Ontology highlight
ABSTRACT:
SUBMITTER: Medlock A
PROVIDER: S-EPMC1794275 | biostudies-literature | 2007 Feb
REPOSITORIES: biostudies-literature
Medlock Amy A Swartz Larkin L Dailey Tamara A TA Dailey Harry A HA Lanzilotta William N WN
Proceedings of the National Academy of Sciences of the United States of America 20070129 6
Ferrochelatase, the terminal enzyme in heme biosynthesis, catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX. Human ferrochelatase is a homodimeric, inner mitochondrial membrane-associated enzyme that possesses an essential [2Fe-2S] cluster. In this work, we report the crystal structure of human ferrochelatase with the substrate protoporphyrin IX bound as well as a higher resolution structure of the R115L variant without bound substrate. The data presented reveal ...[more]