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Literature summary for 1.17.4.1 extracted from
- Cation mediation of radical transfer between Trp48 and Tyr356 during O2 activation by protein R2 of Escherichia coli ribonucleotide reductase: relevance to R1-R2 radical transfer in nucleotide reduction? (2006), Biochemistry, 45, 8823-8830.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Y122F | subunit R2, study on kinetics of decay of W48 cation radical | Escherichia coli |
| Y122F/Y356F | subunit R2, study on kinetics of decay of W48 cation radical | Escherichia coli |
| Y356F | subunit R2, study on kinetics of decay of W48 cation radical | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
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- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin | presence of divalent cations mediates a rapid radical-transfer equilibrium between W48 and Y356. Cation-mediated propagation of the radical from W48 to Y356 gives rise to a fast phase of Y radical production that is essentially coincident with W48 cation radical formation and creates an efficient pathway for decay of W48 cation radical | Escherichia coli |
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