English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Anaerobic degradation of naphthalene and 2-methylnaphthalene by strains of marine sulfate-reducing bacteria.

Musat, F., Galushko, A., Jacob, J., Widdel, F., Kube, M., Reinhardt, R., et al. (2009). Anaerobic degradation of naphthalene and 2-methylnaphthalene by strains of marine sulfate-reducing bacteria. Environmental Microbiology, 11(1), 209-219. doi:10.1111/j.1462-2920.2008.01756.x.

Item is

Basic

show hide
Genre: Journal Article
Alternative Title : Environ Microbiol

Files

show Files
hide Files
:
fulltext.pdf (Any fulltext), 299KB
 
File Permalink:
-
Name:
fulltext.pdf
Description:
-
OA-Status:
Visibility:
Restricted (Max Planck Institute for Molecular Genetics, MBMG; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
eDoc_access: MPG
License:
-

Locators

show

Creators

show
hide
 Creators:
Musat, Florin1, Author
Galushko, Alexander1, Author
Jacob, Jacob1, Author
Widdel, Friedrich1, Author
Kube, Michael2, Author           
Reinhardt, Richard2, Author           
Wilkes, Heinz, Author
Schink, Bernhard, Author
Rabus, Ralf1, Author
Affiliations:
1Max Planck Society, ou_persistent13              
2High Throughput Technologies, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433552              

Content

show
hide
Free keywords: -
 Abstract: The anaerobic biodegradation of naphthalene, an aromatic hydrocarbon in tar and petroleum, has been repeatedly observed in environments but scarcely in pure cultures. To further explore the relationships and physiology of anaerobic naphthalene-degrading microorganisms, sulfate-reducing bacteria (SRB) were enriched from a Mediterranean sediment with added naphthalene. Two strains (NaphS3, NaphS6) with oval cells were isolated which showed naphthalene-dependent sulfate reduction. According to 16S rRNA gene sequences, both strains were Deltaproteobacteria and closely related to each other and to a previously described naphthalene-degrading sulfate-reducing strain (NaphS2) from a North Sea habitat. Other close relatives were SRB able to degrade alkylbenzenes, and phylotypes enriched anaerobically with benzene. If in adaptation experiments the three naphthalene-grown strains were exposed to 2-methylnaphthalene, this compound was utilized after a pronounced lag phase, indicating that naphthalene did not induce the capacity for 2-methylnaphthalene degradation. Comparative denaturing gel electrophoresis of cells grown with naphthalene or 2-methylnaphthalene revealed a striking protein band which was only present upon growth with the latter substrate. Peptide sequences from this band perfectly matched those of a protein predicted from genomic libraries of the strains. Sequence similarity (50% identity) of the predicted protein to the large subunit of the toluene-activating enzyme (benzylsuccinate synthase) from other anaerobic bacteria indicated that the detected protein is part of an analogous 2-methylnaphthalene-activating enzyme. The absence of this protein in naphthalene-grown cells together with the adaptation experiments as well as isotopic metabolite differentiation upon growth with a mixture of d8-naphthalene and unlabelled 2-methylnaphthalene suggest that the marine strains do not metabolize naphthalene by initial methylation via 2-methylnaphthalene, a previously suggested mechanism. The inability to utilize 1-naphthol or 2-naphthol also excludes these compounds as free intermediates. Results leave open the possibility of naphthalene carboxylation, another previously suggested activation mechanism.

Details

show
hide
Language(s): eng - English
 Dates: 2009-01-01
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Environmental Microbiology
  Alternative Title : Environ Microbiol
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 11 (1) Sequence Number: - Start / End Page: 209 - 219 Identifier: ISSN: 1462-2912