Investigation of electronic structure of Fe-S clusters (emslcsd6)
EMSL Project ID
2231
Abstract
We propose to use EMSL software and hardware (Molecular Science Computation Facility) to perform theoretical calculations of the electronic structures of Fe-S clusters.Fe-S proteins are ubiquitous in living organisms. They belong to one of the most important classes of biological electron transfer agents. Their functionality is critically dependent on the electronic structure of their active sites, i.e. one-Fe center, Fe2S2, Fe3S4, and Fe4S4 clusters.A new experimental technique that combines electrospray ionization mass spectrometry and photoelectron spectroscopy has been developed in Prof. Lai-Sheng Wangs group at EMSL. Some preliminary photoelectron spectra of Fe-S clusters have been obtained using this apparatus. The proposed calculations are required to interpret the new experimental data and advance our understanding of the nature of Fe-S bonding and the electronic properties of the Fe-S centers. Particularly, the new experimental results will be used to benchmark theoretical methods used to study the Fe-S clusters and other transition metal complexes.
Project Details
Project type
Capability Research
Start Date
2001-04-01
End Date
2003-02-24
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members
Related Publications
Niu S, and T Ichiye. 2009. "Insight into Environmental Effects on Bonding and Redox Properties of [4Fe-4S] Clusters in Proteins." Journal of the American Chemical Society 131(16):5724-5725. doi:10.1021/ja900406j
Niu S, and T Ichiye. 2009. "Probing Ligand Effects on the Redox Energies of [4Fe-4S] Clusters Using Broken-Symmetry Density Functional Theory." Journal of Physical Chemistry A 113(19):5671–5676. doi:10.1021/jp809446q
Shuqiang Niu, Jeffrey A. Nichols and Toshiko Ichiye, Optimization of Spin-Unrestricted Density Functional Theory for Redox Properties of Rubredoxin Redox Site Analogues, J. Chem. Theory Comput., 2009, 5 (5), pp 1361-1368