Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,6-diaminopurineriboside diphosphate + reduced thioredoxin
2'-deoxy-2,6-diaminopurineriboside diphosphate + H2O
-
-
-
?
2-aminopurineriboside diphosphate + reduced thioredoxin
2'-deoxy-2-aminopurineriboside diphosphate + H2O
-
-
-
?
8-vinyl-ADP + reduced thioredoxin
8-vinyl-2'-deoxy-ADP + thioredoxin disulfide + H2O
-
-
-
-
?
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
benzimidazoleriboside diphosphate + reduced thioredoxin
2'-deoxybenzimidazolriboside diphosphate + H2O
-
-
-
?
CDP + reduced thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
CTP + reduced thioredoxin
2'-dCTP + thioredoxin disulfide + H2O
-
-
-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
class I RNRs
-
-
?
nucleoside 5'-diphosphate + NrdH-redoxin
2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
only class Ib RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class I and class II RNRs
-
-
?
purineriboside diphosphate + reduced thioredoxin
2'-deoxypurineriboside diphosphate + H2O
-
-
-
?
ribonucleoside 5'-diphosphate + thioredoxin
2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
ribonucleoside diphosphate + reduced glutaredoxin
2'-deoxyribonucleoside diphosphate + oxidized glutaredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
tubercidin diphosphate + reduced thioredoxin
2'-deoxytubercidin diphosphate + oxidized thioredoxin + H2O
-
14% of GDP reduction rate
-
?
UDP + reduced thioredoxin
2'-deoxy-UDP + oxidized thioredoxin + H2O
-
-
-
-
?
UDP + thioredoxin
2'-dUDP + thioredoxin disulfide + H2O
additional information
?
-
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
-
-
-
?
ADP + thioredoxin
2'-dADP + thioredoxin disulfide + H2O
the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair
-
-
?
CDP + reduced thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + reduced thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
-
kinetics of hydrogen atom abstraction from substrate by an active site thiyl radical in ribonucleotide reductase
-
-
?
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
-
-
-
?
CDP + thioredoxin
2'-deoxyCDP + thioredoxin disulfide + H2O
-
coupled assay method with NADPH, transient spectrometric measurement of Y356 radical intermediate, Y356 radical initiation is prompted by excitation of a proximal anthraquinone or benzophenone chromophore on a 20-mer peptide Y-R2C19, bound to subunit alpha2, both the Anq and BPA-containing peptides are competent in deoxycytidine diphosphate formation and turnover occurs via Y731 to Y730 to C439 pathway-dependent radical transport in R1, overview. Peptide Y-R2C19 is identical to the C-terminal peptide tail of the R2 subunit and is a known competitive inhibitor of binding of the native R2 protein to R1
-
-
?
ribonucleoside 5'-diphosphate + thioredoxin
2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
-
-
-
?
ribonucleoside 5'-diphosphate + thioredoxin
2'-deoxyribonuleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
at the completion of each turnover cycle, the active site of R1 becomes oxidized and subsequently regenerates by a cysteine pair at its C-terminal domain R1-CTD, that acts in trans to reduce the active site of its neighboring monomer, R1-CTD interacts with the N-terminal domain of R1, R1-NTD, which involves a conserved two-residue sequence motif in the R1-NTD, overview
-
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
UDP + thioredoxin
2'-dUDP + thioredoxin disulfide + H2O
-
-
-
?
UDP + thioredoxin
2'-dUDP + thioredoxin disulfide + H2O
the enzyme converts ribonucleotides to deoxyribonucleotides, a reaction that is essential for DNA biosynthesis and repair
-
-
?
additional information
?
-
-
each catalytic turnover by aerobic ribonucleotide reductase requires the assembly of the two proteins, R1 (alpha2) and R2 (beta2), to produce deoxyribonucleotides for DNA synthesis
-
-
?
additional information
?
-
-
the Sml1-R1 interaction causes SML1-dependent lethality, the CX2C motif of Rnr1 Is essential for viability. overview
-
-
?
additional information
?
-
-
mechanism of radical transport in the R1 subunit of the class I enzyme, overview
-
-
?
additional information
?
-
ribonucleotide reductases catalyze the reduction of ribonucleotides to deoxyribonucleotides for DNA synthesis
-
-
?
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
-
-
?
additional information
?
