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

1 February 2001

journal article
Published by Springer Nature in Nature Structural & Molecular Biology

Vol. 8 (2) , 156-160
https://doi.org/10.1038/84152

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.

Keywords

ENZYME

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