Document Type
Article
Publication Date
12-2007
Abstract
Density functional theory (DFT) and x-ray absorption fine structure (XAFS) spectroscopy are complementary tools for the biophysical study of active sites in metalloproteins. DFT is used to compute XAFS multiple scattering Debye Waller factors, which are then employed in genetic algorithm-based fitting process to obtain a global fit to the XAFS in the space of fitting parameters. Zn-Cys sites, which serve important functions as transcriptional switches in Zn finger proteins and matrix metalloproteinases, previously have proven intractable by this method; here these limitations are removed. In this work we evaluate optimal DFT nonlocal functionals and basis sets for determining optimal geometries and vibrational densities of states of mixed ligation Zn(His)4−n(Cys)n" role="presentation" style="display: inline; line-height: normal; word-spacing: normal; overflow-wrap: normal; white-space: nowrap; float: none; direction: ltr; max-width: none; max-height: none; min-width: 0px; min-height: 0px; border: 0px; padding: 0px 2px 0px 0px; margin: 0px; position: relative;">Zn(His)4−n(Cys)nZn(His)4−n(Cys)n sites. Theoretical results are compared to experimental XAFS measurements and Raman spectra from the literature and tabulated for use.
Recommended Citation
Dimakis, Nicholas, et al. “Zinc Cysteine Active Sites of Metalloproteins: A Density Functional Theory and x-Ray Absorption Fine Structure Study.” The Journal of Chemical Physics, vol. 128, no. 11, American Institute of Physics, Mar. 2008, p. 115104, doi:10.1063/1.2835601.
Publication Title
Journal of Chemical Physics
DOI
10.1063/1.2835601
Comments
© 2008 American Institute of Physics. Original published version available at https://doi.org/10.1063/1.2835601