-
-
ribonucleotide reductase catalyzes the reduction of ribonucleotides to deoxyribonucleotides. Electron transfer to and from the tyrosyl radical, at Y122, in RNR is coupled to a conformational change in the beta2 subunit, vibrational spectroscopy analysis, overview
-
-
?
additional information
?
-
the RNR reaction involves replacement by hydrogen of the hydroxyl group on the 2'-carbon of the nucleoside diphosphate substrate. This chemically difficult replacement occurs by a free-radical mechanism. The enzyme employs a heterobinuclear MnIV/FeIII cluster for radical initiation. In essence, the MnIV ion of the cluster functionally replaces the Y radical of the conventional class I RNR. The Ct beta2 protein also autoactivates by reaction of its reduced MnII/FeII metal cluster with O2. In this reaction, an unprecedented MnIV/FeIV intermediate accumulates almost stoichiometrically and decays by one-electron reduction of the FeIV site. This reduction is mediated by the near-surface residue, Y222, overview
-
-
?
additional information
?
-
-
class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the conversion of nucleoside 5'-diphosphates, NDPs, to deoxynucleotides, dNDPs. The active site for NDP reduction resides in the alpha2 subunit, and the essential diferric-tyrosyl radical, Y122 radical, cofactor that initiates transfer of the radical to the active site cysteine in R2 (C439), 35A Ā° removed, is located in subunit beta2. The oxidation involves a hopping mechanism through aromatic amino acids, Y122, W48, and Y356 in subunit beta2 to Y731, Y730, and C439 in subunit alpha2, and a reversible proton-coupled electron transfer
-
-
?
additional information
?
-
-
active-site structure and active-site model clusters, overview. Electron transfers and kinetic control, overview
-
-
?
additional information
?
-
-
in the class I RNRs, a tyrosine radical is generated in the beta2 subunit, a di-ironoxo enzyme. In class II a tyrosine radical is generated directly on alpha or alpha2 by cleavage of adenosylcobalamin. In both cases, the radical is channeled to a cysteine in the active site of the alpha subunit to initiate catalysis
-
-
?
additional information
?
-
-
substrate is CDP with ATP as effector, detection of NH2Y radical intermediates capable of dNDP formation
-
-
?
additional information
?
-
-
the class I RNR active-site disulfide bridge between Cys225 and Cys462 must be reduced for a complete turnover. The electron required for this reduction is provided by a redox network, which involves a cysteine pair at the C-terminus of the R1 subunit, the thioredoxin or glutaredoxin system, and NADPH. For in vitro experiments, the disulfide bridge can be reduced by small thiol compounds such as DTT
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Co2+
-
class II enzymes contain cobalamin as cofactor
Fe
-
class I enzymes contain diferric(III)-tyrosyl radical cofactor
Manganese
-
construction of heterobinuclear Mn(II)Fe(II) and Mn(III)Fe(III) clusters within a single beta-protomer of the small subunit of Escherichia coli ribonucleotide reductase due to differential binding affinity of the A- and B-sites
Mn2+
class Ib ribonucleotide reductase can initiate reduction of nucleotides to deoxynucleotides with either a MnIII 2-tyrosyl radical or a FeIII 2-tyrosyl radical cofactor in the NrdF subunit. Whereas FeIII 2-tyrosyl radical can self-assemble from FeII 2-NrdF and O2, activation of MnII 2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2. Structures of MnII 2-NrdF in complex with reduced and oxidized NrdI: a continuous channel connects the NrdI flavin cofactor to the NrdF MnII 2 active site.
