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5JCA

NADP(H) bound NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) from Pyrococcus furiosus

Summary for 5JCA
Entry DOI10.2210/pdb5jca/pdb
DescriptorNADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) subunit alpha, NADH-dependent Ferredoxin:NADP Oxidoreductase (NfnI) subunit beta, IRON/SULFUR CLUSTER, ... (9 entities in total)
Functional Keywordsnfni, oxidoreductase, pyrococcus furiosus, nadp(h) bound nfni
Biological sourcePyrococcus furiosus
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Cellular locationCytoplasm : Q8U195 Q8U194
Total number of polymer chains2
Total formula weight87665.93
Authors
Zadvornyy, O.A.,Schut, G.J.,Nguyen, D.M.,Artz, J.H.,Tokmina-Lukaszewska, M.,Lipscomb, G.,Adams, M.W.,Peters, J.W. (deposition date: 2016-04-14, release date: 2017-04-12, Last modification date: 2024-05-22)
Primary citationLubner, 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: 28394885
DOI: 10.1038/nchembio.2348
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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