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219 related items for PubMed ID: 1332707
1. EPR stopped-flow studies of the reaction of the tyrosyl radical of protein R2 from ribonucleotide reductase with hydroxyurea. Lassmann G, Thelander L, Gräslund A. Biochem Biophys Res Commun; 1992 Oct 30; 188(2):879-87. PubMed ID: 1332707 [Abstract] [Full Text] [Related]
2. The tyrosyl free radical in ribonucleotide reductase. Gräslund A, Sahlin M, Sjöberg BM. Environ Health Perspect; 1985 Dec 30; 64():139-49. PubMed ID: 3007085 [Abstract] [Full Text] [Related]
3. Escherichia coli ribonucleotide reductase. Radical susceptibility to hydroxyurea is dependent on the regulatory state of the enzyme. Karlsson M, Sahlin M, Sjöberg BM. J Biol Chem; 1992 Jun 25; 267(18):12622-6. PubMed ID: 1618767 [Abstract] [Full Text] [Related]
4. Structure of the tyrosyl radical in bacteriophage T4-induced ribonucleotide reductase. Sahlin M, Gräslund A, Ehrenberg A, Sjöberg BM. J Biol Chem; 1982 Jan 10; 257(1):366-9. PubMed ID: 6273437 [Abstract] [Full Text] [Related]
5. ESR studies on reactivity of protein-derived tyrosyl radicals formed by prostaglandin H synthase and ribonucleotide reductase. Lassmann G, Curtis J, Liermann B, Mason RP, Eling TE. Arch Biochem Biophys; 1993 Jan 10; 300(1):132-6. PubMed ID: 8380961 [Abstract] [Full Text] [Related]
6. Reduction and loss of the iron center in the reaction of the small subunit of mouse ribonucleotide reductase with hydroxyurea. Nyholm S, Thelander L, Gräslund A. Biochemistry; 1993 Nov 02; 32(43):11569-74. PubMed ID: 8218224 [Abstract] [Full Text] [Related]
7. Reduction of the tyrosyl radical and the iron center in protein R2 of ribonucleotide reductase from mouse, herpes simplex virus and E. coli by p-alkoxyphenols. Pötsch S, Sahlin M, Langelier Y, Gräslund A, Lassmann G. FEBS Lett; 1995 Oct 23; 374(1):95-9. PubMed ID: 7589521 [Abstract] [Full Text] [Related]
8. EPR distance measurements support a model for long-range radical initiation in E. coli ribonucleotide reductase. Bennati M, Robblee JH, Mugnaini V, Stubbe J, Freed JH, Borbat P. J Am Chem Soc; 2005 Nov 02; 127(43):15014-5. PubMed ID: 16248626 [Abstract] [Full Text] [Related]
9. Kinetics of transient radicals in Escherichia coli ribonucleotide reductase. Formation of a new tyrosyl radical in mutant protein R2. Katterle B, Sahlin M, Schmidt PP, Pötsch S, Logan DT, Gräslund A, Sjöberg BM. J Biol Chem; 1997 Apr 18; 272(16):10414-21. PubMed ID: 9099682 [Abstract] [Full Text] [Related]
10. EPR study of the mixed-valent diiron sites in mouse and herpes simplex virus ribonucleotide reductases. Effect of the tyrosyl radical on structure and reactivity of the diferric center. Davydov RM, Davydov A, Ingemarson R, Thelander L, Ehrenberg A, Gräslund A. Biochemistry; 1997 Jul 29; 36(30):9093-100. PubMed ID: 9230041 [Abstract] [Full Text] [Related]
11. The iron-oxygen reconstitution reaction in protein R2-Tyr-177 mutants of mouse ribonucleotide reductase. Epr and electron nuclear double resonance studies on a new transient tryptophan radical. Pötsch S, Lendzian F, Ingemarson R, Hörnberg A, Thelander L, Lubitz W, Lassmann G, Gräslund A. J Biol Chem; 1999 Jun 18; 274(25):17696-704. PubMed ID: 10364210 [Abstract] [Full Text] [Related]
12. Facile electron transfer during formation of cluster X and kinetic competence of X for tyrosyl radical production in protein R2 of ribonucleotide reductase from mouse. Yun D, Krebs C, Gupta GP, Iwig DF, Huynh BH, Bollinger JM. Biochemistry; 2002 Jan 22; 41(3):981-90. PubMed ID: 11790122 [Abstract] [Full Text] [Related]
14. Enzymic modification of a tyrosine residue to a stable free radical in ribonucleotide reductase. Barlow T, Eliasson R, Platz A, Reichard P, Sjöberg BM. Proc Natl Acad Sci U S A; 1983 Mar 05; 80(6):1492-5. PubMed ID: 6300856 [Abstract] [Full Text] [Related]
15. Ribonucleotide reductase: kinetic methods for demonstrating radical transfer pathway in protein R2 of mouse enzyme in generation of tyrosyl free radical. Gräslund A. Methods Enzymol; 2002 Mar 05; 354():399-414. PubMed ID: 12418242 [No Abstract] [Full Text] [Related]
16. Addition of oxygen to the diiron(II/II) cluster is the slowest step in formation of the tyrosyl radical in the W103Y variant of ribonucleotide reductase protein R2 from mouse. Yun D, Saleh L, García-Serres R, Chicalese BM, An YH, Huynh BH, Bollinger JM. Biochemistry; 2007 Nov 13; 46(45):13067-73. PubMed ID: 17941645 [Abstract] [Full Text] [Related]
17. Reactivity of the tyrosyl radical of Escherichia coli ribonucleotide reductase -- control by the protein. Gerez C, Elleingand E, Kauppi B, Eklund H, Fontecave M. Eur J Biochem; 1997 Oct 15; 249(2):401-7. PubMed ID: 9370346 [Abstract] [Full Text] [Related]
18. Kinetic studies on the reduction of the tyrosyl radical of the R2 subunit of E. coli ribonucleotide reductase. Swarts JC, Aquino MA, Han JY, Lam KY, Sykes AG. Biochim Biophys Acta; 1995 Mar 15; 1247(2):215-24. PubMed ID: 7696311 [Abstract] [Full Text] [Related]
19. New paramagnetic species formed at the expense of the transient tyrosyl radical in mutant protein R2 F208Y of Escherichia coli ribonucleotide reductase. Liu A, Sahlin M, Pötsch S, Sjöberg BM, Gräslund A. Biochem Biophys Res Commun; 1998 May 29; 246(3):740-5. PubMed ID: 9618282 [Abstract] [Full Text] [Related]
20. Effect of the tyrosyl radical on the reduction and structure of the Escherichia coli ribonucleotide reductase protein R2 diferric site as probed by EPR on the mixed-valent state. Davydov R, Sahlin M, Kuprin S, Gräslund A, Ehrenberg A. Biochemistry; 1996 Apr 30; 35(17):5571-6. PubMed ID: 8611548 [Abstract] [Full Text] [Related] Page: [Next] [New Search]