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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

Chowdhury, N. P., Mowafy, A. M., Demmer, J. K., Upadhyay, V., Koelzer, S., Jayamani, E., et al. (2014). Studies on the Mechanism of Electron Bifurcation Catalyzed by Electron Transferring Flavoprotein (Etf) and Butyryl-CoA Dehydrogenase (Bcd) of Acidaminococcus fermentans. The Journal of Biological Chemistry, 289(8), 5145-5157. doi:10.1074/jbc.M113.521013.

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 Creators:
Chowdhury, Nilanjan Pal1, 2, Author
Mowafy, Amr M.1, 2, Author
Demmer, Julius K.2, 3, Author           
Upadhyay, Vikrant3, Author           
Koelzer, Sebastian1, Author
Jayamani, Elamparithi1, 2, Author
Kahnt, Joerg2, Author
Hornung, Marco1, 2, Author
Demmer, Ulrike3, Author           
Ermler, Ulrich3, Author           
Buckel, Wolfgang1, 2, Author
Affiliations:
1Laboratorium für Mikrobiologie, Fachbereich Biologie and SYNMIKRO, Philipps-Universität, 35032 Marburg, Germany, ou_persistent22              
2Max-Planck-Institut für terrestrische Mikrobiologie, Karl-von-Frisch-Str. 10, 35043 Marburg, Max Planck Society, Germany, ou_persistent22              
3Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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 Abstract: 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 nonstabilized neutral semiquinone, β-FADHˑ, 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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Language(s): eng - English
 Dates: 201420142014-02-21
 Publication Status: Published in print
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.M113.521013
 Degree: -

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Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: 14 Volume / Issue: 289 (8) Sequence Number: - Start / End Page: 5145 - 5157 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1