methionine has been researched along with cytochromes c1 in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 3 (75.00) | 18.2507 |
| 2000's | 1 (25.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Daldal, F; Davidson, E; Gray, KA | 1 |
| Graham, LA; Phillips, JD; Trumpower, BL | 1 |
| Daldal, F; Darrouzet, E; Knaff, DB; Li, J; Mandaci, S; Qin, H | 1 |
| Daldal, F; Darrouzet, E; Dutton, PL; Moser, CC; Osyczka, A | 1 |
4 other study(ies) available for methionine and cytochromes c1
| Article | Year |
|---|---|
Mutagenesis of methionine-183 drastically affects the physicochemical properties of cytochrome c1 of the bc1 complex of Rhodobacter capsulatus.
Topics: Amino Acid Sequence; Base Sequence; Carbon Monoxide; Chemical Phenomena; Chemistry, Physical; Cytochrome b Group; Cytochromes c1; Electrophoresis, Polyacrylamide Gel; Heme; Iron; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Restriction Mapping; Rhodobacter capsulatus; Spectrophotometry | 1992 |
Subunit 9 of the Saccharomyces cerevisiae cytochrome bc1 complex is required for insertion of EPR-detectable iron-sulfur cluster into the Rieske iron-sulfur protein.
Topics: Blotting, Western; Cloning, Molecular; Cytochrome b Group; Cytochromes c1; Electron Spin Resonance Spectroscopy; Electron Transport Complex III; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Gene Deletion; Genes, Fungal; Iron; Iron-Sulfur Proteins; Kinetics; Macromolecular Substances; Methionine; Mitochondria; Oxygen Consumption; Protein Biosynthesis; Recombinant Proteins; Restriction Mapping; Saccharomyces cerevisiae; Sulfur | 1993 |
Substitution of the sixth axial ligand of Rhodobacter capsulatus cytochrome c1 heme yields novel cytochrome c1 variants with unusual properties.
Topics: Amino Acid Substitution; Binding Sites; Cytochromes c1; Electron Transport Complex III; Heme; Histidine; Ligands; Lysine; Methionine; Mutagenesis, Site-Directed; NADH Dehydrogenase; Oxidation-Reduction; Rhodobacter capsulatus; Spectrophotometry | 1999 |
Controlling the functionality of cytochrome c(1) redox potentials in the Rhodobacter capsulatus bc(1) complex through disulfide anchoring of a loop and a beta-branched amino acid near the heme-ligating methionine.
Topics: Amino Acid Sequence; Binding Sites; Cytochromes c1; Disulfides; Electron Transport; Electron Transport Complex III; Electrophoresis, Polyacrylamide Gel; Factor Xa; Heme; Methionine; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Plasmids; Protein Folding; Rhodobacter capsulatus; Sequence Homology, Amino Acid | 2001 |