The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis

@article{Wu2001The2,
  title={The 2.0 {\AA} structure of human ferrochelatase, the terminal enzyme of heme biosynthesis},
  author={Chia-Kuei Wu and Harry A. Dailey and John P. Rose and Amy E. Burden and Vera M. Sellers and Bi-Cheng Wang},
  journal={Nature Structural Biology},
  year={2001},
  volume={8},
  pages={156-160}
}
Human ferrochelatase (E.C. 4.99.1.1) is a homodimeric (86 kDa) mitochondrial membrane-associated enzyme that catalyzes the insertion of ferrous iron into protoporphyrin to form heme. We have determined the 2.0 Å structure from the single wavelength iron anomalous scattering signal. The enzyme contains two NO-sensitive and uniquely coordinated [2Fe-2S] clusters. Its membrane association is mediated in part by a 12-residue hydrophobic lip that also forms the entrance to the active site pocket… Expand
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Ferrochelatase seems to have a structurally conserved core region that is common to the enzyme from bacteria, plants and mammals, and it is proposed that porphyrin binds in the identified cleft; this cleft also includes the metal-binding site of the enzyme. Expand
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TLDR
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TLDR
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TLDR
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