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. We propose to extend our previous studies on blue copper and CuA sites, using a combination of S K-, Cu L-, and Cu K-edge and EXAFS spectroscopies, to define the electronic and geometric structure of Cu-containing proteins involved in electron transfer and O2 activation. We plan to study axial mutants and H-bonding mutants of blue-copper proteins to evaluate the changes in ET properties due to these perturbations. Investigation of CuA axial and equatorial mutants will be combined with a pH dependent study to understand the role of these mutants in tuning the redox potential and ET properties of the site. We also plan to study model complexes of mononuclear, binuclear, and multinuclear Cu and Heme-Cu containing proteins that are involved in O2 binding and activation to understand mechanistic pathways of O2 activation in the proteins. The model study will be extended and correlated to the protein systems to further understand their reactivity.
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