Suppression of axial methionine fluxion in Hydrogenobacter thermophilus Gln64Asn cytochrome c552.

@article{Wen2005SuppressionOA,
  title={Suppression of axial methionine fluxion in Hydrogenobacter thermophilus Gln64Asn cytochrome c552.},
  author={Xin Wen and Kara L Bren},
  journal={Biochemistry},
  year={2005},
  volume={44 13},
  pages={5225-33}
}
Proteins in the cytochrome c (cyt c) family with His-Met heme axial ligation display diverse heme electronic structures as revealed by the NMR spectra of their oxidized (paramagnetic) forms. These variations in electronic structure are thought to result primarily from differences in heme axial Met orientation among cyt c species. The factors determining Met orientation in cyts c, however, remain poorly understood. An additional layer of complexity was revealed with the recent finding that the… CONTINUE READING