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4.99.1.9	678312	Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX	Biochemistry	46	87-94	2007	Bacillus subtilis 168	https://pubmed.ncbi.nlm.nih.gov/17198378/	
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4.99.1.9	738499	Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes	J. Bacteriol.	174	8081-8093	1992	Bacillus subtilis 168	https://pubmed.ncbi.nlm.nih.gov/1459957/	
4.99.1.9	739725	Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis	Structure	5	1501-1510	1997	Bacillus subtilis	https://pubmed.ncbi.nlm.nih.gov/9384565/	
4.99.1.9	739725	Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis	Structure	5	1501-1510	1997	Bacillus subtilis 168	https://pubmed.ncbi.nlm.nih.gov/9384565/	
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4.99.1.9	739547	Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin	Proc. Natl. Acad. Sci. USA	112	2210-2215	2015	Cutibacterium acnes	https://pubmed.ncbi.nlm.nih.gov/25646457/	
4.99.1.9	739547	Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin	Proc. Natl. Acad. Sci. USA	112	2210-2215	2015	Mycobacterium tuberculosis	https://pubmed.ncbi.nlm.nih.gov/25646457/	
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4.99.1.9	771075	Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen-bonding interactions of the four propionate groups	FEBS J.	289	1680-1699	2022	Listeria monocytogenes	https://pubmed.ncbi.nlm.nih.gov/34719106/	
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