(Q54611977)

English

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

scientific article

In more languages

default for all languages

No label defined

No description defined

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

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

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

Britt-Marie Sjöberg

4

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

Astrid Gräslund

5

object named as

Gräslund A

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

author name string

Sahlin M

1

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

Lassmann G

2

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

Pötsch S

3

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

language of work or name

0 references

publication date

1 May 1995

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

number of pages

12

1 reference

based on heuristic

inferred from page(s)

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

270

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

21

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

12361-12372

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

Oxygen activation and the conservation of energy in cell respiration

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

Resonance Raman spectroscopy of ribonucleotide reductase. Evidence for a deprotonated tyrosyl radical and photochemistry of the binuclear iron center.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

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.270.21.12361

21 January 2018

The Asp-His-Fe triad of cytochrome c peroxidase controls the reduction potential, electronic structure, and coupling of the tryptophan free radical to the heme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

The tyrosyl free radical in ribonucleotide reductase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

Time-resolved EPR studies with DNA photolyase: excited-state FADH0 abstracts an electron from Trp-306 to generate FADH-, the catalytically active form of the cofactor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

Charge transfer in peptides. Pulse radiolysis investigation of one-electron reactions in dipeptides of tryptophan and tyrosine

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

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.270.21.12361

21 January 2018

Purification and characterization of recombinant mouse and herpes simplex virus ribonucleotide reductase R2 subunit

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

Structure and function of the Escherichia coli ribonucleotide reductase protein R2

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

From RNA to DNA, why so many ribonucleotide reductases?

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

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.270.21.12361

21 January 2018

Reduced forms of the iron-containing small subunit of ribonucleotide reductase from Escherichia coli.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

An ENDOR study of the tyrosyl free radical in ribonucleotide reductase from Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

Electron-tunneling pathways in proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

High valent iron oxo intermediates might be involved during activation of ribonucleotide reductase: single oxygen atom donors generate the tyrosyl radical

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

Activation of the iron-containing B2 protein of ribonucleotide reductase by hydrogen peroxide

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.21.12361

21 January 2018

Identifiers

10.1074/JBC.270.21.12361

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7759477

Sitelinks

Wikipedia(0 entries)

Wikibooks(0 entries)

Wikinews(0 entries)

Wikiquote(0 entries)

Wikisource(0 entries)

Wikiversity(0 entries)

Wikivoyage(0 entries)

Wiktionary(0 entries)

Multilingual sites(0 entries)

Retrieved from "https://www.wikidata.org/w/index.php?title=Q54611977&oldid=1949653648"