13C NMR spectroscopy of core heme carbons as a simple tool to elucidate the coordination state of ferric high-spin heme proteins.

@article{Alontaga200613CNS,
  title={13C NMR spectroscopy of core heme carbons as a simple tool to elucidate the coordination state of ferric high-spin heme proteins.},
  author={Aileen Yung Alontaga and Richard A. Bunce and Angela Wilks and Mario Rivera},
  journal={Inorganic chemistry},
  year={2006},
  volume={45 22},
  pages={
          8876-81
        }
}
Evidence is presented demonstrating that the magnitudes of the 13C chemical shifts originating from heme meso carbons provide a straightforward diagnostic tool to elucidate the coordination state of high-spin heme proteins and enzymes. Pentacoordinate high-spin heme centers exhibit 13C meso shifts centered at approximately 250 ppm, whereas their hexacoordinate counterparts exhibit 13C shifts centered at approximately -80 ppm. The relatively small spectral window (400 to -100 ppm) covering the… CONTINUE READING
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