| Literature DB >> 11175906 |
C K Wu1, H A Dailey, J P Rose, A Burden, V M Sellers, B C Wang.
Abstract
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 A 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. The positioning of highly conserved residues in the active site in conjunction with previous biochemical studies support a catalytic model that may have significance in explaining the enzymatic defects that lead to the human inherited disease erythropoietic protoporphyria.Entities:
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Year: 2001 PMID： 11175906 DOI： 10.1038/84152
Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368