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Iron Sulfur Covalency in Rubredoxins and model systems using Xrays and EPR Spectroscopies.
X-ray absorptions spectroscopy methods are being used to determine the covalency of the iron-sulfur complexes on Rubredoxins. Rubredoxins are metalloproteins that contain Iron-Sulfur protein active sites which are involved in covalency and electron transfer. The Iron Sulfur active site contains an iron metal surrounded by four thiolates bonds (SHR functional group) from the cysteine protein that have high covalency that contribute to the redox reactions of this protein molecule. the way spectroscopy is used to determine the covalency and electron transfer is by performing calculations on the ligand field of the protein which determines the transitions of the Iron sulfur protein charge transfer and determines the whether the energy is high or low indicating either high or low covalency. The method used for this metalloprotein is called the ligand k-edge x-ray spectroscopy, which provides us with information that helps determine the interactions of the Iron Sulfur protein. The covalency of the Iron sulfur bonds go through an exchange of coupling altering their magnetic properties and transferring the electrons between the HOMO and LUMO orbitals causing conductivity.

The K-edge data determined using the XAS, indicates that the Iron four monomer leads to determining the covalency of the thiolate sites in the protein.

Covalency of electrons between the Iron sulfur protein is crucial because it describes the electronic structure, the bonding, the interactions of the elctrons in the d block, physcial activity, chemical activity and conductivity of the molecules.

Comparison of Covalency and redox potentials with ordinary Td(Fe(RS)4)
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the unusually high covalency which lowers the inner sphere reorganization energy allowing rapid e- transfer
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Mechanism Forelectron Transport in Mitochondria and Chloroplasts
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