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
Fe2+
each beta-protomer of the small betabeta subunit (R2) contains a binuclear iron cluster with inequivalent binding sites: FeA and FeB. The majority of the protein binds only one Fe(II)atom per betabeta subunit. Additional iron occupation can be achieved upon exposure to O2 or in high glycerol buffers. The binding of the first Fe(II) atom to the active site in a beta-protomer (beta1) induces a global protein conformational change that inhibits access of metal to the active site in the other beta-protomer (betaII). The binding of the same Fe(II) atom also induces a local effect at the active site in beta1-protomer, which lowers the affinity for metal in the A-site
Fe2+
assembly, maintenance, and role in catalysis of the Fe2 III/III-Y radical cofactor of Ecbeta2 subunit, structure modelling, detailed overview
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
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
Fe2+
class Ib ribonucleotide reductase can initiate reduction of nucleotides to deoxynucleotides with either a MnIII 2-tyrosyl radical or a FeIII 2-tyrosyl radical cofactor in the NrdF subunit. Whereas FeIII 2-tyrosyl radical can self-assemble from FeII 2-NrdF and O2, activation of MnII 2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2
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
Fe3+
-
diferric(III)-tyrosyl radical cofactor
Iron
-
-
Iron
-
Raman spectroscopy of B2 subunit shows Fe-O vibration of an oxygen-coordinated ligand
Iron
-
iron center stabilizes tyrosyl radical, distance between the iron center and the tyrosyl radical is estimated to be 6-9.0 A
Iron
-
B2 subunit contains 2 nonidentical high spin Fe3+ ions in an antiferromagnetically coupled binuclear complex that resembles both methydroxohemerythrin and oxyhemerythrin
Iron
-
2 separate iron centers in subunit B2, 1 center on each beta subunit, distance between iron centers: 25 A, distance between Fe-Fe atoms: 3.3 A
Iron
proposed in vitro mechanism for the assembly of the diferric tyrosyl radical cofactor of subunit R2
Iron
-
oxo- or carboxylate-bridge between the antiferromagnetically coupled pair of high spin Fe3+, possibly with a binding oxo-group
Iron
-
X-ray absorption fine structure, EXAFS, of iron-containing subunit, Fe-Fe distance in subunit B2 is in the 3.26-3.48 A range
Iron
-
iron binds directly to the enzyme structure and not via sulfur
Iron
-
iron center is composed of 2 high spin iron atoms antiferromagnetically coupled through a micro-oxo bridge
Iron
-
subunit B2 contains iron, nonheme-like porphyrin complexes
Iron
-
B2 subunit contains 2 dinuclear Fe3+ centers
Iron
-
construction of heterobinuclear Mn(II)Fe(II) and Mn(III)Fe(III) clusters within a single beta-protomer of the small subunit of Escherichia coli ribonucleotide reductase due to differential binding affinity of the A- and B-sites. The binding of the first metal is under kinetic control. The binding of the first Fe(II) atom to the active site in a beta-protomer induces a global protein conformational change that inhibits access of metal to the active site in the other protomer and also induces a local effect at the active site in the first protomer, which lowers the affinity for metal in the A-site
Iron
-
subunit R2 dimer has two equivalent dinuclear iron centers. Iron atoms have both histidine and carboxyl acid ligands and are bridged by the carboxylate group of E115
Mg2+
-
-
Mg2+
-
subunit B1 requires Mg2+ ions in the 10 mM concentration range for activity
Mn3+
-
dimanganese(III)-tyrosyl radical cofactor
Mn3+
-
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Kjoller Larsen, I.; Sjöberg, B.M.; Thelander, L.
Characterization of the active site of ribonucleotide reductase of Escherichia coli, bacteriophage T4 and mammalian cells by inhibition studies with hydroxyurea analogues
Eur. J. Biochem.
125
75-81
1982
Tequatrovirus T4, Bos taurus, Escherichia coli, Mus musculus
brenda
Thelander, L.; Sjöberg, B.M.; Eriksson, S.
Ribonucleoside diphosphate reductase (Escherichia coli)
Methods Enzymol.
51
227-237
1978
Escherichia coli, Escherichia coli overproducing
brenda
Lammers, M.; Follmann, H.
The ribonucleotide reductases - a unique group of metalloenzymes essential for cell proliferation
Struct. Bonding
54
27-91
1983
Tequatrovirus T4, Tequintavirus T5, Enterobacteria phage T6, Bos taurus, Saccharomyces cerevisiae, Oryctolagus cuniculus, Escherichia coli, Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus, Tetradesmus obliquus
-
brenda
Joelson, T.; Uhlin, U.; Eklund, H.; Sjöberg, B.M.; Hahne, S.; Karlsson, M.
Crystallization and preliminary crystallographic data of ribonucleotide reductase protein B2 from Escherichia coli
J. Biol. Chem.
259
9076-9077
1984
Escherichia coli
brenda
Salowe, S.P.; Stubbe, J.
Cloning, overproduction, and purification of the B2 subunit of ribonucleoside-diphosphate reductase
J. Bacteriol.
165
363-366
1986
Escherichia coli
brenda
Sahlin, M.; Sjöberg, B.M.; Backes, G.; Loehr, T.; Sanders-Loehr, J.
