NMR STUDIES OF HUMAN FERREDOXIN

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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. NMR will be used to probe the origin of the spectroscopic differencesbetween reduced vertebrate and chloroplast [2Fe-2S] ferredoxins and the conformational changes that reduction induces to the protein in vertebrate ferredoxins. Selective isopotic labeling will be used to assign resonances from amino acids at and nearby the cluster. These data will then be analyzed with density functional calculations. 2-D and 3-D NMR experiments on globally C13 and N15 labeled samples will be used to obtain solution structure information of the protein in both redox states, thereby providing a picture of the reduction-induced conformational changes. This, combined with a detailed picture of the geometric and electronic structure of the active site cluster obtained from the analysis of the paramagnetically shifted region, will provide detailed insight into the orgin of this conformational change.