دورية أكاديمية
Compounds with capacity to quench the tyrosyl radical in Pseudomonas aeruginosa ribonucleotide reductase.
| العنوان: | Compounds with capacity to quench the tyrosyl radical in Pseudomonas aeruginosa ribonucleotide reductase. |
|---|---|
| المؤلفون: | Berggren G; Department of Chemistry, Ångström Laboratory, Uppsala University, Uppsala, Sweden. gustav.berggren@kemi.uu.se., Sahlin M; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden., Crona M; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.; Swedish Orphan Biovitrum AB, Stockholm, Sweden., Tholander F; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden., Sjöberg BM; Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden. britt-marie.sjoberg@dbb.su.se. |
| المصدر: | Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry [J Biol Inorg Chem] 2019 Sep; Vol. 24 (6), pp. 841-848. Date of Electronic Publication: 2019 Jun 20. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Springer Country of Publication: Germany NLM ID: 9616326 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1432-1327 (Electronic) Linking ISSN: 09498257 NLM ISO Abbreviation: J Biol Inorg Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Berlin : Springer, c1996- |
| مواضيع طبية MeSH: | Free Radicals/*chemistry , Free Radicals/*metabolism , Pseudomonas aeruginosa/*enzymology , Ribonucleotide Reductases/*metabolism , Tyrosine/*chemistry , Tyrosine/*metabolism, Pseudomonas aeruginosa/genetics ; Pseudomonas aeruginosa/metabolism ; Ribonucleotide Reductases/genetics |
| مستخلص: | Ribonucleotide reductase (RNR) has been extensively probed as a target enzyme in the search for selective antibiotics. Here we report on the mechanism of inhibition of nine compounds, serving as representative examples of three different inhibitor classes previously identified by us to efficiently inhibit RNR. The interaction between the inhibitors and Pseudomonas aeruginosa RNR was elucidated using a combination of electron paramagnetic resonance spectroscopy and thermal shift analysis. All nine inhibitors were found to efficiently quench the tyrosyl radical present in RNR, required for catalysis. Three different mechanisms of radical quenching were identified, and shown to depend on reduction potential of the assay solution and quaternary structure of the protein complex. These results form a good foundation for further development of P. aeruginosa selective antibiotics. Moreover, this study underscores the complex nature of RNR inhibition and the need for detailed spectroscopic studies to unravel the mechanism of RNR inhibitors. |
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| معلومات مُعتمدة: | 2016-01920 International Vetenskapsrådet; 621-2014-5670 International Vetenskapsrådet |
| فهرسة مساهمة: | Keywords: Diferric-oxo center; EPR; Inhibitors; Radicals; Ribonucleotide reductase; Thermal shift analysis |
| المشرفين على المادة: | 0 (Free Radicals) 42HK56048U (Tyrosine) EC 1.17.4.- (Ribonucleotide Reductases) |
| تواريخ الأحداث: | Date Created: 20190621 Date Completed: 20200713 Latest Revision: 20200713 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC6754346 |
| DOI: | 10.1007/s00775-019-01679-w |
| PMID: | 31218442 |
| قاعدة البيانات: | MEDLINE |
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