Activation of the iron-containing B2 protein of ribonucleotide reductase by hydrogen peroxide
Biochem. Biophys. Res. Commun.
167
813-818
1990
Escherichia coli
brenda
Smith, S.L.; Douglas, K.T.
Stereoselective, strong inhibition of ribonucleotide reductase from E. coli by cisplatin
Biochem. Biophys. Res. Commun.
162
715-723
1989
Escherichia coli
brenda
Stubbe, J.
Ribonucleotide reductases
Adv. Enzymol. Relat. Areas Mol. Biol.
63
349-419
1990
Escherichia coli, Herpes simplex virus, Mus musculus
brenda
Holmgren, A.
Regulation of ribonucleotide reductase
Curr. Top. Cell. Regul.
19
47-76
1981
Escherichia phage T2, Tequatrovirus T4, Tequintavirus T5, Enterobacteria phage T6, Bos taurus, Oryctolagus cuniculus, Escherichia coli, Homo sapiens, Rattus norvegicus
brenda
Stubbe, J.
Ribonucleotide reductases: amazing and confusing
J. Biol. Chem.
265
5329-5332
1990
Escherichia coli
brenda
Larsson, A.; Reichard, P.
Enzymatic synthesis of deoxyribonucleotides. IX. Allosteric effects in the reduction of pyrimidine ribonucleotides by the ribonucleoside diphosphate reductase system of Escherichia coli
J. Biol. Chem.
241
2533-2539
1966
Escherichia coli
brenda
Thelander, L.
Physicochemical characterization of ribonucleoside diphosphate reductase from Escherichia coli
J. Biol. Chem.
248
4591-4601
1973
Escherichia coli
brenda
Nordlund, P.; Sjöberg, B.M.; Eklund, H.
Three-dimensional structure of the free radical protein of ribonucleotide reductase
Nature
345
593-598
1990
Escherichia coli
brenda
Nordlund, P.; Uhlin, U.; Westergren, C.; Joelsen, T.; Sjöberg, B.M.; Eklund, H.
New crystal forms of the small subunit of ribonucleotide reductase from Escherichia coli
FEBS Lett.
258
251-254
1989
Escherichia coli
brenda
Ribi, H.O.; Reichard, P.; Kornberg, R.D.
Two-dimensional crystals of enzyme-effector complexes: ribonucleotide reductase at 18-A resolution
Biochemistry
26
7974-7979
1987
Escherichia coli
brenda
Bunker, G.; Petersson, L.; Sjöberg, B.M.; Sahlin, M.; Chance, M.; Chance, B.; Ehrenberg, A.
Extended X-ray absorption fine structure studies on the iron-containing subunit of ribonucleotide reductase from Escherichia coli
Biochemistry
26
4708-4716
1987
Escherichia coli
brenda
Reichard, P.; Ehrenberg, A.
Ribonucleotide reductase - a radical enzyme
Science
221
514-519
1983
Escherichia coli
brenda
Stubbe, J.; Ator, M.; Krenitsky, T.
Mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Evidence for 3-C-H bond cleavage
J. Biol. Chem.
258
1625-1630
1983
Escherichia coli
brenda
Atkin, C.L.; Thelander, L.; Reichard, P.; Lang, G.
Iron and free radical in ribonucleotide reductase. Exchange of iron and Mossbauer spectroscopy of the protein B2 subunit of the Escherichia coli enzyme
J. Biol. Chem.
248
7464-7472
1973
Escherichia coli
brenda
Sjöberg, B.M.; Gräslund, A.; Loehr, J.S.; Loehr, T.M.
Ribonucleotide reductase: a structural study of the dimeric iron site
Biochem. Biophys. Res. Commun.
94
793-799
1980
Escherichia coli
brenda
Petersson, L.; Gräslund, A.; Ehrenberg, A.; Sjöberg, B.M.; Reichard, P.
The iron center in ribonucleotide reductase from Escherichia coli
J. Biol. Chem.
255
6706-6712
1980
Escherichia coli
brenda
Engström, Y.; Eriksson, S.; Thelander, L.; Akerman, M.
Ribonucleotide reductase from calf thymus. Purification and properties
Biochemistry
18
2941-2948
1979
Bos taurus, Escherichia coli
brenda
Jordan, A.; Pontis, E.; Atta, M.; Krook, M.; Gibert, I.; Barbe, J.; Reichard, P.
