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Literature summary for 1.3.1.109 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)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Acidaminococcus fermentans

KM Value [mM]

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

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(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
-
?
(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

Organism UniProt Comment Textmining
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
-
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

Oxidation Stability Organism
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)

Purification (Comment) Organism
-
Acidaminococcus fermentans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(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
-
?
(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
-
?
(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
-
?
(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

Subunits Comment Organism
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

Synonyms Comment Organism
bifurcating butyryl-CoA dehydrogenase
-
Acidaminococcus fermentans

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
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
NADH no activity with NADPH Acidaminococcus fermentans

General Information

General Information Comment Organism
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