Ferrochelatase (also known as PPIX ferrochelatase; Enzyme Commission number 4.9.9.1.1) catalyzes the insertion of ferrous iron into PPIX to form heme. This reaction unites the biochemically synchronized pathways of porphyrin synthesis and iron transport in nearly all living organisms. The ferrochelatases are an evolutionarily diverse family of enzymes with no more than six active site residues known to be perfectly conserved. The availability of over thirty different crystal structures, including many with bound metal ions or porphyrins, has added tremendously to our understanding of ferrochelatase structure and function. It is generally believed that ferrous iron is directly channeled to ferrochelatase in vivo, but the identity of the suspected chaperone remains uncertain despite much recent progress in this area. Identification of a conserved metal ion binding site at the base of the active site cleft may be an important clue as to how ferrochelatases acquire iron, and catalyze desolvation during transport to the catalytic site to complete heme synthesis.

中文翻译：

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铁螯合酶：卟啉生物合成和铁转运途径的融合

铁螯合酶（也称为 PPIX 铁螯合酶；酶委员会编号 4.9.9.1.1）催化亚铁插入 PPIX 以形成血红素。该反应在几乎所有生物体中结合了卟啉合成和铁转运的生化同步途径。ferrochelatases 是一个进化多样化的酶家族，具有不超过六个已知完全保守的活性位点残基。三十多种不同晶体结构的可用性，包括许多具有结合金属离子或卟啉的晶体结构，极大地增加了我们对铁螯合酶结构和功能的理解。一般认为亚铁在体内直接被引导至亚铁螯合酶，但尽管最近在该领域取得了很大进展，但疑似伴侣的身份仍然不确定。