English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  A conspicuous nickel protein in microbial mats that oxidize methane anaerobically

Krüger, M., Meyerdierks, A., Glöckner, F. O., Amann, R., Widdel, F., Kube, M., et al. (2003). A conspicuous nickel protein in microbial mats that oxidize methane anaerobically. Nature, 426(6968), 878-881.

Item is

Files

show Files
hide Files
:
Krueger4.pdf (Publisher version), 511KB
 
File Permalink:
-
Name:
Krueger4.pdf
Description:
-
OA-Status:
Visibility:
Restricted ( Max Planck Society (every institute); )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Krüger, M.1, Author           
Meyerdierks, A.2, Author           
Glöckner, F. O.3, Author           
Amann, R.2, Author           
Widdel, F.1, Author           
Kube, M.2, Author           
Reinhardt, R.1, Author           
Kahnt, R., Author
Bocher, R., Author
Thauer, R. K.1, Author           
Shima, S.4, Author           
Affiliations:
1Department of Microbiology, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481695              
2Department of Molecular Ecology, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481696              
3Microbial Genomics Group, Department of Molecular Ecology, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481697              
4Department of Biogeochemistry, Max Planck Institute for Marine Microbiology, Max Planck Society, ou_2481693              

Content

show
hide
Free keywords: -
 Abstract: Anaerobic oxidation of methane (AOM) in marine sediments is an important microbial process in the global carbon cycle and in control of greenhouse gas emission. The responsible organisms supposedly reverse the reactions of methanogenesis1,2,3,4,5,6,7,8, but cultures providing biochemical proof of this have not been isolated. Here we searched for AOM-associated cell components in microbial mats from anoxic methane seeps in the Black Sea9,10,11. These mats catalyse AOM rather than carry out methanogenesis. We extracted a prominent nickel compound displaying the same absorption spectrum as the nickel cofactor F430 of methyl-coenzyme M reductase, the terminal enzyme of methanogenesis12; however, the nickel compound exhibited a higher molecular mass than F430. The apparent variant of F430 was part of an abundant protein that was purified from the mat and that consists of three different subunits. Determined amino-terminal amino acid sequences matched a gene locus cloned from the mat. Sequence analyses revealed similarities to methyl-coenzyme M reductase from methanogenic archaea. The abundance of the nickel protein (7% of extracted proteins) in the mat suggests an important role in AOM.

Details

show
hide
Language(s): eng - English
 Dates: 2003-12-18
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 176805
ISI: 000187342000068
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature
  Abbreviation : Nature
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 426 (6968) Sequence Number: - Start / End Page: 878 - 881 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238