The importance of quantitative Mossbauer spectroscopy of MoFe-protein from Azotobacter vinelandii
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1985.tb08679.x/fullpdf
Reference29 articles.
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5. Fully Active Fe-Protein of the Nitrogenase from Azotobacter vinelandii Contains at least Eight Iron Atoms and Eight Sulphide Atoms per Molecule
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2. NITROGENASE STRUCTURE AND FUNCTION: A Biochemical-Genetic Perspective;Annual Review of Microbiology;1995-10
3. Synthesis, structural characterization, and properties of new single and double cubanes containing the MoFe3S4 structural unit and molybdenum-bound polycarboxylate ligands. Clusters with a molybdenum-coordination environment similar to that in the iron-molybdenum cofactor of nitrogenase;Inorganic Chemistry;1995-01
4. Mössbauer characterization of the metal clusters in Azotobacter vinelandii nitrogenase VFe protein.;Journal of Biological Chemistry;1994-08
5. Mössbauer spectroscopy of metalloproteins and the use of Fourier transforms;EJB Reviews 1993;1994
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