Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity.
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Evidence That the β Subunit of Chlamydia trachomatis Ribonucleotide Reductase Is Active with the Manganese Ion of Its Manganese(IV)/Iron(III) Cofactor in Site 1Structural Basis for Assembly of the Mn IV /Fe III Cofactor in the Class Ic Ribonucleotide Reductase from Chlamydia trachomatisA new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductaseYeast DNA damage-inducible Rnr3 has a very low catalytic activity strongly stimulated after the formation of a cross-talking Rnr1/Rnr3 complex.Isolation of ribonucleotide reductase from Mycobacterium tuberculosis and cloning, expression, and purification of the large subunitLocalization and characterization of two nucleotide-binding sites on the anaerobic ribonucleotide reductase from bacteriophage T4.Ribonucleotide reductase genes of Bacillus prophages: a refuge to introns and intein coding sequences.Two distinct mechanisms of inactivation of the class Ic ribonucleotide reductase from Chlamydia trachomatis by hydroxyurea: implications for the protein gating of intersubunit electron transfer.The disulfide bonding system suppresses CsgD-independent cellulose production in Escherichia coli.Bacillus subtilis class Ib ribonucleotide reductase is a dimanganese(III)-tyrosyl radical enzyme.Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductaseRole of the C terminus of the ribonucleotide reductase large subunit in enzyme regeneration and its inhibition by Sml1Ribonucleotide reductase in the archaeon Pyrococcus furiosus: a critical enzyme in the evolution of DNA genomes?RNA-dependent inhibition of ribonucleotide reductase is a major pathway for 5-azacytidine activity in acute myeloid leukemia.Spectroscopic and theoretical approaches for studying radical reactions in class I ribonucleotide reductase.Targeting the Large Subunit of Human Ribonucleotide Reductase for Cancer Chemotherapy.Cloning, sequencing, and expression of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii.A manganese(IV)/iron(IV) intermediate in assembly of the manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase.Branched activation- and catalysis-specific pathways for electron relay to the manganese/iron cofactor in ribonucleotide reductase from Chlamydia trachomatis.Formation and function of the Manganese(IV)/Iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductaseFunction of the diiron cluster of Escherichia coli class Ia ribonucleotide reductase in proton-coupled electron transfer.Radical-translocation intermediates and hurdling of pathway defects in "super-oxidized" (Mn(IV)/Fe(IV)) Chlamydia trachomatis ribonucleotide reductase.Direct Measurement of the Radical Translocation Distance in the Class I Ribonucleotide Reductase from Chlamydia trachomatis.Two active site asparagines are essential for the reaction mechanism of the class III anaerobic ribonucleotide reductase from bacteriophage T4.Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase.In vivo assay for low-activity mutant forms of Escherichia coli ribonucleotide reductase.Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins.The conserved active site asparagine in class I ribonucleotide reductase is essential for catalysis.A unique cysteine-rich Zn-finger domain present in a majority of class II ribonucleotide reductases mediates catalytic turnover.Carboxymethylation of MutS-cysteine-15 specifically inactivates adenosylcobalamin-dependent glutamate mutase. Examination of the role of this residue in coenzyme-binding and catalysis.Cross-talk between the allosteric effector-binding sites in mouse ribonucleotide reductase.The irreversible inactivation of ribonucleotide reductase from Escherichia coli by superoxide radicals.Crystallization and crystallographic investigations of ribonucleotide reductase protein R1 from Escherichia coli.
P2860
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P2860
Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity.
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1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh
1992年學術文章
@zh-hant
name
Characterization of C439SR1, a ...... vel thioredoxin-like activity.
@en
type
label
Characterization of C439SR1, a ...... vel thioredoxin-like activity.
@en
prefLabel
Characterization of C439SR1, a ...... vel thioredoxin-like activity.
@en
P2093
P356
P1433
P1476
Characterization of C439SR1, a ...... vel thioredoxin-like activity.
@en
P2093
P304
P356
10.1021/BI00155A031
P407
P577
1992-10-01T00:00:00Z