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"Evidence for two different classes of redox-active cysteines in ribonucleotide reductase of Escherichia coli." |
Aberg A, Hahne S, Karlsson M, Larsson A, Ormo M, Ahgren A, Sjoberg BM |
Published July 25, 1989 in J Biol Chem volume 264 .
Pubmed ID: 2663852
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). |
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Last modification of this entry: Oct. 11, 2010
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