PMID:8267617
| Citation |
Bianchi, V, Eliasson, R, Fontecave, M, Mulliez, E, Hoover, DM, Matthews, RG and Reichard, P (1993) Flavodoxin is required for the activation of the anaerobic ribonucleotide reductase. Biochem. Biophys. Res. Commun. 197:792-7 |
|---|---|
| Abstract |
The inactive anaerobic ribonucleotide reductase from Escherichia coli is transformed by a multienzyme system and S-adenosylmethionine + NADPH into a radical protein that is enzymatically active. One of the activating enzyme components was earlier shown to be ferredoxin (flavodoxin):NADP+ reductase. Here we present evidence that flavodoxin, but not ferredoxin, also is a component of the system. Light reduced deazaflavin can substitute for the flavodoxin system. An additional unidentified low-molecular weight component further stimulates the reaction. |
| Links |
PubMed Online version:10.1006/bbrc.1993.2548 |
| Keywords |
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/metabolism; Anaerobiosis; Base Sequence; Chromatography, Gel; Cloning, Molecular; DNA Primers; Enzyme Activation; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli/growth & development; Flavodoxin/biosynthesis; Flavodoxin/isolation & purification; Flavodoxin/metabolism; Genes, Bacterial; Kinetics; Molecular Sequence Data; Polymerase Chain Reaction; Recombinant Proteins/biosynthesis; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Restriction Mapping; Ribonucleotide Reductases/isolation & purification; Ribonucleotide Reductases/metabolism |
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