Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25646457, PubMed:25908396). Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:25646457, PubMed:25908396). It can also insert iron into protoporphyrin IX (PubMed:1459957, PubMed:8119288, PubMed:21052751, PubMed:25646457). Has weaker activity with 2,4 disulfonate, deuteroporphyrin and 2,4 hydroxyethyl (PubMed:25646457, PubMed:12761666). In vitro, can also use Zn(2+) or Cu(2+) (PubMed:8119288, PubMed:16140324, PubMed:21052751, PubMed:12761666). Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+) Stimulated by Mg(2+) (PubMed:12761666). Inhibited by Cd(2+) (PubMed:12761666). Inhibited by N-methylmesoporphyrin (N-MeMP) and 2,4-disulfonic acid deuteroporphyrin IX (dSDP) (PubMed:10704318, PubMed:16140324, PubMed:18423489). kcat is 0.11 min(-1) with coproporphyrin III as substrate (PubMed:25646457). kcat is 78 min(-1) with Fe(2+) as substrate (PubMed:25908396). Optimum pH is 7.2 with Zn(2+) and protoporphyrin IX as substrates. Porphyrin-containing compound metabolism; protoheme biosynthesis. Monomer (PubMed:8119288). Interacts with frataxin/Fra (PubMed:25826316). Deletion mutant requires hemin for growth. Belongs to the ferrochelatase family.