(Q30818700)

26 June 2017

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title

Glycyl radical enzymes: a conservative structural basis for radicals (English)

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26 June 2017

Eklund H

1

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26 June 2017

Fontecave M

series ordinal

2

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26 June 2017

publication date

1 November 1999

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26 June 2017

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26 June 2017

volume

7

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26 June 2017

issue

11

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26 June 2017

page(s)

R257-62

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

26 June 2017

cites work

1 reference

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7 January 2021

A model for the role of multiple cysteine residues involved in ribonucleotide reduction: amazing and still confusing

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7 January 2021

Thiyl radicals in ribonucleotide reductases.

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7 January 2021

The Free Radical of the Anaerobic Ribonucleotide Reductase fromEscherichia coliIs at Glycine 681

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7 January 2021

Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli

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7 January 2021

The free radical in pyruvate formate-lyase is located on glycine-734

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7 January 2021

From RNA to DNA, why so many ribonucleotide reductases?

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7 January 2021

Ribonucleotide reductases

1 reference

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7 January 2021

Structure of ribonucleotide reductase protein R1

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2800%2980019-2

7 January 2021

Ribonucleotide reductase in the archaeon Pyrococcus furiosus: a critical enzyme in the evolution of DNA genomes?

1 reference

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7 January 2021

The B12-dependent ribonucleotide reductase from the archaebacterium Thermoplasma acidophila: an evolutionary solution to the ribonucleotide reductase conundrum

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7 January 2021

B12-dependent ribonucleotide reductases from deeply rooted eubacteria are structurally related to the aerobic enzyme from Escherichia coli.

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7 January 2021

The anaerobic Escherichia coli ribonucleotide reductase. Subunit structure and iron sulfur center.

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7 January 2021

Activation of the anaerobic ribonucleotide reductase from Escherichia coli. The essential role of the iron-sulfur center for S-adenosylmethionine reduction.

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7 January 2021

Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding

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7 January 2021

A Glycyl Radical Site in the Crystal Structure of a Class III Ribonucleotide Reductase

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7 January 2021

Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase

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7 January 2021

Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase

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7 January 2021

Glycyl free radical in pyruvate formate-lyase: synthesis, structure characteristics, and involvement in catalysis.

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7 January 2021

Electron paramagnetic resonance evidence for a cysteine-based radical in pyruvate formate-lyase inactivated with mercaptopyruvate

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7 January 2021

Bacteriophage T4 anaerobic ribonucleotide reductase contains a stable glycyl radical at position 580.

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7 January 2021

Post-translational activation introduces a free radical into pyruvate formate-lyase

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7 January 2021

Mass spectrometric determination of the radical scission site in the anaerobic ribonucleotide reductase of Escherichia coli

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7 January 2021

Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase.

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7 January 2021

A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase

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7 January 2021

Protein Radicals in Enzyme Catalysis

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7 January 2021

The mechanism of the anaerobic Escherichia coli ribonucleotide reductase investigated with nuclear magnetic resonance spectroscopy

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7 January 2021

Pyruvate formate-lyase mechanism involving the protein-based glycyl radical

1 reference

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7 January 2021

Hydrogen exchange of the glycyl radical of pyruvate formate-lyase is catalyzed by cysteine 419

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2800%2980019-2

7 January 2021

10.1016/S0969-2126(00)80019-2

Identifiers

DOI

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26 June 2017

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