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245 related items for PubMed ID: 16482244
1. PELDOR study on the tyrosyl radicals in the R2 protein of mouse ribonucleotide reductase. Biglino D, Schmidt PP, Reijerse EJ, Lubitz W. Phys Chem Chem Phys; 2006 Jan 07; 8(1):58-62. PubMed ID: 16482244 [Abstract] [Full Text] [Related]
2. Pulsed ELDOR spectroscopy measures the distance between the two tyrosyl dadicals in the R2 subunit of the E. coli ribonucleotide reductase. Bennati M, Weber A, Antonic J, Perlstein DL, Robblee J, Stubbe J. J Am Chem Soc; 2003 Dec 10; 125(49):14988-9. PubMed ID: 14653724 [Abstract] [Full Text] [Related]
3. Structure of the tyrosyl biradical in mouse R2 ribonucleotide reductase from high-field PELDOR. Denysenkov VP, Biglino D, Lubitz W, Prisner TF, Bennati M. Angew Chem Int Ed Engl; 2008 Dec 10; 47(7):1224-7. PubMed ID: 18172843 [No Abstract] [Full Text] [Related]
4. High-field pulsed electron-electron double resonance spectroscopy to determine the orientation of the tyrosyl radicals in ribonucleotide reductase. Denysenkov VP, Prisner TF, Stubbe J, Bennati M. Proc Natl Acad Sci U S A; 2006 Sep 05; 103(36):13386-90. PubMed ID: 16938868 [Abstract] [Full Text] [Related]
5. 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]
6. Pulsed 180-GHz EPR/ENDOR/PELDOR spectroscopy. Hertel MM, Denysenkov VP, Bennati M, Prisner TF. Magn Reson Chem; 2005 Nov 29; 43 Spec no.():S248-55. PubMed ID: 16235223 [Abstract] [Full Text] [Related]
7. 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]
9. PELDOR spectroscopy with DOPA-beta2 and NH2Y-alpha2s: distance measurements between residues involved in the radical propagation pathway of E. coli ribonucleotide reductase. Seyedsayamdost MR, Chan CT, Mugnaini V, Stubbe J, Bennati M. J Am Chem Soc; 2007 Dec 26; 129(51):15748-9. PubMed ID: 18047343 [Abstract] [Full Text] [Related]
11. Loss of the tyrosyl radical in mouse ribonucleotide reductase by (-)-epicatechin. Schroeder P, Voevodskaya N, Klotz LO, Brenneisen P, Gräslund A, Sies H. Biochem Biophys Res Commun; 2005 Jan 21; 326(3):614-7. PubMed ID: 15596143 [Abstract] [Full Text] [Related]
14. Peroxyl adduct radicals formed in the iron/oxygen reconstitution reaction of mutant ribonucleotide reductase R2 proteins from Escherichia coli. Sahlin M, Cho KB, Pötsch S, Lytton SD, Huque Y, Gunther MR, Sjöberg BM, Mason RP, Gräslund A. J Biol Inorg Chem; 2002 Jan 21; 7(1-2):74-82. PubMed ID: 11862543 [Abstract] [Full Text] [Related]
15. 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]
16. 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]
18. Site-specific replacement of Y356 with 3,4-dihydroxyphenylalanine in the beta2 subunit of E. coli ribonucleotide reductase. Seyedsayamdost MR, Stubbe J. J Am Chem Soc; 2006 Mar 01; 128(8):2522-3. PubMed ID: 16492021 [Abstract] [Full Text] [Related]
19. 2,3-difluorotyrosine at position 356 of ribonucleotide reductase R2: a probe of long-range proton-coupled electron transfer. Yee CS, Chang MC, Ge J, Nocera DG, Stubbe J. J Am Chem Soc; 2003 Sep 03; 125(35):10506-7. PubMed ID: 12940718 [Abstract] [Full Text] [Related]