Heme binding to a conserved Cys-Pro-Val motif is crucial for the catalytic function of mitochondrial heme lyases.

@article{Steiner1996HemeBT,
  title={Heme binding to a conserved Cys-Pro-Val motif is crucial for the catalytic function of mitochondrial heme lyases.},
  author={H{\aa}kan Steiner and Gy Kisp{\'a}l and Alfred Zollner and Albert Haid and Walter Neupert and Roland Lill},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 51},
  pages={32605-11}
}
Covalent attachment of heme to the apoforms of mitochondrial cytochromes c and c1 requires the activity of cytochrome c heme lyase (CCHL) and cytochrome c1 heme lyase (CC1HL), respectively. The two enzymes differ in their cytochrome specificity, but they are related in sequence, and both contain conserved Cys-Pro-Val (CPV) motifs. By using various in vitro assays we investigated whether heme can bind directly to heme lyases and whether the CPV motif may be involved in heme binding. Heme… CONTINUE READING

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