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Correlating the active site structure of copper metalloproteins with their spectroscopic and chemical properties


EMSL Project ID
25685

Abstract

We propose to implement 63Cu and 65Cu, in combination with quantum chemical calculations, to study the metal sites of blue copper proteins, oxidase enzymes, and copper chaperones. Living systems 'tune' the reduction potentials of these proteins over a range of over 1 V. Tuning redox sites is essentail both for biological function and for designing non-biological catalysts for specific functions. Using NMR as a probe of the active site structure, we will determine at an atomic level of detail how the structure is correlated with the redox potential.

Project Details

Project type
Large-Scale EMSL Research
Start Date
2007-08-01
End Date
2009-09-30
Status
Closed

Team

Principal Investigator

Gerard Harbison
Institution
University of Nebraska - Lincoln

Team Members

Andrew Lipton
Institution
Environmental Molecular Sciences Laboratory

Related Publications

Harbison GS. 2015. "Polarization of Core Orbitals and Computation of Nuclear Quadrupole Coupling Constants using Gaussian Basis Sets." , Pacific Northwest National Laboratory, Richland, WA. doi:10.1016/j.jmr.2015.05.002 [Unpublished]
Low Temperature 65Cu NMR Spectroscopy of the Cu+ Site in Azurin Andrew S. Lipton, Robert W. Heck, Wibe A. de Jong, Amy R. Gao, Xiongjian Wu, Adrienne Roehrich, Gerard S. Harbison, and Paul D. Ellis Received March 5, 2009; Publication Date (Web): September 11, 2009 | doi: 10.1021/ja901308v