nitrosylprotoheme has been researched along with carbon monoxide in 2 studies
*Carbon Monoxide: Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed) [MeSH]
*Carbon Monoxide: Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed) [MeSH]
Studies (nitrosylprotoheme) | Trials (nitrosylprotoheme) | Recent Studies (post-2010) (nitrosylprotoheme) | Studies (carbon monoxide) | Trials (carbon monoxide) | Recent Studies (post-2010) (carbon monoxide) |
---|---|---|---|---|---|
25 | 0 | 3 | 18,800 | 678 | 5,063 |
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 1 (50.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 1 (50.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Crane, BR; Getzoff, ED; Siegel, LM | 1 |
Bouzhir-Sima, L; Liebl, U; Lobato, L; Vos, MH; Wilson, MT; Yamashita, T | 1 |
2 other study(ies) available for nitrosylprotoheme and carbon monoxide
Article | Year |
---|---|
Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, inhibitors, intermediates, and products.
Topics: Binding Sites; Carbon Monoxide; Catalysis; Crystallography, X-Ray; Cyanides; Escherichia coli; Heme; Hemeproteins; Ligands; Nitrates; Nitrites; Oxidation-Reduction; Oxidoreductases Acting on Sulfur Group Donors; Substrate Specificity; Sulfites | 1997 |
Dynamics of the heme-binding bacterial gas-sensing dissimilative nitrate respiration regulator (DNR) and activation barriers for ligand binding and escape.
Topics: Animals; Bacterial Proteins; Binding Sites; Carbon Monoxide; Cytochromes c; DNA, Bacterial; Fluorescence Polarization; Gene Expression Regulation, Bacterial; Heme; Horses; Kinetics; Ligands; Nitric Oxide; Promoter Regions, Genetic; Protein Binding; Pseudomonas aeruginosa; Transcription Factors | 2014 |