The Rieske protein is found in the bc1 complex (complex III) and plays an important role in transporting electrons and protons through the electron transport chain. The Rieske protein contains a [2Fe-2S] cluster ligated by a 2-cystines and 2- histidines. The reduction potential of this cluster is pH-dependent and varies across species.   An H134C mutant of the Thermus thermophilus Rieske substitutes one of the ligating histidines for a cysteine, changing the ligation structure of the cluster from a 2Cys-2His to a 3Cys-1His environment. To study the effects of this mutation, the protein is subjected to modification with diethyl pyrocarbonate (DEPC) and to pH changes. The behavior of this protein is compared to the wild type protein as observed through circular dichroism and UV visible spectroscopy. Because of the similarity in the iron-sulfur cluster ligands, H134C will also be compared to another mitochondrial protein, mitoNEET, which contains a 3Cys-1His environment.

Spectroscopic and chemical modification of the H134C mutant of the <i>Thermus thermophius</i> Rieske protein

245th National Meeting (2013)

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Spectroscopic and chemical modification of the H134C mutant of the Thermus thermophius Rieske protein