Article
Protein dynamics in the region of the sixth ligand methionine revealed by studies of imidazole binding to Rhodobacter capsulatus cytochrome c2 hinge mutants.
Biochemistry - 22 Jun 2004
Dumortier C, Fitch J, Van Petegem F, Vermeulen W, Meyer T E, Van Beeumen J J, Cusanovich M A
Abstract excerpt
All class I c-type cytochromes studied to date undergo a dynamic process in the oxidized state, which results in the transient breaking of the iron-methionine-sulfur bond and sufficient movement to allow the binding of exogenous ligands (imidazole in this work). In the case of Rhodobacter capsulatus cytochrome c(2), the sixth heme ligand Met96 and up to 14 flanking residues (positions 88-100, termed the hinge...
Topics
- Cytochromes c2
- Imidazoles
- Kinetics
- Ligands
- Methionine
- Mutation
- Rhodobacter capsulatus
