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Last modified: 16 April 1999

Bibliography on structural studies of ribonucleotide reductase R2­type proteins

  1. Ai, J., Broadwater, J.A., Loehr, T.M., Sanders­Loehr, J. and Fox, B.G. (1997) Azide adducts of stearoyl­ACP desaturase: A model for µ­1,2 bridging by dioxygen in the binuclear iron active site. J. Biol. Inorg. Chem. 2, 37-45.
  2. Åberg, A., Nordlund, P. and Eklund, H. (1993) Unusual clustering of carboxyl side chains in the core of iron­free ribonucleotide reductase. Nature 361, 276-278.
  3. Åberg, A., Ormö, M., Nordlund, P. and Sjöberg, B.­M. (1993) Autocatalytic generation of Dopa in the engineered protein R2 F208Y from Escherichia coli ribonucleotide reductase and crystal structure of the Dopa­208 protein. Biochemistry 32, 9845-9850.
  4. Allard, P., Barra, A.L., Andersson, K.K., Schmidt, P.P., Atta, M. and Gräslund, A. (1996) Characterization of a new tyrosyl free radical in Salmonella typhimurium ribonucleotide reductase with EPR at 9.45 and 245 GHz. J. Am. Chem. Soc. 118, 895-896.
  5. Andersson, M.E., Högbom, M., Rinaldo­Matthis, A., Andersson, K.K., Sjöberg, B.­M. and Nordlund, P. (1999) The crystal structure of an azide complex of the diferrous R2 subunit of ribonucleotide reductase displays a novel carboxylate shift with important mechanistic implications for diiron­catalyzed oxygen activation. J. Am. Chem. Soc. 121, 2346-2352.
  6. Atkin, C.L., Thelander, L., Reichard, P. and Lang, G. (1973) Iron and free radical in ribonucleotide reductase. Exchange of iron and Mössbauer spectroscopy of the protein B2 subunit of the Escherichia coli enzyme. J. Biol. Chem. 248, 7464-7472.
  7. Atta, M., Nordlund, P., Åberg, A., Eklund, H. and Fontecave, M. (1992) Substitution of manganese for iron in ribonucleotide reductase from Escherichia coli. Spectroscopic and crystallographic characterization. J. Biol. Chem. 267, 20682-20688.
  8. Atta, M., Lamarche, N., Battioni, J.P., Massie, B., Langelier, Y., Mansuy, D. and Fontecave, M. (1993) Escherichia coli and herpes­simplex­virus ribonucleotide reductase R2 subunit. Compared reactivities of the redox centres. Biochem. J. 290, 807-810.
  9. Atta, M., Debäcker, N., Andersson, K.K., Latour, J.­M., Thelander, L. and Gräslund, A. (1996) EPR and multi­field magnetisation of reduced forms of the binuclear iron centre in ribonucleotide reductase from mouse. J. Biol. Inorg. Chem. 1, 210-220.
  10. Backes, G., Sahlin, M., Sjöberg, B.­M., Loehr, T.M. and Sanders­Loehr, J. (1989) Resonance Raman spectroscopy of ribonucleotide reductase. Evidence for a deprotonated tyrosyl radical and photochemistry of the binuclear iron center. Biochemistry 28, 1923-1929.
  11. Barynin, V.V., Vagin, A.A., Melik­Adamyan, W.R., Grebenko, A.I., Khangulov, S.V., Popov, A.N., Adrianova, M.E. and Vainshtein, B.K. (1986) Three­dimensional structure of the T­catalase with a 3 Å resolution. Dokl. Akad. Nauk SSSR 288, 877-880.
  12. Bender, C.J., Rosenzweig, A.C., Lippard, S.J. and Peisach, J. (1994) Nuclear hyperfine coupling of nitrogen in the coordination sphere of the diiron center of methane monooxygenase hydroxylase. J. Biol. Chem. 269, 15993-15998.
