Biophysical and structural analysis of a novel heme B iron ligation in the flavocytochrome cellobiose dehydrogenase.

@article{Rotsaert2003BiophysicalAS,
  title={Biophysical and structural analysis of a novel heme B iron ligation in the flavocytochrome cellobiose dehydrogenase.},
  author={Frederik A J Rotsaert and B Martin Hallberg and Simon de Vries and Pierre Moenne-Loccoz and Christina Divne and V. Renganathan and Michael H. Gold},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 35},
  pages={33224-31}
}
The fungal extracellular flavocytochrome cellobiose dehydrogenase (CDH) participates in lignocellulose degradation. The enzyme has a cytochrome domain connected to a flavin-binding domain by a peptide linker. The cytochrome domain contains a 6-coordinate low spin b-type heme with unusual iron ligands and coordination geometry. Wild type CDH is only the second example of a b-type heme with Met-His ligation, and it is the first example of a Met-His ligation of heme b where the ligands are… CONTINUE READING
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