This Article
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 Maeng, J. H.
Right arrow Articles by Kato, N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Maeng, J. H.
Right arrow Articles by Kato, N.

 Previous Article  |  Next Article 

J. Bacteriol., 07 1996, 3695-3700, Vol 178, No. 13
Copyright © 1996, American Society for Microbiology

Isolation and characterization of a novel oxygenase that catalyzes the first step of n-alkane oxidation in Acinetobacter sp. strain M-1

JH Maeng, Y Sakai, Y Tani and N Kato
Department of Agricultural Chemistry, Kyoto University, Japan.

In the Finnerty pathway for n-alkane, oxidation in Acinetobacter sp., n- alkanes are postulated to be attacked by a dioxygenase and the product, n-alkyl hydroperoxide, is further metabolized to the corresponding aldehyde via the peroxy acid [W. R. Finnerty, P. 184-188, in A. H. Applewhite (ed.), Proceedings of the World Conference on Biotechnology for the Fats and Oil Industry, 1988]. However, no biochemical evidence regarding the first-step reaction is available. In this study, we found a novel n-alkane-oxidizing enzyme that requires only molecular oxygen, i.e., not NAD(P)H, in our isolate, Acinetobacter sp. strain M-1, and purified it to apparent homogeneity by gel electrophoresis. The purified enzyme is a homodimeric protein with a molecular mass of 134 kDa, contains 1 mol of flavin adenine dinucleotide per mol of subunit, and requires CU2+ for its activity. The enzyme uses n-alkanes ranging in length from 10 to 30 carbon atoms and is also active toward n- alkenes (C12 to C20) and some aromatic compounds with substituted alkyl groups but not toward a branched alkane, alcohol, or aldehyde. Transient accumulation of n-alkyl hydroperoxide was detected in the course of the reaction, and no oxygen radical scavengers affected the enzyme activity. From these properties, the enzyme is most probably a dioxygenase that catalyzes the introduction of two atoms of oxygen to the substrate, leading to the formation of the corresponding n-alkyl hydroperoxide. The enzymatic evidence strongly supports the existence of an n-alkane oxidation pathway, which is initiated by a dioxygenase reaction, in Acinetobacter spp.


This article has been cited by other articles:

  • Wasmund, K., Burns, K. A., Kurtboke, D. I., Bourne, D. G. (2009). Novel Alkane Hydroxylase Gene (alkB) Diversity in Sediments Associated with Hydrocarbon Seeps in the Timor Sea, Australia. Appl. Environ. Microbiol. 75: 7391-7398 [Abstract] [Full Text]  
  • Callaghan, A. V., Tierney, M., Phelps, C. D., Young, L. Y. (2009). Anaerobic Biodegradation of n-Hexadecane by a Nitrate-Reducing Consortium. Appl. Environ. Microbiol. 75: 1339-1344 [Abstract] [Full Text]  
  • Throne-Holst, M., Wentzel, A., Ellingsen, T. E., Kotlar, H.-K., Zotchev, S. B. (2007). Identification of Novel Genes Involved in Long-Chain n-Alkane Degradation by Acinetobacter sp. Strain DSM 17874. Appl. Environ. Microbiol. 73: 3327-3332 [Abstract] [Full Text]  
  • Van Hamme, J. D., Singh, A., Ward, O. P. (2003). Recent Advances in Petroleum Microbiology. Microbiol. Mol. Biol. Rev. 67: 503-549 [Abstract] [Full Text]  
  • Cussiol, J. R. R., Alves, S. V., Antonio de Oliveira, M., Netto, L. E. S. (2003). Organic Hydroperoxide Resistance Gene Encodes a Thiol-dependent Peroxidase. J. Biol. Chem. 278: 11570-11578 [Abstract] [Full Text]  
  • Vangnai, A. S., Arp, D. J., Sayavedra-Soto, L. A. (2002). Two Distinct Alcohol Dehydrogenases Participate in Butane Metabolism by Pseudomonas butanovora. J. Bacteriol. 184: 1916-1924 [Abstract] [Full Text]  
  • Hamamura, N., Yeager, C. M., Arp, D. J. (2001). Two Distinct Monooxygenases for Alkane Oxidation in Nocardioides sp. Strain CF8. Appl. Environ. Microbiol. 67: 4992-4998 [Abstract] [Full Text]  
  • Geißdörfer, W., Kok, R. G., Ratajczak, A., Hellingwerf, K. J., Hillen, W. (1999). The Genes rubA and rubB for Alkane Degradation in Acinetobacter sp. Strain ADP1 Are in an Operon with estB, Encoding an Esterase, and oxyR. J. Bacteriol. 181: 4292-4298 [Abstract] [Full Text]  
  • Mongkolsuk, S., Praituan, W., Loprasert, S., Fuangthong, M., Chamnongpol, S. (1998). Identification and Characterization of a New Organic Hydroperoxide Resistance (ohr) Gene with a Novel Pattern of Oxidative Stress Regulation from Xanthomonas campestris pv. phaseoli. J. Bacteriol. 180: 2636-2643 [Abstract] [Full Text]  
  • Ratajczak, A., Geißdörfer, W., Hillen, W. (1998). Alkane Hydroxylase from Acinetobacter sp. Strain ADP1 Is Encoded by alkM and Belongs to a New Family of Bacterial Integral-Membrane Hydrocarbon Hydroxylases. Appl. Environ. Microbiol. 64: 1175-1179 [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»