BRENDA - Enzyme Database

Mechanistic insights into energy conservation by flavin-based electron bifurcation

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.; Nat. Chem. Biol. 13, 655-659 (2017)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.6.1.4
-
Pyrococcus furiosus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.6.1.4
Pyrococcus furiosus
Q8U195 and Q8U194
Q8U195: subunit alpha, Q8U194: subunit beta
-
Purification (Commentary)
EC Number
Commentary
Organism
1.6.1.4
-
Pyrococcus furiosus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.6.1.4
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
reduction of both NAD+ and Fd by Nfn enzymes is coupled to the bifurcation of electrons from NADPH oxidation. The exergonic coupling of the NADP(H) and NAD(H) half reactions in Nfn is presumed to be mediated by NADPH oxidation at L-FAD followed by electron transfer to the proximal [2Fe-2S] cluster and subsequently the NAD(H) binding site at S-FAD. Biophysical analysis of the enzyme provides the first direct insight into the mechanism of flavin-based electron bifurcation and the requisite structural features
745843
Pyrococcus furiosus
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.6.1.4
heterodimer
1 * 31000 + 1 * 53000, SDS-PAGE
Pyrococcus furiosus
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.6.1.4
FAD
the 31000 Da subunit contains one FAD (S-FAD) and a [2Fe-2S] cluster with an unusual Asp ligand. The 53000 Da subunit contains one FAD (L-FAD), which is the site of electron bifurcation, and two [4Fe-4S] clusters. The L-FAD proximal [4Fe-4S] cluster coordination includes an unusual Glu ligand. S-FAD and L-FAD bind NADH and NADPH, respectively
Pyrococcus furiosus
1.6.1.4
[2Fe-2S]-center
the 31000 Da subunit contains one FAD (S-FAD) and a [2Fe-2S] cluster. The [2Fe-2S] cluster is unusual, with a relatively high (positive) reduction potential and coordination by one Asp and three Cys ligands
Pyrococcus furiosus
1.6.1.4
[4Fe-4S]-center
the 53000 Da subunit contains one FAD (L-FAD), which is the site of electron bifurcation, and two [4Fe-4S] clusters
Pyrococcus furiosus
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.6.1.4
-
Pyrococcus furiosus
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.6.1.4
FAD
the 31000 Da subunit contains one FAD (S-FAD) and a [2Fe-2S] cluster with an unusual Asp ligand. The 53000 Da subunit contains one FAD (L-FAD), which is the site of electron bifurcation, and two [4Fe-4S] clusters. The L-FAD proximal [4Fe-4S] cluster coordination includes an unusual Glu ligand. S-FAD and L-FAD bind NADH and NADPH, respectively
Pyrococcus furiosus
1.6.1.4
[2Fe-2S]-center
the 31000 Da subunit contains one FAD (S-FAD) and a [2Fe-2S] cluster. The [2Fe-2S] cluster is unusual, with a relatively high (positive) reduction potential and coordination by one Asp and three Cys ligands
Pyrococcus furiosus
1.6.1.4
[4Fe-4S]-center
the 53000 Da subunit contains one FAD (L-FAD), which is the site of electron bifurcation, and two [4Fe-4S] clusters
Pyrococcus furiosus
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.6.1.4
-
Pyrococcus furiosus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.6.1.4
NAD+ + 2 NADPH + 2 oxidized ferredoxin [iron-sulfur] cluster
reduction of both NAD+ and Fd by Nfn enzymes is coupled to the bifurcation of electrons from NADPH oxidation. The exergonic coupling of the NADP(H) and NAD(H) half reactions in Nfn is presumed to be mediated by NADPH oxidation at L-FAD followed by electron transfer to the proximal [2Fe-2S] cluster and subsequently the NAD(H) binding site at S-FAD. Biophysical analysis of the enzyme provides the first direct insight into the mechanism of flavin-based electron bifurcation and the requisite structural features
745843
Pyrococcus furiosus
NADH + H+ + 2 NADP+ + 2 reduced ferredoxin [iron-sulfur] cluster
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.6.1.4
heterodimer
1 * 31000 + 1 * 53000, SDS-PAGE
Pyrococcus furiosus