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Literature summary extracted from

  • Chowdhury, N.P.; Mowafy, A.M.; Demmer, J.K.; Upadhyay, V.; Koelzer, S.; Jayamani, E.; Kahnt, J.; Hornung, M.; Demmer, U.; Ermler, U.; Buckel, W.
    Studies on the mechanism of electron bifurcation catalyzed by electron transferring flavoprotein (Etf) and butyryl-CoA dehydrogenase (Bcd) of Acidaminococcus fermentans (2013), J. Biol. Chem., 289, 5145-5157.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.109 expression of the electron transfer flavoprotein in Escherichia coli Acidaminococcus fermentans

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.1.109
-
 Acidaminococcus fermentans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.109 0.012
-
 NADH pH 7, temperature not specified in the publication Acidaminococcus fermentans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.109 42000
-
 because electron transferring flavoprotein (EtfAf) and butanoyl-CoA dehydrogenase (BcdAf) are separated proteins in solution, a transient Bcd-Etf complex is sufficient to perform a bifurcation process. Electron transferring flavoprotein (EtfAf) is a heterodimer with a molecular mass of around 66 kDa (theoretically 37600 + 28400 Da). Butanoyl-CoA dehydrogenase (BcdAf) is homotetrameric flavoprotein (4 * 42000 Da) Acidaminococcus fermentans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.109 (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster Acidaminococcus fermentans the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
-
 ?
1.3.1.109 (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster Acidaminococcus fermentans DSM 20731 the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.109 Acidaminococcus fermentans D2RIQ2 and D2RIQ3 and D2RL84 D2RIQ2: electron transfer flavoprotein beta-subunit, D2RIQ3: electron transfer flavoprotein alpha-subunit, D2RL84: acyl-CoA dehydrogenase domain protein
-
1.3.1.109 Acidaminococcus fermentans DSM 20731 D2RIQ2 and D2RIQ3 and D2RL84 D2RIQ2: electron transfer flavoprotein beta-subunit, D2RIQ3: electron transfer flavoprotein alpha-subunit, D2RL84: acyl-CoA dehydrogenase domain protein
-

Oxidation Stability

EC Number Oxidation Stability Organism
1.3.1.109 although EtfAf and BcdAf are stable under air, all the experiments are performed in an anaerobic chamber under an atmosphere of 95% N2 and 5% H2, since ferredoxin and the reduced forms of flavin are oxygen-sensitive Acidaminococcus fermentans

