Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.17.4.1 extracted from

  • Jensen, K.P.; Bell, C.B.; Clay, M.D.; Solomon, E.I.
    Peroxo-type intermediates in class I ribonucleotide reductase and related binuclear non-heme iron enzymes (2009), J. Am. Chem. Soc., 131, 12155-12171.
    View publication on PubMed
Search for more literature for 1.17.4.1

Activating Compound

Activating Compound Comment Organism Structure
additional information mechanism for the activation of peroxy intermediates in binuclear non-heme iron enzymes for reactivity Escherichia coli

Protein Variants

Protein Variants Comment Organism
D84E the mutation provides a ligand environment similar to that found in methane monooxygenase, MMO, renders this residue bidentate, and Glu204 becomes monodentate. The RNR mutant, however, remains distinct from MMO, which has a beta-1,1 type Glu-bridge, most likely due to the effects of second sphere residues Escherichia coli
W48A/Y122F the reaction remains at the level of the peroxo-intermediate, structural analysis Escherichia coli
W48F/D84E the reaction remains at the level of the peroxo-intermediate, structural analysis Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ two Fe2+ ions, each bound to one histidine and one terminal acidic residue, with Asp84 binding to Fe1 and Glu204 binding to Fe2. The di-iron binding site is involved in the catalytic reaction and enzyme activation, overview Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P69924
-
-

Reaction

Reaction Comment Organism Reaction ID
2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin reaction mechanism, two possible pathways, overview Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information peroxo-type intermediates occur in the non-heme di-iron enzyme class Ia ribonucleotide reductase. Water or a proton can bind to the di-iron site of ribonucleotide reductase and facilitate changes that affect the electronic structure of the iron sites and activate the site for further reaction. Two potential reaction pathways, spectroscopic and computational analysis, overview Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
class I ribonucleotide reductase
-
 Escherichia coli
class I RNR
-
 Escherichia coli