A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase (Q27748304)

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

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scholarly article

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

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Escherichia coli

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based on heuristic

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Britt-Marie Sjöberg

6

object named as

B M Sjöberg

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author name string

A L Persson

1

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B Katterle

3

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S Pötsch

4

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M Sahlin

5

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M Eriksson

2

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language of work or name

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publication date

12 December 1997

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Journal of Biological Chemistry

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272

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50

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31533-41

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From RNA to DNA, why so many ribonucleotide reductases?

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https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

The evolution of ribonucleotide reduction

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https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

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

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https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Structure and function of the Escherichia coli ribonucleotide reductase protein R2

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https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Structure of ribonucleotide reductase protein R1

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https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Site-directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2. Effects on catalytic activity and subunit interaction.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

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

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https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

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

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21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Interaction of C225SR1 mutant subunit of ribonucleotide reductase with R2 and nucleoside diphosphates: tales of a suicidal enzyme

1 reference

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21 January 2018

Mechanism of inactivation of Escherichia coli ribonucleotide reductase by 2'-chloro-2'-deoxyuridine 5'-diphosphate: evidence for generation of a 2'-deoxy-3'-ketonucleotide via a net 1,2 hydrogen shift

1 reference

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21 January 2018

Inactivation of ribonucleotide reductase by (E)-2'-fluoromethylene-2'-deoxycytidine 5'-diphosphate: a paradigm for nucleotide mechanism-based inhibitors.

1 reference

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21 January 2018

Inactivation of Escherichia coli ribonucleotide reductase by 2'-deoxy-2'-mercaptouridine 5'-diphosphate. Electron paramagnetic resonance evidence for a transient protein perthiyl radical.

1 reference

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21 January 2018

A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes

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https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Rapid and efficient site-specific mutagenesis without phenotypic selection

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https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Rapid and efficient site-specific mutagenesis without phenotypic selection

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https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

30 Ribonucleoside diphosphate reductase (Escherichia coli)

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https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

An ultrafiltration assay for nucleotide binding to ribonucleotide reductase.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Magnetic interaction between the tyrosyl free radical and the antiferromagnetically coupled iron center in ribonucleotide reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

EPR stopped-flow studies of the reaction of the tyrosyl radical of protein R2 from ribonucleotide reductase with hydroxyurea

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Crystallization and crystallographic investigations of ribonucleotide reductase protein R1 from Escherichia coli.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Processing of X-ray diffraction data collected in oscillation mode

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https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

The CCP4 suite: programs for protein crystallography

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Improved methods for building protein models in electron density maps and the location of errors in these models

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Carboxyl-terminal peptides as probes for Escherichia coli ribonucleotide reductase subunit interaction: kinetic analysis of inhibition studies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Ribonucleotide Reductase from Escherichia coli: Demonstration of a Highly Active Form of the Enzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Products of the inactivation of ribonucleoside diphosphate reductase from Escherichia coli with 2'-azido-2'-deoxyuridine 5'-diphosphate

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Density functional calculations on model tyrosyl radicals

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https://api.crossref.org/works/10.1074%2FJBC.272.50.31533

21 January 2018

Identifiers

10.1074/JBC.272.50.31533

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