5JFC
NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus
Summary for 5JFC
| Entry DOI | 10.2210/pdb5jfc/pdb |
| Related | 5JCA |
| Descriptor | NADH-dependent Ferredoxin:NADP Oxidoreductase subunit alpha, NADH-dependent Ferredoxin:NADP Oxidoreductase subunit beta, IRON/SULFUR CLUSTER, ... (7 entities in total) |
| Functional Keywords | nfni, oxidoreductase, pyrococcus furiosus, nadp(h) bound nfni |
| Biological source | Pyrococcus furiosus More |
| Total number of polymer chains | 2 |
| Total formula weight | 86828.41 |
| Authors | Zadvornyy, O.A.,Schut, G.J.,Nguyen, D.M.,Artz, J.H.,Tokmina-Lukaszewska, M.,Lipscomb, G.,King, P.W.,Adams, M.W.,Peters, J.W. (deposition date: 2016-04-19, release date: 2017-04-12, Last modification date: 2024-03-06) |
| Primary citation | Lubner, C.E.,Jennings, D.P.,Mulder, D.W.,Schut, G.J.,Zadvornyy, O.A.,Hoben, J.P.,Tokmina-Lukaszewska, M.,Berry, L.,Nguyen, D.M.,Lipscomb, G.L.,Bothner, B.,Jones, A.K.,Miller, A.F.,King, P.W.,Adams, M.W.W.,Peters, J.W. Mechanistic insights into energy conservation by flavin-based electron bifurcation. Nat. Chem. Biol., 13:655-659, 2017 Cited by PubMed Abstract: The recently realized biochemical phenomenon of energy conservation through electron bifurcation provides biology with an elegant means to maximize utilization of metabolic energy. The mechanism of coordinated coupling of exergonic and endergonic oxidation-reduction reactions by a single enzyme complex has been elucidated through optical and paramagnetic spectroscopic studies revealing unprecedented features. Pairs of electrons are bifurcated over more than 1 volt of electrochemical potential by generating a low-potential, highly energetic, unstable flavin semiquinone and directing electron flow to an iron-sulfur cluster with a highly negative potential to overcome the barrier of the endergonic half reaction. The unprecedented range of thermodynamic driving force that is generated by flavin-based electron bifurcation accounts for unique chemical reactions that are catalyzed by these enzymes. PubMed: 28394885DOI: 10.1038/nchembio.2348 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.598 Å) |
Structure validation
Download full validation report
