Metal use in ribonucleotide reductase R2, di-iron, di-manganese and heterodinuclear--an intricate bioinorganic workaround to use different metals for the same reaction (Q37832401)

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scientific article published on 25 January 2011

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English	Metal use in ribonucleotide reductase R2, di-iron, di-manganese and heterodinuclear--an intricate bioinorganic workaround to use different metals for the same reaction	scientific article published on 25 January 2011

Statements

scholarly article

1 reference

Europe PubMed Central

24 August 2017

1 reference

Europe PubMed Central

Metal use in ribonucleotide reductase R2, di-iron, di-manganese and heterodinuclear--an intricate bioinorganic workaround to use different metals for the same reaction (English)

1 reference

Europe PubMed Central

24 August 2017

object named as

Martin Högbom

1

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publication date

25 January 2011

1 reference

Europe PubMed Central

24 August 2017

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Europe PubMed Central

24 August 2017

3

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Europe PubMed Central

24 August 2017

2

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Europe PubMed Central

24 August 2017

110-120

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Europe PubMed Central

24 August 2017

Metalloproteins and metal sensing

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X-ray structures of ferritins and related proteins

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Di-iron-carboxylate proteins

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Three-dimensional structure of the free radical protein of ribonucleotide reductase

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Stearoyl-acyl carrier protein delta 9 desaturase from Ricinus communis is a diiron-oxo protein

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Hydroxylation of C-H bonds at carboxylate-bridged diiron centres

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Evolution of the soluble diiron monooxygenases

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Rational reprogramming of the R2 subunit of Escherichia coli ribonucleotide reductase into a self-hydroxylating monooxygenase.

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Restoring proper radical generation by azide binding to the iron site of the E238A mutant R2 protein of ribonucleotide reductase from Escherichia coli

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The ferritin superfamily: Supramolecular templates for materials synthesis

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Evidence of RNAi in humans from systemically administered siRNA via targeted nanoparticles

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Ribonucleotide reductase inhibitors and future drug design

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Ribonucleotide reductases

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From RNA to DNA, why so many ribonucleotide reductases?

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21 January 2018

To be there when the picture is painted

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Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase

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Structural basis for allosteric substrate specificity regulation in anaerobic ribonucleotide reductases

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Ribonucleotide reductases: the evolution of allosteric regulation

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The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer

1 reference

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Structure of ribonucleotide reductase protein R1

1 reference

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21 January 2018

The use of thiols by ribonucleotide reductase.

1 reference

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21 January 2018

Di-iron-tyrosyl radical ribonucleotide reductases

1 reference

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Radical initiation in the class I ribonucleotide reductase: long-range proton-coupled electron transfer?

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Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology

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Structural basis for adenosylcobalamin activation in AdoCbl-dependent ribonucleotide reductases

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The anaerobic ribonucleoside triphosphate reductase from Escherichia coli requires S-adenosylmethionine as a cofactor

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Deoxyribonucleotide synthesis in anaerobic microorganisms: the class III ribonucleotide reductase

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The ribonucleotide reductase jigsaw puzzle: a large piece falls into place.

1 reference

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Quantum chemical studies of radical-containing enzymes

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The radical site in chlamydial ribonucleotide reductase defines a new R2 subclass

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Ribonucleotide reductases

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Spectrum and Iron Content of Protein B2 from Ribonucleoside Diphosphate Reductase

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Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductase.

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Transient free radicals in iron/oxygen reconstitution of mutant protein R2 Y122F. Possible participants in electron transfer chains in ribonucleotide reductase.

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Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase.

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Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site

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Identification of protonated oxygenic ligands of ribonucleotide reductase intermediate X.

