arginine has been researched along with plastoquinone in 3 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 2 (66.67) | 18.2507 |
| 2000's | 1 (33.33) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Cao, JC; Vermaas, WF | 1 |
| Depka, B; Edelman, M; Jansen, MA; Trebst, A | 1 |
| Finazzi, G; Kallas, T; Middleton-Zarka, KA; Nelson, ME; Wang, QJ; Whitmarsh, J | 1 |
3 other study(ies) available for arginine and plastoquinone
| Article | Year |
|---|---|
Arginine residues in the D2 polypeptide may stabilize bicarbonate binding in photosystem II of Synechocystis sp. PCC.
Topics: Arginine; Base Sequence; Bicarbonates; Chlorophyll; Cyanobacteria; Diuron; Formates; Glutamine; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxygen; Peptides; Photolysis; Photosynthetic Reaction Center Complex Proteins; Plastoquinone; Serine | 1991 |
Engagement of specific sites in the plastoquinone niche regulates degradation of the D1 protein in photosystem II.
Topics: Animals; Arginine; Bacterial Proteins; Binding Sites; Chlamydomonas reinhardtii; Culture Techniques; Mutation; Nitrophenols; Photosynthetic Reaction Center Complex Proteins; Photosystem II Protein Complex; Plant Proteins; Plants; Plastoquinone; Trypsin; Ultraviolet Rays | 1993 |
Cytochrome b6 arginine 214 of Synechococcus sp. PCC 7002, a key residue for quinone-reductase site function and turnover of the cytochrome bf complex.
Topics: Alleles; Animals; Arginine; Binding Sites; Chlamydomonas; Cyanobacteria; Cytochrome b6f Complex; Cytochromes b6; Electrochemistry; Electrons; Heme; Hydrogen; Kinetics; Models, Biological; Models, Genetic; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Oxygen; Phenotype; Plasmids; Plastoquinone; Polymerase Chain Reaction; Protein Structure, Tertiary; Quinones; Spectrophotometry; Synechococcus; Time Factors | 2005 |