دورية أكاديمية
ESR studies on reactivity of protein-derived tyrosyl radicals formed by prostaglandin H synthase and ribonucleotide reductase.
| العنوان: | ESR studies on reactivity of protein-derived tyrosyl radicals formed by prostaglandin H synthase and ribonucleotide reductase. |
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| المؤلفون: | Lassmann G; Max-Delbrück-Center of Molecular Medicine, Berlin-Buch, Germany., Curtis J, Liermann B, Mason RP, Eling TE |
| المصدر: | Archives of biochemistry and biophysics [Arch Biochem Biophys] 1993 Jan; Vol. 300 (1), pp. 132-6. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Country of Publication: United States NLM ID: 0372430 Publication Model: Print Cited Medium: Print ISSN: 0003-9861 (Print) Linking ISSN: 00039861 NLM ISO Abbreviation: Arch Biochem Biophys Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: <2000- > : San Diego, CA : Elsevier Original Publication: New York, NY : Academic Press |
| مواضيع طبية MeSH: | Cyclooxygenase Inhibitors/*pharmacology , Prostaglandin-Endoperoxide Synthases/*metabolism , Ribonucleotide Reductases/*metabolism , Tyrosine/*metabolism, Animals ; Anisoles/pharmacology ; Carcinoma, Ehrlich Tumor/enzymology ; Electron Spin Resonance Spectroscopy/methods ; Eugenol/pharmacology ; Free Radicals/metabolism ; Hydroxyurea/pharmacology ; Indoleacetic Acids/pharmacology ; Indomethacin/pharmacology ; Kinetics ; Male ; Mice ; Prostaglandin-Endoperoxide Synthases/chemistry ; Ribonucleotide Reductases/chemistry ; Seminal Vesicles/enzymology ; Sheep |
| مستخلص: | Using ESR spectroscopy, the ability of enzyme inhibitors to quench protein-derived tyrosyl radicals was studied in two different enzymes, prostaglandin H synthase and ribonucleotide reductase. The prostaglandin H synthase inhibitors indomethacin, eugenol, and MK-410 effectively prevent the formation of tyrosyl radicals during the oxidation of arachidonic acid by prostaglandin H synthase from ram seminal vesicles. A direct reaction with preformed tyrosyl radicals was observed only with eugenol. The other prostaglandin H synthase inhibitors were ineffective. The ribonucleotide reductase inhibitors hydroxyurea and 4-hydroxyanisole, which effectively inactivate the tyrosyl radical in the active site of ribonucleotide reductase present in tumor cells, exhibit a different reactivity with tyrosyl radicals formed by prostaglandin H synthase. Hydroxyurea quenches preformed tyrosyl radicals in prostaglandin H synthase weakly, whereas 4-hydroxyanisole does not quench tyrosyl radicals in prostaglandin H synthase at all. Eugenol, which quenches preformed prostaglandin H synthase-derived tyrosyl radicals, also quenches the tyrosyl radical in ribonucleotide reductase. The results suggest that the reactivity of protein-linked tyrosyl radicals in ribonucleotide reductase and those formed during prostaglandin H synthase catalysis are very different and have unrelated roles in enzyme catalysis. |
| المشرفين على المادة: | 0 (Anisoles) 0 (Cyclooxygenase Inhibitors) 0 (Free Radicals) 0 (Indoleacetic Acids) 3T8H1794QW (Eugenol) 40738-05-4 (MK 410) 42HK56048U (Tyrosine) 6HT8U7K3AM (mequinol) EC 1.14.99.1 (Prostaglandin-Endoperoxide Synthases) EC 1.17.4.- (Ribonucleotide Reductases) X6Q56QN5QC (Hydroxyurea) XXE1CET956 (Indomethacin) |
| تواريخ الأحداث: | Date Created: 19930101 Date Completed: 19930223 Latest Revision: 20131121 |
| رمز التحديث: | 20240627 |
| DOI: | 10.1006/abbi.1993.1018 |
| PMID: | 8380961 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 0003-9861 |
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| DOI: | 10.1006/abbi.1993.1018 |