Electrochemical characterization of the iron-molybdenum cofactor from Azotobacter vinelandii nitrogenase
- 1 September 1985
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 107 (19) , 5364-5368
- https://doi.org/10.1021/ja00305a007
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- The Effect of the Redox Potential on the Activity of the Nitrogenase and on the Fe-Protein of Azotobacter vinelandiEuropean Journal of Biochemistry, 1982
- Redox and spectroscopic properties of oxidized MoFe protein from Azotobacter vinelandiiBiochemistry, 1980
- Large-scale purification of high activity Azotobacter vinelandii nitrogenaseBiochimica et Biophysica Acta (BBA) - Enzymology, 1980
- Synthesis and electronic and redox properties of "double-cubane" cluster complexes containing molybdenum iron sulfide (MoFe3S4) and tungsten iron sulfide (WFe3S4) coresJournal of the American Chemical Society, 1980
- Oxidation-reduction properties and complexation reactions of the iron-molybdenum cofactor of nitrogenase.Journal of Biological Chemistry, 1980
- Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase.Proceedings of the National Academy of Sciences, 1979
- Nitrogenase X: Mössbauer and EPR studies on reversibly oxidized MoFe protein from Azotobacter vinelandii OP Nature of the iron centersBiochimica et Biophysica Acta (BBA) - Protein Structure, 1978
- Electron-paramagnetic-resonance studies on the redox properties of the molybdenum-iron protein of nitrogenase between +50 and −450 mVBiochemical Journal, 1978
- Novel metal cluster in the iron-molybdenum cofactor of nitrogenase. Spectroscopic evidenceJournal of Biological Chemistry, 1978
- Synthetic analogs of the active sites of iron-sulfur proteins. 15. Comparative polarographic potentials of the [Fe4S4(SR)4]2-,3- and Clostridium pasteurianum ferredoxin redox couplesJournal of the American Chemical Society, 1977