Article
Site-directed mutagenesis reveals a conservation of the copper-binding site and the crucial role of His24 in CopH from Cupriavidus metallidurans CH34.
Journal of inorganic biochemistry - 1 Dec 2009
Sendra Véronique, Gambarelli Serge, Bersch Beate, Covès Jacques
Abstract excerpt
CopH is a periplasmic copper-binding protein from Cupriavidus metallidurans CH34 that contains two histidine residues. Both His24 and His26 contribute to the formation of two high-affinity copper-binding sites in wild-type CopH and are likely involved in a 2N2O coordination sphere in the equatorial plane. We have used site-directed mutagenesis, and a series of spectroscopic and calorimetric studies to further...
Topics
- Binding Sites
- Carrier Proteins
- Copper
- Cupriavidus
- Histidine
- Mutagenesis, Site-Directed
- Mutation
- Protein Binding
