A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin.

@article{Robinson2003APA,
  title={A pH-dependent aquomet-to-hemichrome transition in crystalline horse methemoglobin.},
  author={Victoria L Robinson and Benjamin B Smith and Arthur Arnone},
  journal={Biochemistry},
  year={2003},
  volume={42 34},
  pages={10113-25}
}
In 1947, Perutz and co-workers reported that crystalline horse methemoglobin undergoes a large lattice transition as the pH is decreased from 7.1 to 5.4. We have determined the pH 7.1 and 5.4 crystal structures of horse methemoglobin at 1.6 and 2.1 A resolution, respectively, and find that this lattice transition involves a 23 A translation of adjacent hemoglobin tetramers as well as changes in alpha heme ligation and the tertiary structure of the alpha subunits. Specifically, when the pH is… CONTINUE READING