Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding (Q27744341)

1 reference

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17 November 2024

U. Uhlin

1 reference

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17 November 2024

S. Ramaswamy

1 reference

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17 November 2024

M. Ekberg

1 reference

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17 November 2024

K. Regnström

1 reference

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17 November 2024

B. M. Sjöberg

1 reference

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17 November 2024

H. Eklund

1 reference

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17 November 2024

language of work or name

English

1 reference

National Center for Biotechnology Information

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/esummary.fcgi?db=pubmed&retmode=json&id=9309223

full work available at URL

17 November 2024

publication date

15 August 1997

0 references

http://www.cell.com/article/S0969212697002591/pdf

file format

Portable Document Format

online access status

open access

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A9309223

https://api.elsevier.com/content/article/PII:S0969212697002591?httpAccept=text/xml

17 November 2024

1 reference

DOI

https://api.crossref.org/works/10.1016/S0969-2126(97)00259-1

https://api.elsevier.com/content/article/PII:S0969212697002591?httpAccept=text/plain

17 November 2024

1 reference

DOI

https://api.crossref.org/works/10.1016/S0969-2126(97)00259-1

17 November 2024

0 references

0 references

0 references

1077-92

0 references

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

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

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The Cys292-->Ala substitution in protein R1 of class I ribonucleotide reductase from Escherichia coli has a global effect on nucleotide binding at the specificity-determining allosteric site.

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NMR structure of oxidized Escherichia coli glutaredoxin: Comparison with reduced E. coli glutaredoxin and functionally related proteins

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The structure of a reduced mutant T4 glutaredoxin

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

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Structure and function of the Escherichia coli ribonucleotide reductase protein R2

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

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

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

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

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

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Pyridine nucleotide - disulfide oxidoreductases

17 November 2024

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17 November 2024

Identifiers

DOI

0 references