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.109
-
 Acidaminococcus fermentans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.109 (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster i.e. crotonyl-CoA. NADH reduces beta-FAD of electron transferring flavoprotein, which bifurcates one electron to butanoyl-CoA dehydrogenase via FAD and the other to ferredoxin. Electron transferring flavoprotein (EtfAf) contains one FAD (alpha-FAD) in subunit alpha and a second FAD (beta-FAD) in subunit beta. The distance between the two isoalloxazine rings is 18 A°. The EtfAf-NAD+ complex structure reveals beta-FAD as acceptor of the hydride of NADH. The formed beta-FADH- is considered as the bifurcating electron donor. As a result of a domain movement, alpha-FAD is able to approach beta-FADH- by about 4 A and to take up one electron yielding a stable anionic semiquinone, alpha-FAD-/*, which donates this electron further to the FAD of butanoyl-CoA dehydrogenase BcdAf after a second domain movement. The remaining nonstabilized neutral semiquinone, beta-FADH*, immediately reduces ferredoxin. This electron flow from beta-FADH* to ferredoxin is only accomplished if the thermodynamically more favorable electron transfer to alpha-FAD-*. is prevented. Therefore, after the first electron transfer to alpha-FAD, a rotation is postulated of domain II toward the FAD binding site of butanoyl-CoA dehydrogenase BcdAf (based on spectroscopic and structural data). This conformational change, concomitantly, also reduces the distance between alpha-FAD-* and FAD from butanoyl-CoA dehydrogenase from about 30 to about 10 A. Thus, alpha-FAD embedded into the weakly associated domain II serves as a shuttle between the electron-donating beta-FADH- and the electron-accepting FAD of butanoyl-CoA dehydrogenase. Repetition leads to reduction of crotonyl-CoA Acidaminococcus fermentans butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 ?
1.3.1.109 (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster i.e. crotonyl-CoA. NADH reduces beta-FAD of electron transferring flavoprotein, which bifurcates one electron to butanoyl-CoA dehydrogenase via FAD and the other to ferredoxin. Electron transferring flavoprotein (EtfAf) contains one FAD (alpha-FAD) in subunit alpha and a second FAD (beta-FAD) in subunit beta. The distance between the two isoalloxazine rings is 18 A°. The EtfAf-NAD+ complex structure reveals beta-FAD as acceptor of the hydride of NADH. The formed beta-FADH- is considered as the bifurcating electron donor. As a result of a domain movement, alpha-FAD is able to approach beta-FADH- by about 4 A and to take up one electron yielding a stable anionic semiquinone, alpha-FAD-/*, which donates this electron further to the FAD of butanoyl-CoA dehydrogenase BcdAf after a second domain movement. The remaining nonstabilized neutral semiquinone, beta-FADH*, immediately reduces ferredoxin. This electron flow from beta-FADH* to ferredoxin is only accomplished if the thermodynamically more favorable electron transfer to alpha-FAD-*. is prevented. Therefore, after the first electron transfer to alpha-FAD, a rotation is postulated of domain II toward the FAD binding site of butanoyl-CoA dehydrogenase BcdAf (based on spectroscopic and structural data). This conformational change, concomitantly, also reduces the distance between alpha-FAD-* and FAD from butanoyl-CoA dehydrogenase from about 30 to about 10 A. Thus, alpha-FAD embedded into the weakly associated domain II serves as a shuttle between the electron-donating beta-FADH- and the electron-accepting FAD of butanoyl-CoA dehydrogenase. Repetition leads to reduction of crotonyl-CoA Acidaminococcus fermentans DSM 20731 butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
 ?
1.3.1.109 (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation Acidaminococcus fermentans butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
-
 ?
1.3.1.109 (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation Acidaminococcus fermentans DSM 20731 butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.1.109 More because electron transferring flavoprotein (EtfAf) and butanoyl-CoA dehydrogenase (BcdAf) are separated proteins in solution, a transient Bcd-Etf complex is sufficient to perform a bifurcation process. Electron transferring flavoprotein (EtfAf) is a heterodimer with a molecular mass of around 66 kDa (theoretically 37600 + 28400 Da). Butanoyl-CoA dehydrogenase (BcdAf) is homotetrameric flavoprotein (4 * 42000 Da) Acidaminococcus fermentans

Synonyms

EC Number Synonyms Comment Organism
1.3.1.109 bifurcating butyryl-CoA dehydrogenase
-
 Acidaminococcus fermentans

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.109 7
-
 assay at Acidaminococcus fermentans

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.109 FAD the electron transferring flavoprotein (EtfAf) contains one FAD (alpha-FAD) in subunit alpha and a second FAD (beta-FAD) in subunit beta. butanoyl-CoA dehydrogenase also contains FAD. beta-FAD of the the electron transferring flavoprotein is the acceptor of the hydride of NADH. The formed beta-FADH- is considered as the bifurcating electron donor. As a result of a domain movement, alpha-FAD is able to approach beta-FADH- by about 4 A and to takeup one electron yielding a stable anionic semiquinone, alpha-FAD-/* , which donates this electron further to the FAD of butanoyl-CoA dehydrogenase BcdAf after a second domain movement. The remaining nonstabilized neutral semiquinone, beta-FADH*, immediately reduces ferredoxin. This electron flow from beta-FADH* to ferredoxin is only accomplished if the thermodynamically more favorable electron transfer to alpha-FAD-*. is prevented. Therefore, after the first electron transfer to alpha-FAD, a rotation is postulated of domain II toward the FAD binding site of butanoyl-CoA dehydrogenase BcdAf (based on spectroscopic and structural data). This conformational change, concomitantly, also reduces the distance between alpha-FAD-* and FAD from butanoyl-CoA dehydrogenase from about 30 to about 10 A. Thus, alpha-FAD embedded into the weakly associated domain II serves as a shuttle between the electron-donating beta-FADH- and the electron-accepting FAD of butanoyl-CoA dehydrogenase. Repetition leads to reduction of crotonyl-CoA Acidaminococcus fermentans
1.3.1.109 NADH no activity with NADPH Acidaminococcus fermentans

General Information

EC Number General Information Comment Organism
1.3.1.109 metabolism the energy-rich reduced ferredoxin contributes to the energy conservation of the organism either by regeneration of NADH via the H+/Na+-pumping ferredoxin-NAD+ reductase also (Rnf) or by reduction of protons to H2, which increases the substrate-level phosphorylation via the oxidative branch of the fermentation Acidaminococcus fermentans