A second class I ribonucleotide reductase in Enterobacteriaceae: characterization of the Salmonella typhimurium enzyme
Proc. Natl. Acad. Sci. USA
91
12892-12896
1994
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Tong, W.; Burdi, D.; Riggs-Gelasco, P.; Chen, S.; Edmondson, D.; Huynh, V.; Stubbe, J.; Han, S.; Arvai, A.; Tainer, J.
Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography
Biochemistry
37
5840-5848
1998
Escherichia coli (P69924)
brenda
Hamann, C.S.; Lentainge, S.; Li, L.S.; Salem, J.S.; Yang, F.D.; Cooperman, B.S.
Chimeric small subunit inhibitors of mammalian ribonucleotide reductase: a dual function for the R2 C-terminus?
Protein Eng.
11
219-224
1998
Escherichia coli, Mus musculus
brenda
Kolberg, M.; Logan, D.T.; Bleifuss, G.; Potsch, S.; Sjoberg, B.M.; Graslund, A.; Lubitz, W.; Lassmann, G.; Lendzian, F.
A new tyrosyl radical on Phe208 as ligand to the diiron center in Escherichia coli ribonucleotide reductase, mutant R2-Y122H. Combined X-ray diffraction and EPR/ENDOR studies
J. Biol. Chem.
280
11233-11246
2005
Escherichia coli (P69924), Escherichia coli
brenda
Birgander, P.L.; Bug, S.; Kasrayan, A.; Dahlroth, S.L.; Westman, M.; Gordon, E.; Sjoberg, B.M.
Nucleotide-dependent formation of catalytically competent dimers from engineered monomeric ribonucleotide reductase protein R1
J. Biol. Chem.
280
14997-15003
2005
Escherichia coli
brenda
Lang, P.; Gerez, C.; Tritsch, D.; Fontecave, M.; Biellmann, J.F.; Burger, A.
Synthesis of 8-vinyladenosine 5'-di- and 5'-triphosphate: evaluation of the diphosphate compound on ribonucleotide reductase
Tetrahedron
59
7315-7322
2003
Escherichia coli
-
brenda
Saleh, L.; Bollinger, J.M.
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?
Biochemistry
45
8823-8830
2006
Escherichia coli
brenda
Cerqueira, N.M.; Fernandes, P.A.; Eriksson, L.A.; Ramos, M.J.
Dehydration of ribonucleotides catalyzed by ribonucleotide reductase: the role of the enzyme
Biophys. J.
90
2109-2119
2006
Escherichia coli
brenda
Pierce, B.S.; Hendrich, M.P.
Local and global effects of metal binding within the small subunit of ribonucleotide reductase
J. Am. Chem. Soc.
127
3613-3623
2005
Escherichia coli
brenda
Seyedsayamdost, M.R.; Stubbe, J.
Site-specific replacement of Y356 with 3,4-dihydroxyphenylalanine in the beta2 subunit of E. coli ribonucleotide reductase
J. Am. Chem. Soc.
128
2522-2523
2006
Escherichia coli
brenda
Nordlund, P.; Eklund, H.
Structure and function of the Escherichia coli ribonucleotide reductase protein R2
J. Mol. Biol.
232
123-164
1993
Escherichia coli
brenda
Zhang, Z.; Yang, K.; Chen, C.C.; Feser, J.; Huang, M.
Role of the C terminus of the ribonucleotide reductase large subunit in enzyme regeneration and its inhibition by Sml1
Proc. Natl. Acad. Sci. USA
104
2217-2222
2007
Saccharomyces cerevisiae, Escherichia coli
brenda
Cerqueira, N.M.; Fernandes, P.A.; Ramos, M.J.
Ribonucleotide reductase: a critical enzyme for cancer chemotherapy and antiviral agents
Recent Pat. Anticancer Drug Discov.
2
11-29
2007
Escherichia coli
brenda
Reece, S.Y.; Seyedsayamdost, M.R.; Stubbe, J.; Nocera, D.G.
Photoactive peptides for light-initiated tyrosyl radical generation and transport into ribonucleotide reductase
J. Am. Chem. Soc.
129
8500-8509
2007
Escherichia coli
brenda
Jiang, W.; Yun, D.; Saleh, L.; Bollinger, J.M.; Krebs, C.
