The enzyme, characterized from the bacterium Acetobacterium woodii, contains two [4Fe-4S] clusters and FAD. The enzyme couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant. It uses the mechanism of electron bifurcation to overcome the steep energy barrier in ferredoxin reduction. It also reduces 4-coumaroyl-CoA and feruloyl-CoA.
The enzyme, characterized from the bacterium Acetobacterium woodii, contains two [4Fe-4S] clusters and FAD. The enzyme couples the endergonic ferredoxin reduction with NADH as reductant to the exergonic reduction of caffeoyl-CoA with the same reductant. It uses the mechanism of electron bifurcation to overcome the steep energy barrier in ferredoxin reduction. It also reduces 4-coumaroyl-CoA and feruloyl-CoA.
the caffeoyl-CoA reductase-Etf complex of Acetobacterium woodii uses the mechanism of flavin-dependent electron bifurcation to drive the endergonic ferredoxin reduction with NADH as reductant by coupling it to the exergonic NADH-dependent reduction of caffeoyl-CoA
the caffeyl-CoA reductase-Etf complex of Acetobacterium woodii uses the mechanism of flavin-dependent electron bifurcation to drive the endergonic ferredoxin reduction with NADH as reductant by coupling it to the exergonic NADH-dependent reduction of caffeoyl-CoA. Reduction of caffeoyl-CoA is also catalyzed in absence of ferredoxin
the caffeoyl-CoA reductase-Etf complex of Acetobacterium woodii uses the mechanism of flavin-dependent electron bifurcation to drive the endergonic ferredoxin reduction with NADH as reductant by coupling it to the exergonic NADH-dependent reduction of caffeoyl-CoA
the caffeyl-CoA reductase-Etf complex of Acetobacterium woodii uses the mechanism of flavin-dependent electron bifurcation to drive the endergonic ferredoxin reduction with NADH as reductant by coupling it to the exergonic NADH-dependent reduction of caffeoyl-CoA. Reduction of caffeoyl-CoA is also catalyzed in absence of ferredoxin
the caffeoyl-CoA reductase-Etf complex of Acetobacterium woodii uses the mechanism of flavin-dependent electron bifurcation to drive the endergonic ferredoxin reduction with NADH as reductant by coupling it to the exergonic NADH-dependent reduction of caffeoyl-CoA
the caffeoyl-CoA reductase-Etf complex of Acetobacterium woodii uses the mechanism of flavin-dependent electron bifurcation to drive the endergonic ferredoxin reduction with NADH as reductant by coupling it to the exergonic NADH-dependent reduction of caffeoyl-CoA
the enzyme contains 4 mol of FAD per of enzyme. The CarCDE complex requires FAD for catalytic activity. No activity can be detected when FAD or FMN (0.25 mM) are used alone as electron acceptor, but together with caffeyl-CoA, they are completely reduced with NADH as reductant. Caffeyl-CoA reduction is stimulated by 26- and 12fold with FAD and FMN, respectively. The Km value for both FAD and FMN is 0.1 mM. Thus, caffeyl-CoA and flavins are reduced simultaneously
no activity can be detected when FAD or FMN (0.25 mM) are used alone as electron acceptor, but together with caffeyl-CoA, they are completely reduced with NADH as reductant. Caffeyl-CoA reduction is stimulated by 26- and 12-fold with FAD and FMN, respectively. The Km value for both FAD and FMN is 0.1 mM. Thus, caffeyl-CoA and flavins are reduced simultaneously
H6LGM6: caffeoyl-CoA reductase CarC, H6LGM7: electron transfer flavoprotein beta subunit CarD, H6LGM8: electron transfer flavoprotein alpha subunit CarE
H6LGM6: caffeoyl-CoA reductase CarC, H6LGM7: electron transfer flavoprotein beta subunit CarD, H6LGM8: electron transfer flavoprotein alpha subunit CarE
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1.3.1.108 caffeoyl-CoA reductase
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