5MAA

PCE reductive dehalogenase from S. multivorans in complex with 3-bromophenol

5MAA の概要

• エントリーDOI: 10.2210/pdb5maa/pdb
• 関連するPDBエントリー: 5M2G
• 分子名称: Tetrachloroethene reductive dehalogenase catalytic subunit PceA, IRON/SULFUR CLUSTER, 5-Methoxybenzimidazolyl-norcobamide, ... (7 entities in total)
• 機能のキーワード: organohalide respiration anaerobic crystallisation cobalamin, oxidoreductase
• 由来する生物種: Sulfurospirillum multivorans DSM 12446
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 109552.49

構造登録者

Kunze, C.,Bommer, M.,Hagen, W.R.,Uksa, M.,Dobbek, H.,Schubert, T.,Diekert, G. (登録日: 2016-11-03, 公開日: 2017-07-12, 最終更新日: 2024-01-17)

主引用文献

Kunze, C.,Bommer, M.,Hagen, W.R.,Uksa, M.,Dobbek, H.,Schubert, T.,Diekert, G.
Cobamide-mediated enzymatic reductive dehalogenation via long-range electron transfer.
Nat Commun, 8:15858-15858, 2017

PubMed Abstract: The capacity of metal-containing porphyrinoids to mediate reductive dehalogenation is implemented in cobamide-containing reductive dehalogenases (RDases), which serve as terminal reductases in organohalide-respiring microbes. RDases allow for the exploitation of halogenated compounds as electron acceptors. Their reaction mechanism is under debate. Here we report on substrate-enzyme interactions in a tetrachloroethene RDase (PceA) that also converts aryl halides. The shape of PceA's highly apolar active site directs binding of bromophenols at some distance from the cobalt and with the hydroxyl substituent towards the metal. A close cobalt-substrate interaction is not observed by electron paramagnetic resonance spectroscopy. Nonetheless, a halogen substituent para to the hydroxyl group is reductively eliminated and the path of the leaving halide is traced in the structure. Based on these findings, an enzymatic mechanism relying on a long-range electron transfer is concluded, which is without parallel in vitamin B-dependent biochemistry and represents an effective mode of RDase catalysis.

PubMed: 28671181
DOI: 10.1038/ncomms15858

実験手法

X-RAY DIFFRACTION (1.686 Å)