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Literature summary for 4.99.1.2 extracted from
- DFT studies of the degradation mechanism of methyl mercury activated by a sulfur-rich ligand (2010), Phys. Chem. Chem. Phys., 12, 3961-3971.
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| CH3Hg+ + H+ | Escherichia coli | theoretical insights into the mechanism of Hg-C bond protonolysis in methyl mercury coordinated by the tris(2-mercapto-1-tert-butylimidazolyl)hydroborato ligand, the structural and functional analogue of the organomercurial lyase MerB, different cleavage pathways including both frontside and backside attack transition states are systematically studied by the hybrid density functional method B3LYP | CH4 + Hg2+ | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P77072 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| CH3Hg+ + H+ | theoretical insights into the mechanism of Hg-C bond protonolysis in methyl mercury coordinated by the tris(2-mercapto-1-tert-butylimidazolyl)hydroborato ligand, the structural and functional analogue of the organomercurial lyase MerB, different cleavage pathways including both frontside and backside attack transition states are systematically studied by the hybrid density functional method B3LYP | Escherichia coli | CH4 + Hg2+ | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| merB | - |
Escherichia coli |
| organomercurial lyase | - |
Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | theoretical insights into the mechanism of Hg-C bond protonolysis in methyl mercury coordinated by the tris(2-mercapto-1-tert-butylimidazolyl)hydroborato ligand, the structural and functional analogue of the organomercurial lyase MerB, different cleavage pathways including both frontside and backside attack transition states are systematically studied by the hybrid density functional method B3LYP | Escherichia coli |
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