(Q57867932)

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Electron Paramagnetic Resonance Evidence for a Novel Interconversion of [3Fe-4S]+and [4Fe-4S]+Clusters with Endogenous Iron and Sulfide in Anaerobic Ribonucleotide Reductase Activasein Vitro

scientific article published in Journal of Biological Chemistry

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scholarly article

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6 November 2019

Electron paramagnetic resonance evidence for a novel interconversion of [3Fe-4S](+) and [4Fe-4S](+) clusters with endogenous iron and sulfide in anaerobic ribonucleotide reductase activase in vitro (English)

1 reference

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6 November 2019

1

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6 November 2019

Astrid Gräslund

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A Gräslund

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6 November 2019

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1 April 2000

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6 November 2019

Journal of Biological Chemistry

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6 November 2019

275

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6 November 2019

12367-12373

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6 November 2019

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6 November 2019

Ribonucleotide reductases

1 reference

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21 January 2018

Oxygen-sensitive ribonucleoside triphosphate reductase is present in anaerobic Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

From RNA to DNA, why so many ribonucleotide reductases?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

A general system for generating unlabelled gene replacements in bacterial chromosomes.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis. Catalytic properties and allosteric regulation of the pure enzyme system.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

Iron-sulfur clusters: nature's modular, multipurpose structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

Aconitase as Ironminus signSulfur Protein, Enzyme, and Iron-Regulatory Protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

Mössbauer studies of beef heart aconitase: evidence for facile interconversions of iron-sulfur clusters

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

[3Fe-4S] to [4Fe-4S] cluster conversion in Desulfovibrio fructosovorans [NiFe] hydrogenase by site-directed mutagenesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

A T14C variant of Azotobacter vinelandii ferredoxin I undergoes facile [3Fe-4S]0 to [4Fe-4S]2+ conversion in vitro but not in vivo

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

[3Fe-4S] <--> [4Fe-4S] cluster interconversion in Desulfovibrio africanus ferredoxin III: properties of an Asp14 --> Cys mutant.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

Mössbauer spectroscopy as a tool for the study of activation/inactivation of the transcription regulator FNR in whole cells of Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

An all-ferrous state of the Fe protein of nitrogenase. Interaction with nucleotides and electron transfer to the MoFe protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

Protein Radicals in Enzyme Catalysis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

The lipoate synthase from Escherichia coli is an iron-sulfur protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

The anaerobic ribonucleotide reductase from Escherichia coli. The small protein is an activating enzyme containing a [4fe-4s](2+) center

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

Endonuclease III is an iron-sulfur protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

3Fe-4S to 4Fe-4S cluster conversion in Escherichia coli fumarate reductase by site-directed mutagenesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

S-Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance

1 reference

https://api.crossref.org/works/10.1074%2FJBC.275.17.12367

21 January 2018

Identifiers

10.1074/JBC.275.17.12367

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10777518%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10777518%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

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