This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Although mitochondrial iron homeostasis is essential for cell viability, it is a mechanism that is poorly understood. Mitochondrial iron is required for heme and iron-sulfur cluster assembly and deficiency causes a collapse in metalloprotein biosynthesis, disrupting cellular pathways where enzymes that require these cofactors participate. However, overabundance of mitochondrial iron leads to oxidative stress in the cell, since iron is highly reactive. Cells have therefore developed protein controlled mechanisms to regulate mitochondrial iron concentrations at the level of metal import, export and possibly metal storage. Cellular respiration is controlled in the mitochondria by metalloproteins, so strict control of mitochondrial iron concentrations is essential for maintaining cell function and also to prevent metal toxicity. A goal of our lab is to characterize the function of two proteins involved in mitochondrial iron homeostasis and cellular respiration. Using XAS spectroscopy, we will characterize the iron active-site structure and reaction mechanism for these proteins to decipher their role in maintaining normal cellular function.
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