Identification of the predominant non-native histidine ligand in unfolded cytochrome c.

@article{Coln1997IdentificationOT,
  title={Identification of the predominant non-native histidine ligand in unfolded cytochrome c.},
  author={Wilfredo Col{\'o}n and L P Wakem and Fred Sherman and Heinrich Roder},
  journal={Biochemistry},
  year={1997},
  volume={36 41},
  pages={12535-41}
}
The heme and its two axial ligands, His18 and Met80, play a central role in the folding/unfolding mechanism of cytochrome c. Because of the covalent heme attachment, His18 remains bound under typical denaturing conditions, while the more labile Met80 ligand is replaced by an alternate histidine ligand. To distinguish between the two possible non-native histidine ligands in horse cytochrome c, variants with a His26 to Gln or His33 to Asn substitution were prepared using a yeast expression system… CONTINUE READING
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