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We study structure-function relationships in heme proteins that play important roles in human physiology as well as those that have potential for application to biotechnological processes. We are exploring the structural features that control enzyme activities, including active site environments, substrate-assisted catalysis and protein environmental conditions. These goals are achieved using mainly resonance Raman (rR) spectroscopy, which is a particularly effective probe of heme-containing enzymes. We also use the combination of rR spectroscopy with the cryoradiolysis method to generate, trap and structurally characterize unstable intermediates involved in the enzymatic cycles of these heme proteins.
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