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Article

A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.

Journal of molecular biology - 2 Nov 2007

Medlock Amy E, Dailey Tamara A, Ross Teresa A, Dailey Harry A, Lanzilotta William N

Abstract excerpt

Ferrochelatase (protoheme ferrolyase, EC 4.99.1.1) is the terminal enzyme in heme biosynthesis and catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme IX (heme). Due to the many critical roles of heme, synthesis of heme is required by the vast majority of organisms. Despite significant investigation of both the microbial and eukaryotic enzyme, details of metal chelation remain...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 17884090
DOI: 10.1016/j.jmb.2007.08.040
PMCID: PMC2083577

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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