GlutaredoxinV1, Main, Exploration, bibRecord, 001227

Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli.

Identifieur interne : 001227 ( Main/Exploration ); précédent : 001226; suivant : 001228

Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli.

Auteurs : E. Mulliez [France] ; S. Ollagnier ; M. Fontecave ; R. Eliasson ; P. Reichard

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 1995.

RBID : pubmed:7568012

Descripteurs français

KwdFr :
- Anaérobiose (MeSH), Cytidine triphosphate (métabolisme), Dioxyde de carbone (métabolisme), Escherichia coli (enzymologie), Ferrosulfoprotéines (isolement et purification), Ferrosulfoprotéines (métabolisme), Formiates (métabolisme), Glycine (métabolisme), Nucléotides désoxycytidyliques (biosynthèse), Oxydoréduction (MeSH), Radicaux libres (MeSH), Ribonucleotide reductases (classification), Ribonucleotide reductases (isolement et purification), Ribonucleotide reductases (métabolisme), Spécificité du substrat (MeSH).
MESH :
- biosynthèse : Nucléotides désoxycytidyliques.
- classification : Ribonucleotide reductases.
- enzymologie : Escherichia coli.
- isolement et purification : Ferrosulfoprotéines, Ribonucleotide reductases.
- métabolisme : Cytidine triphosphate, Dioxyde de carbone, Ferrosulfoprotéines, Formiates, Glycine, Ribonucleotide reductases.
- Anaérobiose, Oxydoréduction, Radicaux libres, Spécificité du substrat.

English descriptors

KwdEn :
- Anaerobiosis (MeSH), Carbon Dioxide (metabolism), Cytidine Triphosphate (metabolism), Deoxycytosine Nucleotides (biosynthesis), Escherichia coli (enzymology), Formates (metabolism), Free Radicals (MeSH), Glycine (metabolism), Iron-Sulfur Proteins (isolation & purification), Iron-Sulfur Proteins (metabolism), Oxidation-Reduction (MeSH), Ribonucleotide Reductases (classification), Ribonucleotide Reductases (isolation & purification), Ribonucleotide Reductases (metabolism), Substrate Specificity (MeSH).
MESH :
- chemical , biosynthesis : Deoxycytosine Nucleotides.
- chemical , classification : Ribonucleotide Reductases.
- chemical , isolation & purification : Iron-Sulfur Proteins, Ribonucleotide Reductases.
- chemical , metabolism : Carbon Dioxide, Cytidine Triphosphate, Formates, Glycine, Iron-Sulfur Proteins, Ribonucleotide Reductases.
- enzymology : Escherichia coli.
- Anaerobiosis, Free Radicals, Oxidation-Reduction, Substrate Specificity.

Abstract

During anaerobic growth Escherichia coli uses a specific ribonucleoside-triphosphate reductase (class III enzyme) for the production of deoxyribonucleoside triphosphates. In its active form, the enzyme contains an iron-sulfur center and an oxygen-sensitive glycyl radical (Gly-681). The radical is generated in the inactive protein from S-adenosylmethionine by an auxiliary enzyme system present in E. coli. By modification of the previous purification procedure, we now prepared a glycyl radical-containing reductase, active in the absence of the auxiliary reducing enzyme system. This reductase uses formate as hydrogen donor in the reaction. During catalysis, formate is stoichiometrically oxidized to CO2, and isotope from [3H]formate appears in water. Thus E. coli uses completely different hydrogen donors for the reduction of ribonucleotides during anaerobic and aerobic growth. The aerobic class I reductase employs redox-active thiols from thioredoxin or glutaredoxin to this purpose. The present results strengthen speculations that class III enzymes arose early during the evolution of DNA.

DOI: 10.1073/pnas.92.19.8759
PubMed: 7568012
PubMed Central: PMC41046

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Deoxycytosine Nucleotides (biosynthesis)</term>
<term>Escherichia coli (enzymology)</term>
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<term>Ribonucleotide reductases (isolement et purification)</term>
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<front><div type="abstract" xml:lang="en">During anaerobic growth Escherichia coli uses a specific ribonucleoside-triphosphate reductase (class III enzyme) for the production of deoxyribonucleoside triphosphates. In its active form, the enzyme contains an iron-sulfur center and an oxygen-sensitive glycyl radical (Gly-681). The radical is generated in the inactive protein from S-adenosylmethionine by an auxiliary enzyme system present in E. coli. By modification of the previous purification procedure, we now prepared a glycyl radical-containing reductase, active in the absence of the auxiliary reducing enzyme system. This reductase uses formate as hydrogen donor in the reaction. During catalysis, formate is stoichiometrically oxidized to CO2, and isotope from [3H]formate appears in water. Thus E. coli uses completely different hydrogen donors for the reduction of ribonucleotides during anaerobic and aerobic growth. The aerobic class I reductase employs redox-active thiols from thioredoxin or glutaredoxin to this purpose. The present results strengthen speculations that class III enzymes arose early during the evolution of DNA.</div>
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   |texte=   Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli.
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	Serveur d'exploration sur la glutarédoxine
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Serveur d'exploration sur la glutarédoxine

Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli.

Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli.

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