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Biochem Biophys Res Commun. 1991 Aug 30;179(1):442-8.

Inactivation of ribonucleotide reductase by nitric oxide.

Author information

1
URA CNRS 1116, Université Paris-Sud, Orsay, France.

Abstract

Ribonucleotide reductase has been demonstrated to be inhibited by NO synthase product(s). The experiments reported here show that nitric oxide generated from sodium nitroprusside, S-nitrosoglutathione and the sydnonimine SIN-1 inhibits ribonucleotide reductase activity present in cytosolic extracts of TA3 mammary tumor cells. Stable derivatives of these nitric oxide donors were either inactive or much less inhibitory. EPR experiments show that the tyrosyl radical of the small subunit of E. Coli or mammalian ribonucleotide reductase is efficiently scavenged by these NO donors.

PMID:
1652957
DOI:
10.1016/0006-291x(91)91390-x
[Indexed for MEDLINE]

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