4.99.1.9	Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin III	 propionate interactions and porphyrin core deformation	Listeria monocytogenes	
4.99.1.9	Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX	Bacillus subtilis	
4.99.1.9	Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX	Bacillus subtilis 168	
4.99.1.9	Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes	Bacillus subtilis	
4.99.1.9	Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes	Bacillus subtilis 168	
4.99.1.9	Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis	Bacillus subtilis	
4.99.1.9	Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis	Bacillus subtilis 168	
4.99.1.9	Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase	Listeria monocytogenes	
4.99.1.9	Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin	Bacillus subtilis	
4.99.1.9	Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin	Cutibacterium acnes