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193 related items for PubMed ID: 1328209

  • 1. Substitution of manganese for iron in ribonucleotide reductase from Escherichia coli. Spectroscopic and crystallographic characterization.
    Atta M, Nordlund P, Aberg A, Eklund H, Fontecave M.
    J Biol Chem; 1992 Oct 15; 267(29):20682-8. PubMed ID: 1328209
    [Abstract] [Full Text] [Related]

  • 2. Mechanistic implications for the formation of the diiron cluster in ribonucleotide reductase provided by quantitative EPR spectroscopy.
    Pierce BS, Elgren TE, Hendrich MP.
    J Am Chem Soc; 2003 Jul 23; 125(29):8748-59. PubMed ID: 12862469
    [Abstract] [Full Text] [Related]

  • 3. Spectroscopic studies of the iron and manganese reconstituted tyrosyl radical in Bacillus cereus ribonucleotide reductase R2 protein.
    Tomter AB, Zoppellaro G, Bell CB, Barra AL, Andersen NH, Solomon EI, Andersson KK.
    PLoS One; 2012 Jul 23; 7(3):e33436. PubMed ID: 22432022
    [Abstract] [Full Text] [Related]

  • 4. Autocatalytic generation of dopa in the engineered protein R2 F208Y from Escherichia coli ribonucleotide reductase and crystal structure of the dopa-208 protein.
    Aberg A, Ormö M, Nordlund P, Sjöberg BM.
    Biochemistry; 1993 Sep 21; 32(37):9845-50. PubMed ID: 8373782
    [Abstract] [Full Text] [Related]

  • 5. A new tyrosyl radical on Phe208 as ligand to the diiron center in Escherichia coli ribonucleotide reductase, mutant R2-Y122H. Combined x-ray diffraction and EPR/ENDOR studies.
    Kolberg M, Logan DT, Bleifuss G, Pötsch S, Sjöberg BM, Gräslund A, Lubitz W, Lassmann G, Lendzian F.
    J Biol Chem; 2005 Mar 25; 280(12):11233-46. PubMed ID: 15634667
    [Abstract] [Full Text] [Related]

  • 6. Crystal structural studies of changes in the native dinuclear iron center of ribonucleotide reductase protein R2 from mouse.
    Strand KR, Karlsen S, Kolberg M, Røhr AK, Görbitz CH, Andersson KK.
    J Biol Chem; 2004 Nov 05; 279(45):46794-801. PubMed ID: 15322079
    [Abstract] [Full Text] [Related]

  • 7. Metal binding and activity of ribonucleotide reductase protein R2 mutants: conditions for formation of the mixed manganese-iron cofactor.
    Popović-Bijelić A, Voevodskaya N, Domkin V, Thelander L, Gräslund A.
    Biochemistry; 2009 Jul 14; 48(27):6532-9. PubMed ID: 19492792
    [Abstract] [Full Text] [Related]

  • 8. High catalytic activity achieved with a mixed manganese-iron site in protein R2 of Chlamydia ribonucleotide reductase.
    Voevodskaya N, Lendzian F, Ehrenberg A, Gräslund A.
    FEBS Lett; 2007 Jul 24; 581(18):3351-5. PubMed ID: 17601579
    [Abstract] [Full Text] [Related]

  • 9. Chemical flexibility of heterobimetallic Mn/Fe cofactors: R2lox and R2c proteins.
    Kutin Y, Kositzki R, Branca RMM, Srinivas V, Lundin D, Haumann M, Högbom M, Cox N, Griese JJ.
    J Biol Chem; 2019 Nov 29; 294(48):18372-18386. PubMed ID: 31591267
    [Abstract] [Full Text] [Related]

  • 10. The conserved serine 211 is essential for reduction of the dinuclear iron center in protein R2 of Escherichia coli ribonucleotide reductase.
    Regnström K, Aberg A, Ormö M, Sahlin M, Sjöberg BM.
    J Biol Chem; 1994 Mar 04; 269(9):6355-61. PubMed ID: 8119985
    [Abstract] [Full Text] [Related]

  • 11. A tyrosyl-dimanganese coupled spin system is the native metalloradical cofactor of the R2F subunit of the ribonucleotide reductase of Corynebacterium ammoniagenes.
    Cox N, Ogata H, Stolle P, Reijerse E, Auling G, Lubitz W.
    J Am Chem Soc; 2010 Aug 18; 132(32):11197-213. PubMed ID: 20698687
    [Abstract] [Full Text] [Related]

  • 12. 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]

  • 13. Density functional theory study of the manganese-containing ribonucleotide reductase from Chlamydia trachomatis: why manganese is needed in the active complex.
    Roos K, Siegbahn PE.
    Biochemistry; 2009 Mar 10; 48(9):1878-87. PubMed ID: 19220003
    [Abstract] [Full Text] [Related]

  • 14. Tryptophan radicals formed by iron/oxygen reaction with Escherichia coli ribonucleotide reductase protein R2 mutant Y122F.
    Sahlin M, Lassmann G, Pötsch S, Slaby A, Sjöberg BM, Gräslund A.
    J Biol Chem; 1994 Apr 22; 269(16):11699-702. PubMed ID: 8163466
    [Abstract] [Full Text] [Related]

  • 15. 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]

  • 16. Cobalt substitution of mouse R2 ribonucleotide reductase as a model for the reactive diferrous state: spectroscopic and structural evidence for a ferromagnetically coupled dinuclear cobalt cluster.
    Strand KR, Karlsen S, Andersson KK.
    J Biol Chem; 2002 Sep 13; 277(37):34229-38. PubMed ID: 12087093
    [Abstract] [Full Text] [Related]

  • 17. Use of a chemical trigger for electron transfer to characterize a precursor to cluster X in assembly of the iron-radical cofactor of Escherichia coli ribonucleotide reductase.
    Saleh L, Krebs C, Ley BA, Naik S, Huynh BH, Bollinger JM.
    Biochemistry; 2004 May 25; 43(20):5953-64. PubMed ID: 15147179
    [Abstract] [Full Text] [Related]

  • 18. The tyrosyl free radical in ribonucleotide reductase.
    Gräslund A, Sahlin M, Sjöberg BM.
    Environ Health Perspect; 1985 Dec 25; 64():139-49. PubMed ID: 3007085
    [Abstract] [Full Text] [Related]

  • 19. Reduction of the small subunit of Escherichia coli ribonucleotide reductase by hydrazines and hydroxylamines.
    Gerez C, Fontecave M.
    Biochemistry; 1992 Jan 28; 31(3):780-6. PubMed ID: 1310046
    [Abstract] [Full Text] [Related]

  • 20. A manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase.
    Jiang W, Yun D, Saleh L, Barr EW, Xing G, Hoffart LM, Maslak MA, Krebs C, Bollinger JM.
    Science; 2007 May 25; 316(5828):1188-91. PubMed ID: 17525338
    [Abstract] [Full Text] [Related]

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