Rubredoxins represent the simplest type of iron-sulfur proteins, in that they contain a single iron ion ligated by sulfur atoms from a surrounding cage of four cysteine residues. Whereas the rubredoxin from Pseudomonas oleovorans has been shown to be involved in the hydroxylation of alkanes, the biological function of the rubredoxin from Clostridium pasteurianum, which is the focus of this study, remains to be discovered. Because of their coordination environment, rubredoxins exhibit large NMR chemical shifts for NMR-active nuclei near the iron-center due to hyperfine coupling to unpaired electrons in the complex. These large shifts give a unique insite into the electronic structure of the coordination environment. This information is used in conjunction with high-level hybrid density functional calculations to achieve our ultimate goal of understanding the electronic structure of the coordination environment of iron-sulfur proteins.
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