A unique cysteine-rich zinc finger domain present in a majority of class II ribonucleotide reductases mediates catalytic turnover-Reference-Cited by-同舟云学术

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A unique cysteine-rich zinc finger domain present in a majority of class II ribonucleotide reductases mediates catalytic turnover

Published:2017-11 Issue:46 Volume:292 Page:19044-19054
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Loderer Christoph,Jonna Venkateswara Rao,Crona Mikael,Rozman Grinberg Inna,Sahlin Margareta,Hofer Anders,Lundin Daniel,Sjöberg Britt-Marie

Funder

Vetenskapsrådet

Cancerfonden

Wenner-Gren Stiftelserna

Carl Tryggers Stiftelse för Vetenskaplig Forskning

Kempestiftelserna

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference41 articles.

1. Ribonucleotide reductases;Nordlund;Annu. Rev. Biochem,2006

2. The origin and evolution of ribonucleotide reduction;Lundin;Life,2015

3. Radical initiation in the class I ribonucleotide reductase: long-range proton-coupled electron transfer;Stubbe;Chem. Rev,2003

4. Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli;Åberg;J. Biol. Chem,1989

5. 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;Mao;Biochemistry,1992

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4. A rapid and sensitive assay for quantifying the activity of both aerobic and anaerobic ribonucleotide reductases acting upon any or all substrates;PLOS ONE;2022-06-08

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