This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Studies into the nature of substrate and small molecule effects on the geometric and electronic structure of non-heme iron enzymes will be continued. XAS pre-edge and edge studies will provide insight into the nature of the changes in coordination number, charge donation and covalency in these systems upon substrate binding. EXAFS analysis will contribute corresponding bond length changes. Comparison with magnetic circular dichroism, electron paramagnetic resonance, and UV-VIS absorption data being collected in our laboratories will allow for a detailed structure-function correlation and insights into the mechanisms of these enzymes. Furthermore, the intermediates of these systems will be investigated using nitrosyl (NO) as a dioxygen analogue. The enzyme-NO studies will first be calibrated using a series of NO model complexes and then extended to some of the protein systems. Using rapid-freeze techniques, intermediates will be studied for those systems where they can be trapped cleanly in significant quantities.
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