target for anti-cancer drugs. Other biological systems that were studied include urease, neuronal nitric oxide synthase, cytochrome bo3, an accessory protein of the nitric oxide reductase (nos) gene cluster, Archaeal zinc-containing ferredoxin, heavy metal responsive regulator proteins, Archaeal transcription factor, and beta-carbonic anhydrase.|Additionally, in an effort to design a biological pathway for the degradation of environmental contaminants, particularly halogenenated aromatic compounds, the substrate specificity of catechol dioxygenase was rationally designed to significantly increase its ability to cleave halogenated and substituted catechols.