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  NADP+ reduction with reduced ferredoxin and NADP+ reduction with NADH are coupled via an electron-bifurcating enzyme complex in Clostridium kluyveri

Wang, S. N., Huang, H. Y., Moll, J., & Thauer, R. K. (2010). NADP+ reduction with reduced ferredoxin and NADP+ reduction with NADH are coupled via an electron-bifurcating enzyme complex in Clostridium kluyveri. Journal of Bacteriology, 192(19), 5115-5123. doi:10.1128/jb.00612-10.

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https://doi.org/10.1128/jb.00612-10 (Publisher version)
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 Creators:
Wang, S. N.1, Author           
Huang, H. Y.2, Author           
Moll, J.2, Author           
Thauer, R. K.3, Author           
Affiliations:
1Department of Biogeochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266312              
2Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266311              
3Emeriti Biochemistry of Anaerobic Microorganisms, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266289              

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 Abstract: It was recently found that the cytoplasmic butyryl-coenzyme A (butyryl-CoA) dehydrogenase-EtfAB complex from Clostridium kluyveri couples the exergonic reduction of crotonyl-CoA to butyryl-CoA with NADH and the endergonic reduction of ferredoxin with NADH via flavin-based electron bifurcation. We report here on a second cytoplasmic enzyme complex in C. kluyveri capable of energetic coupling via this novel mechanism. It was found that the purified iron-sulfur flavoprotein complex NfnAB couples the exergonic reduction of NADP+ with reduced ferredoxin (Fdred) and the endergonic reduction of NADP+ with NADH in a reversible reaction: Fdred2− + NADH + 2 NADP+ + H+ = Fdox + NAD+ + 2 NADPH. The role of this energy-converting enzyme complex in the ethanol-acetate fermentation of C. kluyveri is discussed.

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Language(s): eng - English
 Dates: 2010-10-01
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 545768
ISI: 000281866900032
DOI: 10.1128/jb.00612-10
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Title: Journal of Bacteriology
  Other : J. Bacteriol.
Source Genre: Journal
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Publ. Info: Washington, DC : American Society for Microbiology (ASM)
Pages: - Volume / Issue: 192 (19) Sequence Number: - Start / End Page: 5115 - 5123 Identifier: ISSN: 0021-9193
CoNE: https://pure.mpg.de/cone/journals/resource/954925410823