Article
The effect of a C298D mutation in CaHydA [FeFe]-hydrogenase: Insights into the protein-metal cluster interaction by EPR and FTIR spectroscopic investigation.
Biochimica et biophysica acta - 1 Jan 2016
Morra Simone, Maurelli Sara, Chiesa Mario, Mulder David W, Ratzloff Michael W, Giamello Elio, King Paul W, Gilardi Gianfranco, Valetti Francesca
Abstract excerpt
A conserved cysteine located in the signature motif of the catalytic center (H-cluster) of [FeFe]-hydrogenases functions in proton transfer. This residue corresponds to C298 in Clostridium acetobutylicum CaHydA. Despite the chemical and structural difference, the mutant C298D retains fast catalytic activity, while replacement with any other amino acid causes significant activity loss. Given the proximity of C298...
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