Formation and function of the manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase
Biochemistry
47
13736-13744
2008
Chlamydia trachomatis (O84835), Chlamydia trachomatis, Escherichia coli (P69924)
brenda
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
J. Am. Chem. Soc.
131
12155-12171
2009
Escherichia coli (P69924)
brenda
Offenbacher, A.R.; Vassiliev, I.R.; Seyedsayamdost, M.R.; Stubbe, J.; Barry, B.A.
Redox-linked structural changes in ribonucleotide reductase
J. Am. Chem. Soc.
131
7496-7497
2009
Escherichia coli
brenda
Cotruvo, J.A.; Stubbe, J.
An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase
Biochemistry
49
1297-1309
2010
Escherichia coli
brenda
Seyedsayamdost, M.R.; Yee, C.S.; Stubbe, J.
Use of 2,3,5-F(3)Y-beta2 and 3-NH(2)Y-alpha2 to study proton-coupled electron transfer in Escherichia coli ribonucleotide reductase
Biochemistry
50
1403-1411
2011
Escherichia coli
brenda
Cotruvo, J.A.; Stubbe, J.
Escherichia coli class Ib ribonucleotide reductase contains a dimanganese(III)-tyrosyl radical cofactor in vivo
Biochemistry
50
1672-1681
2011
Escherichia coli, Escherichia coli GR536
brenda
Sanchez-Romero, M.A.; Molina, F.; Jimenez-Sanchez, A.
Correlation between ribonucleoside-diphosphate reductase and three replication proteins in Escherichia coli
BMC Mol. Biol.
11
11
2010
Escherichia coli
brenda
Holmgren, A.; Sengupta, R.
The use of thiols by ribonucleotide reductase
Free Radic. Biol. Med.
49
1617-1628
2010
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Lactobacillus leichmannii, Mus musculus
brenda
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
Inorg. Chem.
50
2302-2320
2011
Escherichia coli
brenda
Sanchez-Romero, M.A.; Molina, F.; Jimenez-Sanchez, A.
Organization of ribonucleoside-diphosphate reductase during multifork chromosome replication in Escherichia coli
Microbiology
157
2220-2225
2011
Escherichia coli, Escherichia coli K-12 CM735
brenda
Logan, D.
Closing the circle on ribonucleotide reductases
Nat. Struct. Mol. Biol.
18
251-253
2011
Escherichia coli, Pseudomonas aeruginosa, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Boal, A.; Cotruvo Jr., J.; Stubbe, J.; Rosenzweig, A.
Structural basis for activation of class Ib ribonucleotide reductase
Science
329
1526-1530
2010
Escherichia coli (P37146)
brenda
Martin, J.E.; Imlay, J.A.
The alternative aerobic ribonucleotide reductase of Escherichia coli, NrdEF, is a manganese-dependent enzyme that enables cell replication during periods of iron starvation
Mol. Microbiol.
80
319-334
2011
Escherichia coli (P39452)
brenda
Ando, N.; Brignole, E.J.; Zimanyi, C.M.; Funk, M.A.; Yokoyama, K.; Asturias, F.J.; Stubbe, J.; Drennan, C.L.
Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase
Proc. Natl. Acad. Sci. USA
108
21046-21051
2011
Escherichia coli (P00452)
brenda
Zimanyi, C.M.; Chen, P.Y.; Kang, G.; Funk, M.A.; Drennan, C.L.
Molecular basis for allosteric specificity regulation in class Ia ribonucleotide reductase from Escherichia coli
eLife
5
e07141
2016
Escherichia coli (P00452 and P69924), Escherichia coli
brenda
Olshansky, L.; Pizano, A.A.; Wei, Y.; Stubbe, J.; Nocera, D.G.
Kinetics of hydrogen atom abstraction from substrate by an active site thiyl radical in ribonucleotide reductase
J. Am. Chem. Soc.
136
16210-16216
2014
Escherichia coli
brenda
Zhu, M.; Dai, X.; Guo, W.; Ge, Z.; Yang, M.; Wang, H.; Wang, Y.P.
Manipulating the bacterial cell cycle and cell size by titrating the expression of ribonucleotide reductase
mBio
8
e01741-17
2017
Escherichia coli (P00452 and P69924)
brenda