Ribonucleotide reductases: The link between an RNA and a DNA world?

Current Opinion in Structural Biology

Volumn 10, Issue 6, 2000, Pages 731-736

  Stubbe, J ^a  

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; FORMATE ACETYLTRANSFERASE; PYRUVIC ACID DERIVATIVE; RIBONUCLEOTIDE REDUCTASE; RNA; UNCLASSIFIED DRUG;

CATALYSIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME REGULATION; ENZYME STRUCTURE; EVOLUTION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; REVIEW; SEQUENCE HOMOLOGY;

EID: 0034525463     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(00)00153-6     Document Type: Review

References (23)

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2. Ribonucleotide reductases in the twenty-first century
3. Protein radicals in enzyme catalysis
4. A glycyl radical site in the crystal structure of a class III ribonucleotide reductase
5. Binding of allosteric effectors to ribonucleotide reductase protein R1: Reduction of active-site cysteines promotes substrate binding
6. Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase
7. Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase
8. The evolution of ribonucleotide reduction
9. From RNA to DNA, why so many ribonucleotide reductases?
10. Ribonucleotide reductases: Amazing and confusing
11. The ten-stranded β/α barrel in ribonucleotide reductase protein R1
12. Thiyl radicals in ribonucleotide reductases
13. Mechanistic investigations of ribonucleotide reductases
14. Iron-sulfur interconversions in the anaerobic ribonucleotide reductase from Escherichia coli
15. Reconstitution and characterization of the polynucleer iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form
16. + cluster
17. Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli
18. Ribonucleoside diphosphate reductase. Formation of active and inactive complexes of proteins B1 and B2
19. Structure and function of the Escherichia coli ribonucleotide reductase protein R2
20. The free radical of the anaerobic ribonucleotide reductase from Escherichia coli is at glycine 681
21. The activating component of the anaerobic ribonucleotide reductase from Escherichia coli. An iron-sulfur center with only three cysteines
22. Cysteines involved in radical generation and catalysis of class III anaerobic ribonucleotide reductase. A protein engineering study of bacteriophage T4 NrdD
23. Cobamides and ribonucleotide reduction. XII. The electron paramagnetic resonance spectrum of ′active coenzyme B12′