Protein dynamics in the region of the sixth ligand methionine revealed by studies of imidazole binding to Rhodobacter capsulatus cytochrome c2 hinge mutants.

@article{Dumortier2004ProteinDI,
  title={Protein dynamics in the region of the sixth ligand methionine revealed by studies of imidazole binding to Rhodobacter capsulatus cytochrome c2 hinge mutants.},
  author={Chantal Dumortier and John Fitch and Filip Van Petegem and Wim Vermeulen and Terry E. Meyer and Jozef J. Van Beeumen and Michael A. Cusanovich},
  journal={Biochemistry},
  year={2004},
  volume={43 24},
  pages={7717-24}
}
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 region), located between two relatively rigid helical regions, may be involved in… CONTINUE READING

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