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Fusion of a functional glutaredoxin to the radical-generating subunit of ribonucleotide reductase

https://doi.org/10.1101/373563
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The Most Interesting Enzyme in the World
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Thioredoxin and Glutaredoxin Systems
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Ribonucleotide reductases: the link between an RNA and a DNA world?
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Macromolecule Analysis Based on Electrophoretic Mobility in Air: Globular Proteins
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Structural Basis for Superoxide Activation of Flavobacterium johnsoniae Class I Ribonucleotide Reductase and for Radical Initiation by Its Dimanganese Cofactor
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Electronic structure of dimanganese(II,III) and dimanganese(III,IV) complexes and dimanganese catalase enzyme: a general EPR spectral simulation approach
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A Tyrosyl−Dimanganese Coupled Spin System is the Native Metalloradical Cofactor of the R2F Subunit of the Ribonucleotide Reductase of Corynebacterium ammoniagenes
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Mechanism of Assembly of the Dimanganese-Tyrosyl Radical Cofactor of Class Ib Ribonucleotide Reductase: Enzymatic Generation of Superoxide Is Required for Tyrosine Oxidation via a Mn(III)Mn(IV) Intermediate
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Metal-free ribonucleotide reduction powered by a DOPA radical in Mycoplasma pathogens
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Systematic re-evaluation of the bis(2-hydroxyethyl)disulfide (HEDS) assay reveals an alternative mechanism and activity of glutaredoxins
inferredcites →https://doi.org/10.1039/c7sc04416jopenalex-snapshot
Glutaredoxins employ parallel monothiol–dithiol mechanisms to catalyze thiol–disulfide exchanges with protein disulfides
inferredcites →https://doi.org/10.1042/bsr20140157openalex-snapshot
The glutaredoxin mono- and di-thiol mechanisms for deglutathionylation are functionally equivalent: implications for redox systems biology
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Physiological functions of thioredoxin and thioredoxin reductase
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Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli
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Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione.
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Cloning, Overexpression, and Characterization of Glutaredoxin 2, An Atypical Glutaredoxin from Escherichia coli
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Characterization of Escherichia coli NrdH
inferredcites →https://doi.org/10.1074/jbc.m115.649624openalex-snapshot
Diversity in Overall Activity Regulation of Ribonucleotide Reductase
inferredcites →https://doi.org/10.1074/jbc.m806738200openalex-snapshot
Oligomerization Status Directs Overall Activity Regulation of the Escherichia coli Class Ia Ribonucleotide Reductase
inferredcites →https://doi.org/10.1074/jbc.m809338200openalex-snapshot
Molecular Mechanisms of Thioredoxin and Glutaredoxin as Hydrogen Donors for Mammalian S Phase Ribonucleotide Reductase
inferredcites →https://doi.org/10.1089/ars.2012.5007openalex-snapshot
Glutaredoxins in Thiol/Disulfide Exchange
inferredcites →https://doi.org/10.1093/nar/gkv1344openalex-snapshot
The Pfam protein families database: towards a more sustainable future
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RefSeq: an update on prokaryotic genome annotation and curation
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Facklamia Species as an Underrecognized Pathogen
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Notes: Phenotypic and Phylogenetic Characterization of Some Globicatella-Like Organisms from Human Sources: Description of Facklamia hominis gen. nov., sp. nov.
inferredcites →https://doi.org/10.1126/science.1098419openalex-snapshot
The Radical Site in Chlamydial Ribonucleotide Reductase Defines a New R2 Subclass
inferredcites →https://doi.org/10.1126/science.1141179openalex-snapshot
A Manganese(IV)/Iron(III) Cofactor in Chlamydia trachomatis Ribonucleotide Reductase
inferredcites →https://doi.org/10.1128/jb.01020-07openalex-snapshot
Characterization of Nucleotide Pools as a Function of Physiological State in Escherichia coli
inferredcites →https://doi.org/10.1128/jcm.36.7.2146-2148.1998openalex-snapshot
Facklamia ignava sp. nov., Isolated from Human Clinical Specimens
inferredcites →https://doi.org/10.1371/journal.pcbi.1002195openalex-snapshot
Accelerated Profile HMM Searches
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DNA building blocks: keeping control of manufacture
inferredcites →https://doi.org/10.3389/fcimb.2014.00035openalex-snapshot
Comparative review of Francisella tularensis and Francisella novicida
inferredcites →https://doi.org/10.3389/fcimb.2014.00052openalex-snapshot
Ribonucleotide reductases: essential enzymes for bacterial life
inferredcites →https://doi.org/10.3390/life5010604openalex-snapshot
The Origin and Evolution of Ribonucleotide Reduction
inferredcites →https://doi.org/10.4331/wjbc.v5.i1.68openalex-snapshot
Thioredoxin and glutaredoxin-mediated redox regulation of ribonucleotide reductase
inferredcites →https://doi.org/10.7554/elife.31529openalex-snapshot
Novel ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit
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