PMID:2663852
| Citation |
Aberg, A, Hahne, S, Karlsson, M, Larsson, A, Ormö, M, Ahgren, A and Sjöberg, BM (1989) Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli. J. Biol. Chem. 264:12249-52 |
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| Abstract |
The large subunit of ribonucleotide reductase from Escherichia coli contains redox-active cysteine residues. In separate experiments, five conserved and 2 nonconserved cysteine residues were substituted with alanines by oligonucleotide-directed mutagenesis. The activities of the mutant proteins were determined in the presence of three different reductants: thioredoxin, glutaredoxin, or dithiothreitol. The results indicate two different classes of redox-active cysteines in ribonucleotide reductase: 1) C-terminal Cys-754 and Cys-759 responsible for the interaction with thioredoxin and glutaredoxin; and 2) Cys-225 and Cys-439 located at the nucleotide-binding site. Our classification of redox-active cysteines differs from the location of the active site cysteines in E. coli ribonucleotide reductase suggested previously (Lin, A.-N. I., Ashley, G. W., and Stubbe, J. (1987) Biochemistry 26, 6905-6909). |
| Links | |
| Keywords |
Allosteric Site; Base Sequence; Binding Sites; Cysteine; Dithiothreitol/pharmacology; Escherichia coli/enzymology; Kinetics; Macromolecular Substances; Molecular Sequence Data; Mutation; Oligodeoxyribonucleotides/chemical synthesis; Oxidation-Reduction; Ribonucleotide Reductases/genetics; Ribonucleotide Reductases/metabolism |
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