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Literature summary for 1.17.4.1 extracted from

  • Jiang, W.; Saleh, L.; Barr, E.W.; Xie, J.; Gardner, M.M.; Krebs, C.; Bollinger, J.M.
    Branched activation- and catalysis-specific pathways for electron relay to the manganese/iron cofactor in ribonucleotide reductase from Chlamydia trachomatis (2008), Biochemistry, 47, 8477-8484.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
O2 activates the MnIV/FeIII cofactor, overview Chlamydia trachomatis

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of wild-type and mutant R2 subunits in Escherichia coli strain BL21(DE3) Chlamydia trachomatis

Protein Variants

Protein Variants Comment Organism
W51F site-directed mutagenesis, the decay of the Mn(IV)/Fe(IV) intermediate is slightly affected Chlamydia trachomatis
Y222F the substitution by site-directed mutagenesis retards the intrinsic decay of the Mn(IV)/Fe(IV) intermediate by about 10fold and diminishes the ability of ascorbate to accelerate the decay by about 65fold but has no detectable effect on the catalytic activity of the Mn(IV)/Fe(III)-R2 product Chlamydia trachomatis
Y338F site-directed mutagenesis, substitution of Y338, the cognate of the subunit interfacial R2 residue in the R1 S R2 PCET pathway of the conventional class I RNRs, has almost no effect on decay of the Mn(IV)/Fe(IV) intermediate but abolishes catalytic activity Chlamydia trachomatis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the class Ic RNR from Chlamydia trachomatis uses a Mn(IV)/Fe(III) cofactor, with high specificity for Mn(IV) in place of the Y• for radical initiation, R2 is activated when its MnII/FeII form reacts with O2 to generate a MnIV/FeIV intermediate, which decays by reduction of the FeIV site to the active Mn(IV)/Fe(III) state, the reduction step in this sequence is mediated by residue Y222, overview Chlamydia trachomatis
Manganese the class Ic RNR from Chlamydia trachomatis uses a Mn(IV)/Fe(III) cofactor, with high specificity for Mn(IV) in place of the Y• for radical initiation, R2 is activated when its MnII/FeII form reacts with O2 to generate a MnIV/FeIV intermediate, which decays by reduction of the FeIV site to the active Mn(IV)/Fe(III) state, the reduction step in this sequence is mediated by residue Y222, overview Chlamydia trachomatis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CDP + thioredoxin Chlamydia trachomatis
-
2'-deoxyCDP + thioredoxin disulfide + H2O
-
?

Organism

Organism UniProt Comment Textmining
Chlamydia trachomatis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CDP + thioredoxin
-
Chlamydia trachomatis 2'-deoxyCDP + thioredoxin disulfide + H2O
-
?

Synonyms

Synonyms Comment Organism
RNR
-
Chlamydia trachomatis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Chlamydia trachomatis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
assay at Chlamydia trachomatis

Cofactor

Cofactor Comment Organism Structure
manganese-iron cofactor the class Ic RNR from Chlamydia trachomatis uses a MnIV/FeIII cofactor, with high specificity for MnIV in place of the tyrosyl radical for radical initiation, R2 is activated when its MnII/FeII form reacts with O2 to generate a MnIV/FeIV intermediate, which decays by reduction of the FeIV site to the active MnIV/FeIII state, the reduction step in this sequence is mediated by residue Y222, overview Chlamydia trachomatis
thioredoxin
-
Chlamydia trachomatis