6QKX
2-Naphthoyl-CoA Reductase-DiHydroNaphthoyl-CoA complex(NCR-DHNCoA co-crystallized complex)
Summary for 6QKX
| Entry DOI | 10.2210/pdb6qkx/pdb |
| Descriptor | NCR, IRON/SULFUR CLUSTER, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total) |
| Functional Keywords | reductase, 2-naphthoyl-coa, 2-naphthoyl-coa reductase, naphthalene, fad, fmn, [4fe-4s], hydride transfer, co-crystallized, flavoprotein |
| Biological source | bacterium enrichment culture clone N47 |
| Total number of polymer chains | 1 |
| Total formula weight | 80435.69 |
| Authors | Kayastha, K.,Ermler, U. (deposition date: 2019-01-30, release date: 2019-05-15, Last modification date: 2024-10-16) |
| Primary citation | 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 Cited by 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: 31061390DOI: 10.1038/s41467-019-10078-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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