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Literature summary for 1.17.4.1 extracted from

  • Han, W.G.; Noodleman, L.
    DFT calculations for intermediate and active states of the diiron center with a tryptophan or tyrosine radical in Escherichia coli ribonucleotide reductase (2011), Inorg. Chem., 50, 2302-2320.
    View publication on PubMedView publication on EuropePMC
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Metals/Ions

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

Organism UniProt Comment Textmining
Escherichia coli
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-
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Substrates and Products (Substrate)

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 ?
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 ?

Subunits

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

Synonyms Comment Organism
class Ia ribonucleotide reductase
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 Escherichia coli
class Ia RNR
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 Escherichia coli

Cofactor

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