Article
EPR studies of recombinant horse L-chain apoferritin and its mutant (E 53,56,57,60 Q) with haemin.
Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine - 1 Feb 2007
de Val Natalia, Hagen Wilfred R, Crichton Robert R
Abstract excerpt
Structural similarities between ferritins and bacterioferritins have been extensively demonstrated. However, there is an essential difference between these two types of ferritins: whereas bacterioferritins bind haem, in-vivo, as Fe(II)-protoporphyrin IX (this haem is located in a hydrophobic pocket along the 2-fold symmetry axes and is liganded by two axial Met 52 residues), eukaryotic ferritins are non-haem iron...
Topics
- Animals
- Apoferritins
- Binding Sites
- Electron Spin Resonance Spectroscopy
- Hemin
- Horses
- Mutant Proteins
- Mutation
- Protein Binding
- Protein Structure, Secondary
- Recombinant Proteins