histidine has been researched along with molybdenum cofactor in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (50.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 1 (25.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Boll, M; Culka, M; Huwiler, SG; Ullmann, GM | 1 |
| Asso, M; Bertrand, P; Blasco, F; Giordano, G; Guigliarelli, B; Magalon, A; Rothery, RA | 1 |
| Blasco, F; Dos Santos, JP; Frixon, C; Giordano, G; Guigliarelli, B; Magalon, A; Santini, CL | 1 |
| Leimkühler, S; Matthies, A; Nimtz, M | 1 |
4 other study(ies) available for histidine and molybdenum cofactor
| Article | Year |
|---|---|
Breaking Benzene Aromaticity-Computational Insights into the Mechanism of the Tungsten-Containing Benzoyl-CoA Reductase.
Topics: Acyl Coenzyme A; Benzene; Catalytic Domain; Electron Transport; Geobacter; Histidine; Oxidoreductases Acting on CH-CH Group Donors; Protons; Pterins; Quantum Theory; Tungsten | 2017 |
Molybdenum cofactor properties and [Fe-S] cluster coordination in Escherichia coli nitrate reductase A: investigation by site-directed mutagenesis of the conserved his-50 residue in the NarG subunit.
Topics: Cell Membrane; Coenzymes; Conserved Sequence; Electron Spin Resonance Spectroscopy; Enzyme Activation; Escherichia coli; Histidine; Iron-Sulfur Proteins; Metalloproteins; Molybdenum; Molybdenum Cofactors; Mutagenesis, Site-Directed; Nitrate Reductase; Nitrate Reductases; Protein Binding; Pteridines | 1998 |
NarJ is a specific chaperone required for molybdenum cofactor assembly in nitrate reductase A of Escherichia coli.
Topics: Cell Fractionation; Coenzymes; Electron Spin Resonance Spectroscopy; Enzyme Activation; Escherichia coli; Histidine; Metalloproteins; Molecular Chaperones; Molybdenum; Molybdenum Cofactors; Nitrate Reductase; Nitrate Reductases; Plasmids; Pteridines; Recombinant Proteins; Spectrometry, Fluorescence | 1998 |
Molybdenum cofactor biosynthesis in humans: identification of a persulfide group in the rhodanese-like domain of MOCS3 by mass spectrometry.
Topics: Amino Acid Sequence; Animals; Coenzymes; Cysteine; Disulfides; Histidine; Humans; Metalloproteins; Mice; Molecular Sequence Data; Molybdenum Cofactors; Mutagenesis, Site-Directed; Nucleotidyltransferases; Peptide Mapping; Protein Structure, Tertiary; Pteridines; Sequence Homology, Amino Acid; Spectrometry, Mass, Electrospray Ionization; Sulfhydryl Compounds; Sulfides; Sulfurtransferases; Thiosulfate Sulfurtransferase | 2005 |