1H-NMR assignments for the heme group and electronic structure in Chlorobium thiosulfatophilum cytochrome c-555

@inproceedings{Senn19841HNMRAF,
  title={1H-NMR assignments for the heme group and electronic structure in Chlorobium thiosulfatophilum cytochrome c-555},
  author={Hans Martin Senn and Michael A. Cusanovich and Kurt W{\"u}thrich},
  year={1984}
}
Abstract Cytochrome c -555 from Chlorobium thiosulfatophilum was investigated by 1 H nuclear magnetic resonance at 360 MHz. Individual 1 H-NMR assignments were obtained for heme c , and the side-chain proton resonances of the axial methionine and the imidazole ring proton lines of the axial histidine were identified. The unpaired electron spin distribution in the heme of the oxidized protein is characterized by outstandingly large hyperfine shifts for all four ring methyl groups, with a… CONTINUE READING

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