Article
Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite reductase.
Journal of the American Chemical Society - 24 Jan 2007
Wijma Hein J, MacPherson Iain, Farver Ole, Tocheva Elitza I, Pecht Israel, Verbeet Martin Ph, Murphy Michael E P, Canters Gerard W
Abstract excerpt
Copper-containing nitrite reductase harbors a type-1 and a type-2 Cu site. The former acts as the electron acceptor site of the enzyme, and the latter is the site of catalytic action. The effect of the methionine ligand on the reorganization energy of the type-1 site was explored by studying the electron-transfer kinetics between NiR (wild type (wt) and the variants Met150Gly and Met150Thr) with Fe(II)EDTA and...
Topics
- Binding Sites
- Catalytic Domain
- Chelating Agents
- Edetic Acid
- Electron Transport
- Glycine
- Iron
- Kinetics
- Ligands
- Methionine
- Mutation
- Nitrite Reductases
- Protein Conformation
