Double integration and titration of the electron paramagnetic resonance signal in the molybdenum-iron protein of Azotobacter vinelandii
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00308a027
Cited by 16 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Catalytic Reduction of Hydrazine to Ammonia with MoFe3S4−Polycarboxylate Clusters. Possible Relevance Regarding the Function of the Molybdenum-Coordinated Homocitrate in Nitrogenase;Inorganic Chemistry;1996-01-01
2. 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
3. EXAFS studies of FeMo-cofactor and MoFe protein: Direct evidence for the long-range Mo-Fe-Fe interaction and cyanide binding to the Mo in FeMo-cofactor;Journal of the American Chemical Society;1994-03
4. Nitrogenase-catalyzed ethane production and CO-sensitive hydrogen evolution from MoFe proteins having amino acid substitutions in an alpha-subunit FeMo cofactor-binding domain.;Journal of Biological Chemistry;1992-10
5. Synthesis and structures of the [MoFe6S6(CO)16]2-, [MoFe4S3(CO)13(PEt3)]2-, and [Mo2Fe2S2(CO)12]2- ions: high-nuclearity molybdenum-iron-sulfur clusters as potential precursors to models for the FeMo-cofactor of nitrogenase;Inorganic Chemistry;1991-05
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