Magnesium-chelatase is a three-component enzyme (EC6.6.1.1) that catalyses the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of chlorophyll and bacteriochlorophyll.[1][2] As a result, it is thought that Mg-chelatase has an important role in channeling intermediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth:
protoporphyrin IX + Mg2+ + ATP + H 2O ADP + phosphate + Mg-protoporphyrin IX + 2 H+
This enzyme belongs to the family of ligases, specifically those forming nitrogen-D-metal bonds in coordination complexes. The systematic name of this enzyme class is Mg-protoporphyrin IX magnesium-lyase. Other names in common use include protoporphyrin IX magnesium-chelatase, protoporphyrin IX Mg-chelatase, magnesium-protoporphyrin IX chelatase, magnesium-protoporphyrin chelatase, magnesium-chelatase, Mg-chelatase, and Mg-protoporphyrin IX magnesio-lyase. This enzyme is part of the biosynthetic pathway to chlorophylls.
^Willows, Robert D. (2003). "Biosynthesis of chlorophylls from protoporphyrin IX". Natural Product Reports. 20 (6): 327–341. doi:10.1039/B110549N. PMID12828371.
Al-Karadaghi S; Hansson, A; Hansson, M; Olsen, JG; Gough, S; Willows, RD; Al-Karadaghi, S (2001). "Interplay between an AAA module and an integrin I domain may regulate the function of magnesium chelatase". J. Mol. Biol. 311 (1): 111–22. doi:10.1006/jmbi.2001.4834. PMID11469861.
