6QKG

2-Naphthoyl-CoA Reductase(NCR)

6QKG の概要

• エントリーDOI: 10.2210/pdb6qkg/pdb
• 分子名称: NCR A, IRON/SULFUR CLUSTER, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: reductase, 2-naphthoyl-coa, 2-naphthoyl-coa reductase, naphthalene, fad, fmn, 4fe-4s, hydride transfer, flavoprotein
• 由来する生物種: bacterium enrichment culture clone N47
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 159027.99

構造登録者

Kayastha, K.,Ermler, U. (登録日: 2019-01-29, 公開日: 2019-05-15, 最終更新日: 2024-10-16)

主引用文献

Willistein, M.,Bechtel, D.F.,Muller, C.S.,Demmer, U.,Heimann, L.,Kayastha, K.,Schunemann, V.,Pierik, A.J.,Ullmann, G.M.,Ermler, U.,Boll, M.
Low potential enzymatic hydride transfer via highly cooperative and inversely functionalized flavin cofactors.
Nat Commun, 10:2074-2074, 2019

PubMed Abstract: Hydride transfers play a crucial role in a multitude of biological redox reactions and are mediated by flavin, deazaflavin or nicotinamide adenine dinucleotide cofactors at standard redox potentials ranging from 0 to -340 mV. 2-Naphthoyl-CoA reductase, a key enzyme of oxygen-independent bacterial naphthalene degradation, uses a low-potential one-electron donor for the two-electron dearomatization of its substrate below the redox limit of known biological hydride transfer processes at E°' = -493 mV. Here we demonstrate by X-ray structural analyses, QM/MM computational studies, and multiple spectroscopy/activity based titrations that highly cooperative electron transfer (n = 3) from a low-potential one-electron (FAD) to a two-electron (FMN) transferring flavin cofactor is the key to overcome the resonance stabilized aromatic system by hydride transfer in a highly hydrophobic pocket. The results evidence how the protein environment inversely functionalizes two flavins to switch from low-potential one-electron to hydride transfer at the thermodynamic limit of flavin redox chemistry.

PubMed: 31061390
DOI: 10.1038/s41467-019-10078-3

実験手法

X-RAY DIFFRACTION (2.2 Å)