MetaCyc Enzyme: ferrochelatase

Gene: hemH Accession Number: G-9035 (MetaCyc)

Species: Rhodobacter sphaeroides

The molecular weight was determined by SDS-PAGE. Gel filtration chromatography of solubilized ferrochelatase in the presence of 0.5% sodium deoxycholate gave a molecular weight of 110 kD. Contrary to a previous report, the calculated millimolar extinction coefficient at 278 nm was 76, based upon a molecular weight of 115 kD [Dailey86a].

Locations: membrane

Map Position: [2,967,945 -> 2,969,078]

Molecular Weight of Polypeptide: 115 kD (experimental) [Dailey86a ]

Unification Links: Entrez-gene:3718861

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Cellular Component: GO:0016020 - membrane [Dailey86a]

Enzymatic reaction of: ferrochelatase

EC Number:

protoporphyrin IX[periplasmic space] + Fe2+[periplasmic space] <=> ferroheme b[periplasmic space] + 2 H+[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

This reaction is reversible.

In Pathways: superpathway of heme biosynthesis from glycine , heme biosynthesis I (aerobic)

Ferrochelatase catalyzes the insertion of ferrous iron into protoporphyrin IX to form protoheme (heme) [Dailey86a].

Inhibitors (Unknown Mechanism): Hg2+ [Dailey86a] , N-ethylmaleimide [Dailey86a] , iodoacetamide [Dailey86a] , copper sulfate [Dailey86a] , diacetyl [Dailey86a] , heme b [Dailey86a]

Kinetic Parameters:

Km (μM)
protoporphyrin IX


Dailey86a: Dailey HA (1986). "Purification and characterization of bacterial ferrochelatase." Methods Enzymol 123;408-15. PMID: 3702737

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Thu Oct 8, 2015, biocyc13.