This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bevers, L. E.
Right arrow Articles by Hagen, W. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bevers, L. E.
Right arrow Articles by Hagen, W. R.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2005, p. 7056-7061, Vol. 187, No. 20
0021-9193/05/$08.00+0     doi:10.1128/JB.187.20.7056-7061.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

WOR5, a Novel Tungsten-Containing Aldehyde Oxidoreductase from Pyrococcus furiosus with a Broad Substrate Specificity

Loes E. Bevers, Emile Bol, Peter-Leon Hagedoorn, and Wilfred R. Hagen*

Department of Biotechnology, Delft University of Technology, Delft, The Netherlands

Received 27 April 2005/ Accepted 27 July 2005

WOR5 is the fifth and last member of the family of tungsten-containing oxidoreductases purified from the hyperthermophilic archaeon Pyrococcus furiosus. It is a homodimeric protein (subunit, 65 kDa) that contains one [4Fe-4S] cluster and one tungstobispterin cofactor per subunit. It has a broad substrate specificity with a high affinity for several substituted and nonsubstituted aliphatic and aromatic aldehydes with various chain lengths. The highest catalytic efficiency of WOR5 is found for the oxidation of hexanal (Vmax = 15.6 U/mg, Km = 0.18 mM at 60°C). Hexanal-incubated enzyme exhibits S = 1/2 electron paramagnetic resonance signals from [4Fe-4S]1+ (g values of 2.08, 1.93, and 1.87) and W5+ (g values of 1.977, 1.906, and 1.855). Cyclic voltammetry of ferredoxin and WOR5 on an activated glassy carbon electrode shows a catalytic wave upon addition of hexanal, suggesting that ferredoxin can be a physiological redox partner. The combination of WOR5, formaldehyde oxidoreductase, and aldehyde oxidoreductase forms an efficient catalyst for the oxidation of a broad range of aldehydes in P. furiosus.

* Corresponding author. Mailing address: Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands. Phone: 31 15 2785051. Fax: 31 15 2782355. E-mail: w.r.hagen{at}tnw.tudelft.nl.

Journal of Bacteriology, October 2005, p. 7056-7061, Vol. 187, No. 20
0021-9193/05/$08.00+0     doi:10.1128/JB.187.20.7056-7061.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Chou, C.-J., Shockley, K. R., Conners, S. B., Lewis, D. L., Comfort, D. A., Adams, M. W. W., Kelly, R. M. (2007). Impact of Substrate Glycoside Linkage and Elemental Sulfur on Bioenergetics of and Hydrogen Production by the Hyperthermophilic Archaeon Pyrococcus furiosus. Appl. Environ. Microbiol. 73: 6842-6853 [Abstract] [Full Text]  
  • Bevers, L. E., Hagedoorn, P.-L., Krijger, G. C., Hagen, W. R. (2006). Tungsten Transport Protein A (WtpA) in Pyrococcus furiosus: the First Member of a New Class of Tungstate and Molybdate Transporters.. J. Bacteriol. 188: 6498-6505 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»