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103 related items for PubMed ID: 11001091
1. EPR evidence of two structurally different diferric sites in Mycobacterium tuberculosis R2-2 ribonucleotide reductase protein. Davydov A, Liu A, Gräslund A. J Inorg Biochem; 2000 Jul 01; 80(3-4):213-8. PubMed ID: 11001091 [Abstract] [Full Text] [Related]
2. 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]
3. The tyrosyl free radical of recombinant ribonucleotide reductase from Mycobacterium tuberculosis is located in a rigid hydrophobic pocket. Liu A, Pötsch S, Davydov A, Barra AL, Rubin H, Gräslund A. Biochemistry; 1998 Nov 17; 37(46):16369-77. PubMed ID: 9819229 [Abstract] [Full Text] [Related]
4. 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]
5. Effect of substrate on the diiron(III) site in stearoyl acyl carrier protein delta 9-desaturase as disclosed by cryoreduction electron paramagnetic resonance/electron nuclear double resonance spectroscopy. Davydov R, Behrouzian B, Smoukov S, Stubbe J, Hoffman BM, Shanklin J. Biochemistry; 2005 Feb 01; 44(4):1309-15. PubMed ID: 15667224 [Abstract] [Full Text] [Related]
6. EPR properties of mixed-valent mu-oxo and mu-hydroxo dinuclear iron complexes produced by radiolytic reduction at 77 K. Davydov RM, Smieja J, Dikanov SA, Zang Y, Que L, Bowman MK. J Biol Inorg Chem; 1999 Jun 01; 4(3):292-301. PubMed ID: 10439074 [Abstract] [Full Text] [Related]
7. EPR studies on a stable sulfinyl radical observed in the iron-oxygen-reconstituted Y177F/I263C protein R2 double mutant of ribonucleotide reductase from mouse. Adrait A, Ohrström M, Barra AL, Thelander L, Gräslund A. Biochemistry; 2002 May 21; 41(20):6510-6. PubMed ID: 12009915 [Abstract] [Full Text] [Related]
8. A stable FeIII-FeIV replacement of tyrosyl radical in a class I ribonucleotide reductase. Voevodskaya N, Lendzian F, Gräslund A. Biochem Biophys Res Commun; 2005 May 20; 330(4):1213-6. PubMed ID: 15823572 [Abstract] [Full Text] [Related]
11. Orientation of the tyrosyl radical in Salmonella typhimurium class Ib ribonucleotide reductase determined by high field EPR of R2F single crystals. Galander M, Uppsten M, Uhlin U, Lendzian F. J Biol Chem; 2006 Oct 20; 281(42):31743-52. PubMed ID: 16854982 [Abstract] [Full Text] [Related]
12. Regeneration of the tyrosyl radical in native or p-butoxyphenol-treated mouse ribonucleotide reductase R2 protein. Davydov A, Gräslund A. Biochem Biophys Res Commun; 1999 May 10; 258(2):322-5. PubMed ID: 10329385 [Abstract] [Full Text] [Related]
17. Reversible red-ox reactions of the diiron site in the mouse ribonucleotide reductase R2 protein. Davydov A, Schmidt PP, Gräslund A. Biochem Biophys Res Commun; 1996 Feb 06; 219(1):213-8. PubMed ID: 8619810 [Abstract] [Full Text] [Related]
19. Structure and interactions of amino acid radicals in class I ribonucleotide reductase studied by ENDOR and high-field EPR spectroscopy. Lendzian F. Biochim Biophys Acta; 2005 Feb 25; 1707(1):67-90. PubMed ID: 15721607 [Abstract] [Full Text] [Related]