Cytochrome c552 mutants: structure and dynamics at the active site probed by multidimensional NMR and vibration echo spectroscopy.

@article{Massari2006CytochromeCM,
  title={Cytochrome c552 mutants: structure and dynamics at the active site probed by multidimensional NMR and vibration echo spectroscopy.},
  author={Aaron M Massari and Brian L. McClain and Ilya J Finkelstein and Andrew P Lee and Heather L. Reynolds and Kara L Bren and Michael D Fayer},
  journal={The journal of physical chemistry. B},
  year={2006},
  volume={110 38},
  pages={
          18803-10
        }
}
Spectrally resolved infrared stimulated vibrational echo experiments are used to measure the vibrational dephasing of a CO ligand bound to the heme cofactor in two mutated forms of the cytochrome c552 from Hydrogenobacter thermophilus. The first mutant (Ht-M61A) is characterized by a single mutation of Met61 to an Ala (Ht-M61A), while the second variant is doubly modified to have Gln64 replaced by an Asn in addition to the M61A mutation (Ht-M61A/Q64N). Multidimensional NMR experiments… CONTINUE READING

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