Differential sensitivity of the tyrosyl radical of mouse ribonucleotide reductase to nitric oxide and peroxynitrite. (Q47681636)

4 February 2018

title

Differential sensitivity of the tyrosyl radical of mouse ribonucleotide reductase to nitric oxide and peroxynitrite. (English)

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4 February 2018

author name string

Guittet O

1

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4 February 2018

Ducastel B

2

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Salem JS

3

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Henry Y

4

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4 February 2018

Rubin H

5

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Lemaire G

6

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Lepoivre M

7

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language of work or name

English

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publication date

1 August 1998

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4 February 2018

Journal of Biological Chemistry

published in

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volume

273

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issue

34

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page(s)

22136-22144

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Structure-function aspects in the nitric oxide synthases

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Modulation of iron regulatory protein functions. Further insights into the role of nitrogen- and oxygen-derived reactive species

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From RNA to DNA, why so many ribonucleotide reductases?

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Structure and function of the Escherichia coli ribonucleotide reductase protein R2

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The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2

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

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Inactivation of ribonucleotide reductase by nitric oxide

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Inhibition of ribonucleotide reductase by nitric oxide derived from thionitrites: reversible modifications of both subunits

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

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High level expression of the large subunit of mouse ribonucleotide reductase in a baculovirus system

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Reaction kinetics for nitrosation of cysteine and glutathione in aerobic nitric oxide solutions at neutral pH. Insights into the fate and physiological effects of intermediates generated in the NO/O2 reaction.

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Correlation between nitric oxide formation during degradation of organic nitrates and activation of guanylate cyclase.

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Sensitivity of the essential zinc-thiolate moiety of yeast alcohol dehydrogenase to hypochlorite and peroxynitrite.

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Nitric oxide rapidly scavenges tyrosine and tryptophan radicals

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Reversible red-ox reactions of the diiron site in the mouse ribonucleotide reductase R2 protein.

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Effect of the tyrosyl radical on the reduction and structure of the Escherichia coli ribonucleotide reductase protein R2 diferric site as probed by EPR on the mixed-valent state.

21 January 2018

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The reaction of no with superoxide

21 January 2018

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The irreversible inactivation of ribonucleotide reductase from Escherichia coli by superoxide radicals.

21 January 2018

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Superoxide and peroxynitrite generation from inducible nitric oxide synthase in macrophages

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.34.22136

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4 February 2018

PubMed ID

9705359

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4 February 2018