Pseudomonas aeruginosa exhibits deficient biofilm formation in the absence of class II and III ribonucleotide reductases due to hindered anaerobic growth. [PDF]
Frontiers in Microbiology, 2016 Chronic lung infections by the ubiquitous and extremely adaptable opportunistic pathogen Pseudomonas aeruginosa correlate with the formation of a biofilm, where bacteria grow in association with an extracellular matrix and display a wide range of changes
Anna eCrespo +3 more
doaj +3 more sources
Metallation and mismetallation of iron and manganese proteins in vitro and in vivo: the class I ribonucleotide reductases as a case study. [PDF]
Metallomics, 2012 How cells ensure correct metallation of a given protein and whether a degree of promiscuity in metal binding has evolved are largely unanswered questions.
Cotruvo JA, Stubbe J.
europepmc +3 more sources
Ribonucleotide Reductases: Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets. [PDF]
Annu Rev Biochem, 2020 Ribonucleotide reductases (RNRs) catalyze the de novo conversion of nucleotides to deoxynucleotides in all organisms, controlling their relative ratios and abundance.
Greene BL +6 more
europepmc +4 more sources
RIBONUCLEOTIDE REDUCTASES [PDF]
Annual Review of Biochemistry, 1998 Ribonucleotide reductases provide the building blocks for DNA replication in all living cells. Three different classes of enzymes use protein free radicals to activate the substrate. Aerobic class I enzymes generate a tyrosyl radical with an iron-oxygen center and dioxygen, class II enzymes employ adenosylcobalamin, and the anaerobic class III enzymes
A, Jordan, P, Reichard
openaire +3 more sources
Kinetics of radical intermediate formation and deoxynucleotide production in 3-aminotyrosine-substituted Escherichia coli ribonucleotide reductases. [PDF]
J Am Chem Soc, 2011 Minnihan EC +3 more
europepmc +4 more sources
Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding [PDF]
eLifeA small, nucleotide-binding domain, the ATP-cone, is found at the N-terminus of most ribonucleotide reductase (RNR) catalytic subunits. By binding adenosine triphosphate (ATP) or deoxyadenosine triphosphate (dATP) it regulates the enzyme activity of all ...
Ornella Bimai +8 more
doaj +2 more sources
Control of metallation and active cofactor assembly in the class Ia and Ib ribonucleotide reductases: diiron or dimanganese? [PDF]
Curr Opin Chem Biol, 2011 Ribonucleotide reductases (RNRs) convert nucleotides to deoxynucleotides in all organisms. Activity of the class Ia and Ib RNRs requires a stable tyrosyl radical (Y•), which can be generated by the reaction of O[subscript 2] with a diferrous cluster on ...
Stubbe J, Cotruvo JA.
europepmc +3 more sources
FleQ-Dependent regulation of the ribonucleotide reductase repressor NrdR in Pseudomonas aeruginosa during biofilm growth and infection [PDF]
Scientific ReportsRibonucleotide reductases (RNRs) are essential enzymes that catalyze the conversion of ribonucleotides to deoxyribonucleotides (dNTPs), a critical step in DNA synthesis and repair.
Domingo Marchan +6 more
doaj +2 more sources
The periodic table of ribonucleotide reductases. [PDF]
J Biol Chem, 2021 Ruskoski TB, Boal AK.
europepmc +2 more sources
Ribonucleotide Reductases from Bifidobacteria Contain Multiple Conserved Indels Distinguishing Them from All Other Organisms: In Silico Analysis of the Possible Role of a 43 aa Bifidobacteria-Specific Insert in the Class III RNR Homolog [PDF]
Frontiers in Microbiology, 2017 Bifidobacteria comprises an important group/order of bacteria whose members have widespread usage in the food and health industry due to their health-promoting activity in the human gastrointestinal tract.
Seema Alnajar +2 more
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