Iron-molybdenum cofactor from nitrogenase. Modified extraction methods as probes for composition.
Open Access
- 1 July 1982
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 257 (14) , 8042-8048
- https://doi.org/10.1016/s0021-9258(18)34294-7
Abstract
No abstract availableThis publication has 24 references indexed in Scilit:
- Spectroscopic investigation of FeMo-cofactor. Coenzyme A as one of the probable components of an active site of nitrogenaseBiochemical and Biophysical Research Communications, 1980
- Large-scale purification of high activity Azotobacter vinelandii nitrogenaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1980
- Composition of the Capsular and Extracellular Polysaccharides of Rhizobium japonicumPlant Physiology, 1980
- A new cluster model for the FeMo-cofactor of nitrogenaseBiochemical and Biophysical Research Communications, 1979
- Nitrogenase XI: Mössbauer studies on the cofactor centers of the MoFe protein from Azotobacter vinelandii OPBiochimica et Biophysica Acta (BBA) - Protein Structure, 1979
- The molybdenum site of nitrogenase. 2. A comparative study of molybdenum-iron proteins and the iron-molybdenum cofactor by x-ray absorption spectroscopyJournal of the American Chemical Society, 1978
- Synthetic approaches to the active sites of iron-sulfur proteinsAccounts of Chemical Research, 1977
- Hindered rotation in N-methylformamide. A peptide-bond model systemBiochemical and Biophysical Research Communications, 1971
- cis and trans Configurations of the Peptide Bond in N-Monosubstituted Amides by Nuclear Magnetic ResonanceJournal of the American Chemical Society, 1964
- Influence of Cations on the Ninhydrin Reaction for the Determination of Amino-AcidsNature, 1953