(Q46947539)

26 December 2017

title

PELDOR study on the tyrosyl radicals in the R2 protein of mouse ribonucleotide reductase (English)

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26 December 2017

4

Wolfgang Lubitz

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26 December 2017

Daniele Biglino

1

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26 December 2017

Peter P Schmidt

series ordinal

2

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26 December 2017

Edward J Reijerse

series ordinal

3

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26 December 2017

language of work or name

English

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publication date

21 November 2005

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26 December 2017

Physical Chemistry Chemical Physics

published in

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26 December 2017

volume

8

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issue

1

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26 December 2017

page(s)

58-62

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26 December 2017

Structure and function of the radical enzyme ribonucleotide reductase

cites work

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Ribonucleotide reductases: the evolution of allosteric regulation

21 January 2018

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Structure of ribonucleotide reductase protein R1

21 January 2018

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Kinetic evidence that a radical transfer pathway in protein R2 of mouse ribonucleotide reductase is involved in generation of the tyrosyl free radical.

21 January 2018

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Pulsed ELDOR spectroscopy measures the distance between the two tyrosyl dadicals in the R2 subunit of the E. coli ribonucleotide reductase

21 January 2018

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Displacement of the tyrosyl radical cofactor in ribonucleotide reductase obtained by single-crystal high-field EPR and 1.4-A x-ray data

21 January 2018

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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

21 January 2018

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Crystal structural studies of changes in the native dinuclear iron center of ribonucleotide reductase protein R2 from mouse

21 January 2018

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Hydrogen bond geometries from electron paramagnetic resonance and electron-nuclear double resonance parameters: density functional study of quinone radical anion-solvent interactions

21 January 2018

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21 January 2018

Identifiers

DOI

10.1039/B513950C

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26 December 2017

PubMed ID

16482244

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26 December 2017