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Ca2+
-
activity depends on Ca2+
Fe
-
class I enzymes contain diferric(III)-tyrosyl radical cofactor
Mn(IV)
-
MnIV/FeIII cofactor
Co2+
-
class II enzymes contain cobalamin as cofactor
Co2+
-
class II enzymes contain cobalamin as cofactor
Co2+
-
class II enzymes contain cobalamin as cofactor
Fe2+
-
classIb RNR biferrous site structure, the spectroscopically defined active site contains a 4-coordinate and a 5-coordinate Fe(II), weakly antiferromagnetically coupled via mu-1,3-carboxylate bridges, detailed spectral analysis, overview
Fe2+
-
the isolated recombinant NrdF contains a diferric-tyrosyl radical [Fe(III)2-Y.] cofactor
Fe2+
-
the manganese- and iron content of the R2 subunit decides about the enzyme activity, determination of metal contents, overview
Fe2+
-
metal content determination of oxidized and reduced subunit R2, electronic features and nuclear geometry of the manganese and iron sites, kinetics, overview. The R2 protein of class I RNR contains a Mn-Fe instead of the standard Fe-Fe cofactor. Ct R2 has a redox-inert phenylalanine replacing the radical-forming tyrosine of classic RNRs, which implies a different mechanism of O2 activation, overview. Structure modelling
Fe2+
unusual cofactor instead of Fe-Fe cofactor in other RNRs. Assembly, maintenance, and role in catalysis of the MnIV/FeIII cofactor of Ctbeta2 subunit, structure modelling, detailed overview
Fe2+
-
the enzyme contains only 0.06 mol iron per mol of R2F subunit
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
Fe2+
-
monomers A and B exhibit mono- and binuclear iron occupancy, the active site iron coordination environment, involving E131, H134, D100, E194, E228, and H231, is different between monomers A and B, binding structure, overview. Mobility and accessibility of the radical iron center, and radical transfer pathway, overview
Fe3+
-
MnIV/FeIII cofactor
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
Fe3+
-
class I enzymes contain diferric(III)-tyrosyl radical cofactor
Fe3+
-
class I enzymes contain diferric(III)-tyrosyl radical cofactor
Fe3+
-
class I enzymes contain diferric(III)-tyrosyl radical cofactor
Fe3+
-
class I enzymes contain diferric(III)-tyrosyl radical cofactor
Fe3+
the dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor is 3.5fold more active than the iron form
Iron
-
no stimulation by iron ions
Iron
-
may substitute or manganese
Iron
-
nonheme iron is an essential component of the enzyme
Iron
-
initiator of catalysis is the paramagnetic Fe(III)Fe(IV) state of the iron cluster. Proposition of reaction scheme of the iron site
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
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
Iron
-
2 iron atoms and a tyrosyl radical per 88000 Da subunit
Iron
an active diiron-tyrosyl radical cofactor is present in the the R2F-1 small subunit
Iron
-
iron is bound tightly to the protein. Enzyme activity is the same in presence and absence of EDTA
Iron
-
120000 Da L2 subunit of regenerating liver contains iron
Iron
-
1.8 mol of iron per mol of R2F subunit, dinuclear iron center
Iron
Tequatrovirus T4
-
-
Iron
Tequatrovirus T4
-
2.3 atoms of nonheme iron per molecule
Iron
-
no stimulation by iron ions
Manganese
-
dimanganic-tyrosyl radical cofactor
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
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
Mg2+
-
class Ib ribonucleotide reductase is a dimanganese(III)-tyrosyl radical enzyme, with Tyr115. Subunit beta, NrdF, contains the metallo-cofactor, essential for the initiation of the reduction process
Mg2+
-
thymus enzyme: about 50% activity in absence of added Mg2+, optimal Mg2+ concentration varies with concentration of nucleotide effector
Mg2+
-
stimulates CDP but not ADP reduction
Mg2+
-
subunit B1 requires Mg2+ ions in the 10 mM concentration range for activity
Mg2+
-
absolutely required
Mg2+
-
activity depends on Mg2+
Mg2+
Tequatrovirus T4
-
-
Mg2+
Tequatrovirus T4
-
5-10 mM, 2-3fold stimulation, not required for enzyme activity
Mn2+
-
the manganese- and iron content of the R2 subunit decides about the enzyme activity, determination of metal contents, overview
Mn2+
-
metal content determination of oxidized and reduced subunit R2, electronic features and nuclear geometry of the manganese and iron sites, kinetics, overview. The R2 protein of class I RNR contains a Mn-Fe instead of the standard Fe-Fe cofactor. Ct R2 has a redox-inert phenylalanine replacing the radical-forming tyrosine of classic RNRs, which implies a different mechanism of O2 activation, overview. Structure modelling
Mn2+
unusual cofactor instead of Fe-Fe cofactor in other RNRs. Assembly, maintenance, and role in catalysis of the MnIV/FeIII cofactor of Ctbeta2 subunit, structure modelling, detailed overview
Mn2+
EPR-silent Mn bound to the polypeptide chain, approx. 0.5 mol manganese ions/mol of R2F polypeptide
Mn2+
-
R2F is a mangagnese-containing enzyme
Mn2+
-
0.8 mol manganese per mol of R2F subunit, oragnized in a coupled binuclear centre with paramagnetic ground state or in a weakly coupled binuclear centre with therminally populated paramagnetic excites state which appears as binuclear Mn2+, overview
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.
Mn3+
-
dimanganese(III)-tyrosyl radical cofactor
Mn3+
-
the MnIII2-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
Mn3+
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo
additional information
-
no stimulation by Mg2+ or Fe2+/Fe3+
additional information
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salt-dependence of calf thymus enzyme: optimal activity in 40 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid buffer, pH 7.6, in the presence of 80-120 mM KCl, precipitation in lower salt concentration, inhibition in higher salt concentration
additional information
-
Mg2+ is not required for activity in vitro
additional information
-
enzyme redox states, overview
additional information
-
R2F does not contain the metals Fe, Co, Ni and Cu
additional information
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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
additional information
Herpes simplex virus
-
Mg2+ is not required for activity in vitro
additional information
-
Glu64 is found in the viral protein in the position that is usually occupied by a metal-coordinating aspartate in other R2s
additional information
-
-
additional information
-
the essential metallo-cofactor is a micro-oxo-micro-carboxylato-diiron cluster adjacent to a stable tyrosyl radical
additional information
-
model of enzyme regulation by nucleoside 5'-triphosphates
additional information
-
Mg2+ is not required for activity in vitro
additional information
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Mg2+ is not required for activity in vitro
additional information
-
Mg2+ is not required for activity in vitro
additional information
-
no stimulation by Mg2+ or Fe2+/Fe3+