Properties of azoferredoxin purified from nitrogen-fixing extracts of Clostridium pasteurianum
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference21 articles.
1. Purification, metal composition and properties of molybdo-ferredoxin and azoferredoxin, two of the components of the nitrogen-fixing system of Clostridium pasteurianum
2. Acetylene Reduction by Nitrogen Fixing Extracts of Clostridium pasteurianum: ATP Requirement and Inhibition by ADP
3. Studies of cold lability and purification of a nitrogen-activating enzyme
4. E. Moustafa and L. E. Mortenson, Anal. Biochem., in the press.
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1. Thermodynamics of nucleotide interactions with the Azotobacter vinelandii nitrogenase iron protein;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1999-01
2. Specific Interaction of the [2Fe-2S] Ferredoxin from Clostridium pasteurianum with the Nitrogenase MoFe Protein;Biochemistry;1997-09-01
3. EPR and Mössbauer studies of nucleotide-bound nitrogenase iron protein from Azotobacter vinelandii.;Journal of Biological Chemistry;1987-11
4. Influence of acetylene on microbial and enzymatic assays;Journal of Microbiological Methods;1984-05
5. Fully Active Fe-Protein of the Nitrogenase from Azotobacter vinelandii Contains at least Eight Iron Atoms and Eight Sulphide Atoms per Molecule;European Journal of Biochemistry;1983-06
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