Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | class Ia ribonucleotide reductase subunit R2 contains a diiron active site, active-site crystal structures of the Fe(II)Fe(II) and Fe(III)Fe(III) clusters, overview | Escherichia coli | |
Fe3+ | class Ia ribonucleotide reductase subunit R2 contains a diiron active site, active-site crystal structures of the Fe(II)Fe(II) and Fe(III)Fe(III) clusters, overview | Escherichia coli | |
additional information | active-site models for the intermediate X-Trp48 radical+ and X-Tyr122 radical, the active Fe(III)Fe(III)-Tyr122 radical, and the met Fe(III)Fe(III) states of Escherichia coli R2 are studied, using broken-symmetry density functional theory incorporated with the conductor-like screening solvation model, overview. Asp84 and Trp48 are most likely the main contributing residues to the result that the transient Fe(IV)Fe(IV) state is not observed in wild-type class Ia R2. Kinetic control of proton transfer to Tyr122 radical plays a critical role in preventing reduction from the active Fe(III)Fe(III)-Tyr122 radical state to the met state, which is potentially the reason why Tyr122 radical in the active state can be stable over a very long period | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | active-site structure and active-site model clusters, overview. Electron transfers and kinetic control, overview | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | subunit R1 contains the substrate binding site and catalyzes dehydroxylation of the 2'-hydroxyl group of the ribose ring. The tyrosine radical in R2 is in the neutral deprotonated form with the oxidized Fe(III)Fe(III) active site | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
class Ia ribonucleotide reductase | - |
Escherichia coli |
class Ia RNR | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | metal cofactor composition and conformation analysis, complex stabilities and geometries, calculations and modelling of enzyme geometries including cofactors and active site, detailed overview | Escherichia coli |