1.3.1.109: butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin)
This is an abbreviated version!
For detailed information about butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin), go to the full flat file.
Word Map on EC 1.3.1.109
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1.3.1.109
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butyrate
-
maritima
-
clostridial
-
thermotoga
-
crotonyl-coa
-
butanol
-
dehydrogenases
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methanogenic
-
synthesis
- 1.3.1.109
- butyrate
- maritima
-
clostridial
-
thermotoga
- crotonyl-coa
- butanol
- dehydrogenases
-
methanogenic
- synthesis
Reaction
Synonyms
BCD, Bcd/electron-transfer flavoprotein complex, Bcd/EtfAB, BcdA-EtfBC, Bct/Etf complex, bifurcating butanoyl-CoA dehydrogenase, bifurcating butyryl coenzyme A dehydrogenase/electron-transferring flavoprotein complex, bifurcating butyryl-CoA dehydrogenase, butanoyl-CoA dehydrogenase (NAD+, ferredoxin), butanoyl-CoA dehydrogenase/Etf complex, butyryl coenzyme A dehydrogenase, butyryl-CoA dehydrogenase, butyryl-CoA dehydrogenase-EtfAB complex, butyryl-CoA dehydrogenase/electron transferring flavoprotein complex, butyryl-CoA dehydrogenase/Etf complex, butyryl-coenzyme A dehydrogenase-EtfAB complex, electron transferring flavoprotein/butyryl-CoA dehydrogenase, Etf-Bcd complex, Etf-butyryl-CoA dehydrogenase complex, EtfAB/Bcd
ECTree
1.3.1.109 butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.3.1.109 - butanoyl-CoA dehydrogenase complex (NAD+, ferredoxin)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + 2 NADH + oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
D2RIQ2; D2RIQ3; D2RL84
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
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
D2RIQ2; D2RIQ3; D2RL84
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
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
-
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
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-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
-
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
-
the enzyme couples the endergonic reduction of ferredoxin with NADH to the exergonic reduction of crotonyl-CoA to butanoyl-CoA
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
D2RIQ2; D2RIQ3; D2RL84
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
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + reduced ferredoxin iron-sulfur cluster
D2RIQ2; D2RIQ3; D2RL84
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
-
-
?
(E)-but-2-enoyl-CoA + 2 NADH + oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
the bifurcating butyryl-CoA dehydrogenase catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH
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-
?
(E)-but-2-enoyl-CoA + 2 NADH + oxidized ferredoxin iron-sulfur cluster
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
the bifurcating butyryl-CoA dehydrogenase catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH
-
-
?
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
(E)-but-2-enoyl-CoA + NADH + oxidized ferredoxin [iron-sulfur] cluster
butanoyl-CoA + NAD+ + reduced ferredoxin [iron-sulfur] cluster
-
-
-
-
?
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
-
-
-
?
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin iron-sulfur cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin iron-sulfur cluster
Q18AQ1; Q18AQ6; Q18AQ5
-
-
-
?
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster
(E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
