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PDBsum entry 4l1f
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Electron transport
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PDB id
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4l1f
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PDB id:
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| Name: |
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Electron transport
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Title:
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Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation
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Structure:
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Acyl-coa dehydrogenase domain protein. Chain: a, b
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Source:
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Acidaminococcus fermentans. Organism_taxid: 591001. Strain: dsm 20731
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Resolution:
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1.79Å
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R-factor:
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0.155
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R-free:
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0.183
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Authors:
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A.M.Mowafy,N.P.Chowdhury,J.Demmer,V.Upadhyay,S.Kolzer,E.Jayamani, J.Kahnt,U.Demmer,U.Ermler,W.Buckel
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Key ref:
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N.P.Chowdhury
et al.
(2014).
Studies on the mechanism of electron bifurcation catalyzed by electron transferring flavoprotein (Etf) and butyryl-CoA dehydrogenase (Bcd) of Acidaminococcus fermentans.
J Biol Chem,
289,
5145-5157.
PubMed id:
DOI:
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Date:
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03-Jun-13
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Release date:
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15-Jan-14
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PROCHECK
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Headers
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References
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D2RL84
(D2RL84_ACIFV) -
Acyl-CoA dehydrogenase domain protein from Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4)
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Seq:
Struc:
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383 a.a.
380 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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J Biol Chem
289:5145-5157
(2014)
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PubMed id:
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Studies on the mechanism of electron bifurcation catalyzed by electron transferring flavoprotein (Etf) and butyryl-CoA dehydrogenase (Bcd) of Acidaminococcus fermentans.
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N.P.Chowdhury,
A.M.Mowafy,
J.K.Demmer,
V.Upadhyay,
S.Koelzer,
E.Jayamani,
J.Kahnt,
M.Hornung,
U.Demmer,
U.Ermler,
W.Buckel.
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ABSTRACT
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Electron bifurcation is a fundamental strategy of energy coupling originally
discovered in the Q-cycle of many organisms. Recently a flavin-based electron
bifurcation has been detected in anaerobes, first in clostridia and later in
acetogens and methanogens. It enables anaerobic bacteria and archaea to reduce
the low-potential [4Fe-4S] clusters of ferredoxin, which increases the
efficiency of the substrate level and electron transport phosphorylations. Here
we characterize the bifurcating electron transferring flavoprotein (EtfAf) and
butyryl-CoA dehydrogenase (BcdAf) of Acidaminococcus fermentans, which couple
the exergonic reduction of crotonyl-CoA to butyryl-CoA to the endergonic
reduction of ferredoxin both with NADH. EtfAf contains one FAD (α-FAD) in
subunit α and a second FAD (β-FAD) in subunit β. The distance between the two
isoalloxazine rings is 18 Å. The EtfAf-NAD(+) complex structure revealed
β-FAD as acceptor of the hydride of NADH. The formed β-FADH(-) is considered
as the bifurcating electron donor. As a result of a domain movement, α-FAD is
able to approach β-FADH(-) by about 4 Å and to take up one electron yielding
a stable anionic semiquinone, α-FAD, which donates this electron further to
Dh-FAD of BcdAf after a second domain movement. The remaining non-stabilized
neutral semiquinone, β-FADH(•), immediately reduces ferredoxin. Repetition of
this process affords a second reduced ferredoxin and Dh-FADH(-) that converts
crotonyl-CoA to butyryl-CoA.
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Links
