9F0F

Coproporphyrin III - LmCpfC WT complex soaked with Fe2+ and anomalous densities

9F0F の概要

• エントリーDOI: 10.2210/pdb9f0f/pdb
• 分子名称: Coproporphyrin III ferrochelatase, coproporphyrin III, 1,2-ETHANEDIOL, ... (6 entities in total)
• 機能のキーワード: metal insertion, porphyrins, coproporphyrin ferrochelatase, metal binding protein
• 由来する生物種: Listeria monocytogenes
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36428.95

構造登録者

Gabler, T.,Hofauer, S. (登録日: 2024-04-16, 公開日: 2024-04-24, 最終更新日: 2025-01-15)

主引用文献

Dali, A.,Gabler, T.,Sebastiani, F.,Furtmuller, P.G.,Becucci, M.,Hofbauer, S.,Smulevich, G.
Entrance channels to coproheme in coproporphyrin ferrochelatase probed by exogenous imidazole binding.
J.Inorg.Biochem., 260:112681-112681, 2024

PubMed Abstract: Iron insertion into porphyrins is an essential step in heme biosynthesis. In the coproporphyrin-dependent pathway, specific to monoderm bacteria, this reaction is catalyzed by the monomeric enzyme coproporphyrin ferrochelatase. In addition to the mechanistic details of the metalation of the porphyrin, the identification of the substrate access channel for ferrous iron to the active site is important to fully understand this enzymatic system. In fact, whether the iron reaches the active site from the distal or the proximal porphyrin side is still under debate. In this study we have thoroughly addressed this question in Listeria monocytogenes coproporphyrin ferrochelatase by X-ray crystallography, steady-state and pre-steady-state imidazole ligand binding studies, together with a detailed spectroscopic characterization using resonance Raman and UV-vis absorption spectroscopies in solution. Analysis of the X-ray structures of coproporphyrin ferrochelatase-coproporphyrin III crystals soaked with ferrous iron shows that iron is present on both sides of the porphyrin. The kinetic and spectroscopic study of imidazole binding to coproporphyrin ferrochelatase‑iron coproporphyrin III clearly indicates the presence of two possible binding sites in this monomeric enzyme that influence each other, which is confirmed by the observed cooperativity at steady-state and a biphasic behavior in the pre-steady-state experiments. The current results are discussed in the context of the entire heme biosynthetic pathway and pave the way for future studies focusing on protein-protein interactions.

PubMed: 39146673
DOI: 10.1016/j.jinorgbio.2024.112681

実験手法

X-RAY DIFFRACTION (2.1 Å)