Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Display Documents


Institute:
Collection:
Print in Citation style Print version     Display:
Sort by: Display records with Fulltext only
Entries: 1-10  
 Basket 
Coupled ferredoxin- and crotonyl-CoA reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri.
Authors: Li, Fuli; Hinderberger, Julia; Seedorf, Henning; Zhang, Jin; Buckel, Wolfgang; Thauer, Rudolf
Date of Publication (YYYY-MM-DD): 2008-02
Title of Journal: Journal of Bacteriology
Volume: 190
Issue / Number: 3
Start Page: 843
End Page: 50
Document Type: Article
ID: 330275.0
The exchange activities of [Fe] hydrogenase (iron-sulfur-cluster-free hydrogenase) from methanogenic archaea in comparison with the exchange activities of [FeFe] and [NiFe] hydrogenases.
Authors: Vogt, Sonja; Lyon, Erica; Shima, Seigo; Thauer, Rudolf
Date of Publication (YYYY-MM-DD): 2008-01
Title of Journal: J Biol Inorg Chem.
Volume: 13
Issue / Number: 1
Start Page: 97
End Page: 106
Document Type: Article
ID: 328878.0
Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy.
Authors: Kern, Denis; Goenrich, Meike; Jaun, Bernhard; Thauer, Rudolf; Harmer, Jeffrey; Hinderberger, Dariush
Date of Publication (YYYY-MM-DD): 2007-11
Title of Journal: Journal of Biological Inorganic Chemistry
Volume: 12
Issue / Number: 8
Start Page: 1097
End Page: 105
Document Type: Article
ID: 323890.0
The CO and CN(-) ligands to the active site Fe in [NiFe]-hydrogenase of Escherichia coli have different metabolic origins.
Authors: Forzi, Lucia; Hellwig, Petra; Thauer, Rudolf; Sawers, Gary
Date of Publication (YYYY-MM-DD): 2007-07-10
Title of Journal: FEBS Letters
Volume: 581
Issue / Number: 17
Start Page: 3317
End Page: 21
Document Type: Article
ID: 319487.0
Structure of coenzyme F420H2 oxidase (FprA), a di-iron flavoprotein from methanogenic Archaea catalyzing the reduction of O2 to H2O.
Authors: Seedorf, Henning; Hagemeier, Christoph; Shima, Seigo; Thauer, Rudolf; Warkentin, Eberhard; Ermler, Ulrich
Date of Publication (YYYY-MM-DD): 2007-03
Title of Journal: FEBS Journal
Volume: 274
Start Page: 1588
End Page: 99
Document Type: Article
ID: 319465.0
Re-citrate synthase from Clostridium kluyveri is phylogenetically related to homocitrate synthase and isopropylmalate synthase rather than to Si-citrate synthase.
Authors: Li, Fuli; Hagemeier, Christoph; Seedorf, Henning; Gottschalk, Gerhard; Thauer, Rudolf
Date of Publication (YYYY-MM-DD): 2007-03
Title of Journal: Journal of Bacteriology
Volume: 189
Issue / Number: 11
Start Page: 4299
End Page: 4304
Document Type: Article
ID: 319486.0
Metal-Carbon bonds in Biology.
Authors: Thauer, Rudolf
Title of Book: In Metial ions in Life Sciences, vol 2
Start Page: 1
End Page: 702
Place of Publication: Chichester
Publisher: Wiley & Sons Ltd.
Date of Publication (YYYY-MM-DD): 2007
Document Type: InBook
ID: 298237.0
A third type of hydrogenase catalyzing H2 activaton.
Authors: Thauer, Rudolf; Shima, Seigo
Date of Publication (YYYY-MM-DD): 2007
Title of Journal: The Chemical Record
Volume: 7
Issue / Number: 1
Start Page: 37
End Page: 46
Document Type: Article
ID: 302150.0
Energy Metabolism of Sulphate Reducing Bacteria.
Authors: Thauer, Rudolf; Stackebrandt, E.; Hamilton, W.A.
Title of Book: Sulphate-Reducing Bacteria: Environmental and Engineered Systems
Start Page: 1
End Page: 37
Place of Publication: Cambridge/USA
Publisher: Cambridge University Press
Date of Publication (YYYY-MM-DD): 2007
Document Type: InBook
ID: 319485.0
Methyl-coenzyme M reductase in methanogens and methanotrophs.
Authors: Thauer, Rudolf; Shima, Seigo
Title of Book: Archaea, Evolution, Physiology and Molecuar Biology
Start Page: 275
End Page: 83
Place of Publication: Malden, USA
Publisher: Blackwell Publishing, Inc
Date of Publication (YYYY-MM-DD): 2007
Document Type: InBook
ID: 328874.0
Entries: 1-10  
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.