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 van Beilen, J. B.
Right arrow Articles by Witholt, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by van Beilen, J. B.
Right arrow Articles by Witholt, B.

 Previous Article  |  Next Article 

Journal of Bacteriology, March 2002, p. 1722-1732, Vol. 184, No. 6
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.6.1722-1732.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Rubredoxins Involved in Alkane Oxidation

Jan B. van Beilen,* Martin Neuenschwander, Theo H. M. Smits,,{dagger} Christian Roth, Stefanie B. Balada, and Bernard Witholt

Institute of Biotechnology, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093 Zürich, Switzerland

Received 2 November 2001/ Accepted 20 December 2001

Rubredoxins (Rds) are essential electron transfer components of bacterial membrane-bound alkane hydroxylase systems. Several Rd genes associated with alkane hydroxylase or Rd reductase genes were cloned from gram-positive and gram-negative organisms able to grow on n-alkanes (Alk-Rds). Complementation tests in an Escherichia coli recombinant containing all Pseudomonas putida GPo1 genes necessary for growth on alkanes except Rd 2 (AlkG) and sequence comparisons showed that the Alk-Rds can be divided in AlkG1- and AlkG2-type Rds. All alkane-degrading strains contain AlkG2-type Rds, which are able to replace the GPo1 Rd 2 in n-octane hydroxylation. Most strains also contain AlkG1-type Rds, which do not complement the deletion mutant but are highly conserved among gram-positive and gram-negative bacteria. Common to most Rds are the two iron-binding CXXCG motifs. All Alk-Rds possess four negatively charged residues that are not conserved in other Rds. The AlkG1-type Rds can be distinguished from the AlkG2-type Rds by the insertion of an arginine downstream of the second CXXCG motif. In addition, the glycines in the two CXXCG motifs are usually replaced by other amino acids. Mutagenesis of residues conserved in either the AlkG1- or the AlkG2-type Rds, but not between both types, shows that AlkG1 is unable to transfer electrons to the alkane hydroxylase mainly due to the insertion of the arginine, whereas the exchange of the glycines in the two CXXCG motifs only has a limited effect.

* Corresponding author. Mailing address: Institute of Biotechnology, Swiss Federal Institute of Technology, ETH-Hönggerberg, CH-8093 Zürich, Switzerland. Phone: 41 1 633 3444. Fax: 41 1 633 1051. E-mail: vanbeilen{at}biotech.biol.ethz.ch.

{dagger} Present address: ENAC/LBE, EPFL, CH-1015 Lausanne, Switzerland.

Journal of Bacteriology, March 2002, p. 1722-1732, Vol. 184, No. 6
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.6.1722-1732.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Hagelueken, G., Wiehlmann, L., Adams, T. M., Kolmar, H., Heinz, D. W., Tummler, B., Schubert, W.-D. (2007). Crystal structure of the electron transfer complex rubredoxin rubredoxin reductase of Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. USA 104: 12276-12281 [Abstract] [Full Text]  
  • Kane, S. R., Chakicherla, A. Y., Chain, P. S. G., Schmidt, R., Shin, M. W., Legler, T. C., Scow, K. M., Larimer, F. W., Lucas, S. M., Richardson, P. M., Hristova, K. R. (2007). Whole-Genome Analysis of the Methyl tert-Butyl Ether-Degrading Beta-Proteobacterium Methylibium petroleiphilum PM1. J. Bacteriol. 189: 1931-1945 [Abstract] [Full Text]  
  • Maruyama, T., Ishikura, M., Taki, H., Shindo, K., Kasai, H., Haga, M., Inomata, Y., Misawa, N. (2005). Isolation and Characterization of o-Xylene Oxygenase Genes from Rhodococcus opacus TKN14. Appl. Environ. Microbiol. 71: 7705-7715 [Abstract] [Full Text]  
  • Vicente, J. B., Teixeira, M. (2005). Redox and Spectroscopic Properties of the Escherichia coli Nitric Oxide-detoxifying System Involving Flavorubredoxin and Its NADH-oxidizing Redox Partner. J. Biol. Chem. 280: 34599-34608 [Abstract] [Full Text]  
  • Marin, M. M., Yuste, L., Rojo, F. (2003). Differential Expression of the Components of the Two Alkane Hydroxylases from Pseudomonas aeruginosa. J. Bacteriol. 185: 3232-3237 [Abstract] [Full Text]  
  • Whyte, L. G., Smits, T. H. M., Labbe, D., Witholt, B., Greer, C. W., van Beilen, J. B. (2002). Gene Cloning and Characterization of Multiple Alkane Hydroxylase Systems in Rhodococcus Strains Q15 and NRRL B-16531. Appl. Environ. Microbiol. 68: 5933-5942 [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»