Rieske proteins are electron transport proteins involved in key biological processes, such as respiration and photosynthesis.  They have a [2Fe-2S] cluster ligated by 2 cysteines and 2 histidines.  A series of mutants, which alter the properties of the cluster in the Rieske protein from Thermus thermophilus, have been designed and produced (L135E, L135R, L135A, and Y158F).  Both wild type protein and the mutants have been reacted with diethyl pyrocarbonate (DEPC), which forms adducts with protein residues, including to the ligating histidines of the [2Fe-2S] cluster.  In the wild type protein, DEPC forms an adduct with His 154 and also results in reduction of the cluster.  L135R, L135A, and Y158F react with DEPC similarly to wild type. L135E, however, reacts very differently with a very slow reduction of the cluster.  The slow reduction is postulated to be the result of the negative charge added proximal to the cluster.

DEPC modification of mutant <i>Thermus thermophilus</i> Rieske proteins differ with a negative charge proximal to the cluster

245th National Meeting (2013)

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DEPC modification of mutant Thermus thermophilus Rieske proteins differ with a negative charge proximal to the cluster