What is it about?
Phosphenolpyruvate (PEP) binding to pyruvate kinase was studied in the presence of different mono- and divalent ions in the catalytic sites. The ions affected the structural change of the protein upon binding and the structure of bound PEP. In particular, a β-sheet was perturbed differently when Na+ was present, the conformational change was particularly large with Mn2+ due to a more closed conformation of the complex, and the carboxylate group of PEP interacted in a more defined way with the protein when Mn2+ was present than when other divalent ions were present.
Why is it important?
The work demonstrates the excellent sensitivity and reproducibility of data obtained with a little applied method to initiate protein reactions in infrared spectroscopy. See also our publication on this method: M. Krasteva, S. Kumar, A. Barth (2006), Spectroscopy 20, 89-94, A dialysis accessory for attenuated total reflection infrared spectroscopy.
The following have contributed to this page: Professor Andreas Barth