(Q54590165)

1 June 2018

title

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

1 reference

1 June 2018

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Ollagnier S

1

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1 June 2018

Mulliez E

2

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1 June 2018

Gaillard J

3

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1 June 2018

Eliasson R

4

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1 June 2018

Fontecave M

5

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1 June 2018

Reichard P

6

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1 June 2018

language of work or name

English

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publication date

1 April 1996

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1 June 2018

Journal of Biological Chemistry

number of pages

7

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based on heuristic

inferred from page(s)

published in

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1 June 2018

volume

271

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1 June 2018

page(s)

9410-9416

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1 June 2018

issue

16

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1 June 2018

From RNA to DNA, why so many ribonucleotide reductases?

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

Escherichia coli ferredoxin NADP+ reductase: activation of E. coli anaerobic ribonucleotide reduction, cloning of the gene (fpr), and overexpression of the protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

Molecular properties of pyruvate formate-lyase activating enzyme.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

Ribonucleoside diphosphate reductase. Formation of active and inactive complexes of proteins B1 and B2.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

Flavodoxin is required for the activation of the anaerobic ribonucleotide reductase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: Isolation and structural properties

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.16.9410

21 January 2018

Identifiers

DOI

10.1074/JBC.271.16.9410

1 reference

1 June 2018

release_5ow4547yc5aatfyk6tlvd4yjmm

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/5ow4547yc5aatfyk6tlvd4yjmm

mapped directly with Wikidata item

24 November 2022

based on heuristic

PubMed ID

8621608

1 reference

1 June 2018