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Gene Review

WS1647  -  flavoprotein

Wolinella succinogenes DSM 1740

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Disease relevance of WS1647


High impact information on WS1647

  • The results suggest that the reduction of methacrylate or acrylate by benzyl viologen radical is most likely catalyzed either by the periplasmic flavoprotein FccA or by a complex consisting of FccA and the predicted c-type cytochrome FccB [3].
  • Previously, the crystal structure of QFR from Wolinella succinogenes was determined based on two different crystal forms, and the site of fumarate binding in the flavoprotein subunit A of the enzyme was located between the FAD-binding domain and the capping domain [Lancaster, C.R.D., Kröger, A., Auer, M., & Michel, H. (1999) Nature 402, 377--385] [4].
  • A monomeric flavoprotein (18.8 kDa) was isolated from the soluble cell fraction of Wolinella succinogenes and was identified as a flavodoxin based on its N-terminal sequence, FMN content, and redox properties [5].


  1. Essential role of Glu-C66 for menaquinol oxidation indicates transmembrane electrochemical potential generation by Wolinella succinogenes fumarate reductase. Lancaster, C.R., Gorss, R., Haas, A., Ritter, M., Mäntele, W., Simon, J., Kröger, A. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  2. A periplasmic flavoprotein in Wolinella succinogenes that resembles the fumarate reductase of Shewanella putrefaciens. Simon, J., Gross, R., Klimmek, O., Ringel, M., Kröger, A. Arch. Microbiol. (1998) [Pubmed]
  3. Periplasmic methacrylate reductase activity in Wolinella succinogenes. Gross, R., Simon, J., Kröger, A. Arch. Microbiol. (2001) [Pubmed]
  4. A third crystal form of Wolinella succinogenes quinol:fumarate reductase reveals domain closure at the site of fumarate reduction. Lancaster, C.R., Gross, R., Simon, J. Eur. J. Biochem. (2001) [Pubmed]
  5. Flavodoxin from Wolinella succinogenes. Biel, S., Klimmek, O., Gross, R., Kröger, A. Arch. Microbiol. (1996) [Pubmed]
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