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Clostridium pasteurianum

Known as: Clostridium pastorianus, Butyribacillus pasteurianus, Bacillus winogradsky 
National Institutes of Health

Papers overview

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2011
2011
Phytase‐active yeasts from grain‐based food and beer
Aims:  To screen yeast strains isolated from grain‐based food and beer for phytase activity to identify high phytase‐active… 
2006
2006
Tetrathiolate coordination of germanium(IV) in a protein active site.
2004
2004
Metal-substituted derivatives of the rubredoxin from Clostridium pasteurianum.
Five different metal-substituted forms of Clostridium pasteurianum rubredoxin have been prepared and crystallized. The single Fe… 
2001
2001
Leucine 41 is a gate for water entry in the reduction of Clostridium pasteurianum rubredoxin
Biological electron transfer is an efficient process even though the distances between the redox moieties are often quite large… 
2000
2000
Thermal stability of Clostridium pasteurianum rubredoxin: Deconvoluting the contributions of the metal site and the protein
To provide a framework for understanding the hyperthermostability of some rubredoxins, a comprehensive analysis of the thermally… 
1998
1998
Solution structure of reduced Clostridium pasteurianum rubredoxin
Abstract The solution structure of reduced Clostridium pasteurianum rubredoxin (MW 6100) is reported here. The protein is highly… 
1997
1997
Assembly of a [2Fe-2S]2+ cluster in a molecular variant of Clostridium pasteurianum rubredoxin.
The rubredoxin from Clostridium pasteurianum contains a single iron atom bound to the polypeptide chain by cysteines 6, 9, 39… 
Highly Cited
1997
Highly Cited
1997
Dissecting contributions to the thermostability of Pyrococcus furiosus rubredoxin: beta-sheet chimeras.
The contributions to thermostability of interactions within the beta-sheet region of rubredoxins (Rds) were investigated by… 
1988
1988
Distinct structural features of the alpha and beta subunits of nitrogenase molybdenum-iron protein of Clostridium pasteurianum: an analysis of amino acid sequences.
Nitrogenase is composed of two separately purified proteins, a molybdenum-iron (MoFe) protein and an iron (Fe) protein… 
1986
1986
On the novel H2-activating iron-sulfur center of the "Fe-only" hydrogenases.
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