Abstract Details 146

Combine Metal K-edge XAS/EXAFS and Ligand (S) K-edge XAS Methods to Understand The Metal Ion Specific Response of NikR Proteins
Abstract ID 146
Presenter Yang Ha
Presentation Type Poster
Full Author List Heidi Hu, Michael Maroney, Britt Hedman, Keith Hodgson, Edward Solomon

Stanford University


NikR protein is a nickel-responsive regulatory protein involved in controlling the concentration intracellular Ni pool in E. coli. Metal K-edge XAS/EXAFS on different metal variant of NikR provided geometric information that different metal ions occupied different binding sites in the protein. Ligand (sulfur) K-edge XAS was then used to study the electronic structures of the metal binding sites, and showed that metal-sulfur bond covalencies can actually affect the metal sites' coordination number and ligand types, thus affect the conformation of the protein folding, which explains the ion specific behavior of NikR.



Funding Acknowledgement