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Literature summary for 1.16.1.1 extracted from
- Rapid-scan stopped-flow studies of the pH dependence of the reaction between mercuric reductase and NADPH (1986), Eur. J. Biochem., 156, 479-488.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas aeruginosa | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Hg2+ + NADPH | - |
Pseudomonas aeruginosa | Hg + NADP+ + H+ | - |
? |  |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADPH | in the presence of an excess of NADPH, the final product of the reaction is probably an NADPH complex of two-electron-reduced enzyme, but below pH 6 the final spectrum becomes less intense suggesting a partial formation of four-electron-reduced enzyme | Pseudomonas aeruginosa | |
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