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Displacement of the tyrosyl radical cofactor in ribonucleotide reductase obtained by single-crystal high-field EPR and 1.4-A x-ray data

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21 January 2018

The evolution of ribonucleotide reduction

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Mechanistic implications for the formation of the diiron cluster in ribonucleotide reductase provided by quantitative EPR spectroscopy

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Local and global effects of metal binding within the small subunit of ribonucleotide reductase

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Crystal structures of oxidized dinuclear manganese centres in Mn-substituted class I ribonucleotide reductase from Escherichia coli: carboxylate shifts with implications for O2 activation and radical generation

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Crystal structure of the di-iron/radical protein of ribonucleotide reductase from Corynebacterium ammoniagenes

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The obligate intracellular bacterium Chlamydia trachomatis is auxotrophic for three of the four ribonucleoside triphosphates

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Cloning and characterization of ribonucleotide reductase from Chlamydia trachomatis

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Crystals of the ribonucleotide reductase R2 protein from Chlamydia trachomatis obtained by heavy-atom co-crystallization

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A stable FeIII-FeIV replacement of tyrosyl radical in a class I ribonucleotide reductase

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Chlamydial ribonucleotide reductase: tyrosyl radical function in catalysis replaced by the FeIII-FeIV cluster

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Structure of the high-valent FeIIIFeIV state in ribonucleotide reductase (RNR) of Chlamydia trachomatis--combined EPR, 57Fe-, 1H-ENDOR and X-ray studies

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A manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase

1 reference

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21 January 2018

High catalytic activity achieved with a mixed manganese-iron site in protein R2 of Chlamydia ribonucleotide reductase

1 reference

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The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state

1 reference

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Branched activation- and catalysis-specific pathways for electron relay to the manganese/iron cofactor in ribonucleotide reductase from Chlamydia trachomatis

1 reference

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Structural analysis of the Mn(IV)/Fe(III) cofactor of Chlamydia trachomatis ribonucleotide reductase by extended X-ray absorption fine structure spectroscopy and density functional theory calculations

1 reference

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Redox intermediates of the Mn-Fe Site in subunit R2 of Chlamydia trachomatis ribonucleotide reductase: an X-ray absorption and EPR study

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Metal binding and activity of ribonucleotide reductase protein R2 mutants: conditions for formation of the mixed manganese-iron cofactor

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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

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Density functional theory analysis of structure, energetics, and spectroscopy for the Mn-Fe active site of Chlamydia trachomatis ribonucleotide reductase in four oxidation states

1 reference

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Formation and function of the Manganese(IV)/Iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase

1 reference

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The manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase: structure, assembly, radical initiation, and evolution

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Carboxylate-bridged dinuclear active sites in oxygenases: diiron, dimanganese, or is heterodinuclear better?

1 reference

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A manganese(IV)/iron(IV) intermediate in assembly of the manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase

1 reference

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Rapid and quantitative activation of Chlamydia trachomatis ribonucleotide reductase by hydrogen peroxide

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Ribonucleotide reductase of Brevibacterium ammoniagenes is a manganese enzyme.

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A divalent metal site in the small subunit of the manganese-dependent ribonucleotide reductase of Corynebacterium ammoniagenes.

1 reference

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The manganese-containing ribonucleotide reductase of Corynebacterium ammoniagenes is a class Ib enzyme.

1 reference

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The active form of the R2F protein of class Ib ribonucleotide reductase from Corynebacterium ammoniagenes is a diferric protein.

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Structural and mutational studies of the carboxylate cluster in iron-free ribonucleotide reductase R2.

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1 reference

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An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase.

1 reference

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21 January 2018

Biochemistry. A never-ending story.

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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

1 reference

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Homologous expression of the nrdF gene of Corynebacterium ammoniagenes strain ATCC 6872 generates a manganese-metallocofactor (R2F) and a stable tyrosyl radical (Y˙) involved in ribonucleotide reduction

1 reference

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Structural Basis for Activation of Class Ib Ribonucleotide Reductase

1 reference

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RNRdb, a curated database of the universal enzyme family ribonucleotide reductase, reveals a high level of misannotation in sequences deposited to Genbank

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In vivo requirement for glutaredoxins and thioredoxins in the reduction of the ribonucleotide reductases of Escherichia coli.

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Predicting zinc binding at the proteome level

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Unusual clustering of carboxyl side chains in the core of iron-free ribonucleotide reductase

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21 January 2018

Identifiers

10.1039/C0MT00095G

1 reference

Europe PubMed Central

24 August 2017

1 reference

Europe PubMed Central

24 August 2017

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