  13. Bollinger, J.M., Jr., Edmondson, D.E., Huynh, B.­H., Filley, J., Norton, J.R. and Stubbe, J. (1991) Mechanism of assembly of the tyrosyl radical­dinuclear iron cluster cofactor of ribonucleotide reductase. Science 253, 292-298.
  14. Bollinger, J.M., Jr., Tong, W.H., Ravi, N., Huynh, B.­H., Edmondson, D.E. and Stubbe, J. (1994a) Mechanism of assembly of the tyrosyl radical­diiron(III) cofactor of E. coli ribonucleotide reductase. 2. Kinetics of the excess Fe2+ reaction by optical, EPR, and Mössbauer spectroscopies. J. Am. Chem. Soc. 116, 8015-8023.
  15. Bollinger, J.M., Jr., Tong, W.H., Ravi, N., Huynh, B.­H., Edmondson, D.E. and Stubbe, J. (1994b) Mechanism of assembly of the tyrosyl radical­diiron(III) cofactor of E. coli ribonucleotide reductase. 3. Kinetics of the limiting Fe2+ reaction by optical, EPR, and Mössbauer spectroscopies. J. Am. Chem. Soc. 116, 8024-8032.
  16. Bollinger, J.M., Jr., Tong, W.H., Ravi, N., Huynh, B.­H., Edmondson, D.E. and Stubbe, J. (1995) Use of rapid kinetics methods to study the assembly of the diferric­tyrosyl radical cofactor of E. coli ribonucleotide reductase. Methods Enzymol. 258, 278-303.
  17. Bollinger, J.M., Jr., Chen, S., Parkin, S.E., Mangravite, L.M., Ley, B.A., Edmondson, D.E. and Huynh, B.­H. (1997) Differential iron(II) affinity of the sites of the diiron cluster in protein R2 of Escherichia coli ribonucleotide reductase: Tracking the individual sites through the O2 activation sequence. J. Am. Chem. Soc. 119, 5976-5977.
  18. Bollinger, J.M., Jr., Krebs, C., Vicol, A., Chen, S., Ley, B.A., Edmondson, D.E. and Huynh, B.­H. (1998) Engineering the diiron site of Escherichia coli ribonucleotide reductase protein R2 to accumulate an intermediate similar to Hperoxo, the putative peroxodiiron(III) complex from the methane monooxygenase catalytic cycle. J. Am. Chem. Soc. 120, 1094-1095.
  19. Broadwater, J.A., Ai, J., Loehr, T.M., Sanders­Loehr, J. and Fox, B.G. (1998) Peroxodiferric intermediate of stearoyl­acyl carrier protein delta9 desaturase: Oxidase reactivity during single turnover and implications for the mechanism of desaturation. Biochemistry 37, 14664-14671.
  20. Bunker, G., Petersson, L., Sjöberg, B.­M., Sahlin, M., Chance, M., Chance, B. and Ehrenberg, A. (1987) Extended X­ray absorption fine structure studies on the iron­containing subunit of ribonucleotide reductase from Escherichia coli. Biochemistry 26, 4708-4716.
  21. Burdi, D., Sturgeon, B.E., Tong, W.H., Stubbe, J. and Hoffman, B.M. (1996) Rapid freeze­quench ENDOR of the radical X intermediate of Escherichia coli ribonucleotide reductase using 17O2, H217O, and 2H2O. J. Am. Chem. Soc. 118, 281-282.
  22. Burdi, D., Willems, J.­P., Riggs­Gelasco, P., Antholine, W.E., Stubbe, J. and Hoffman, B.M. (1998) The core structure of X generated in the assembly of the diiron cluster of ribonucleotide reductase: 17O2 and H217O ENDOR. J. Am. Chem. Soc. 120, 12910-12919.
  23. Buzy, A., Millar, A.L., Legros, V., Wilkins, P.C., Dalton, H. and Jennings, K.R. (1998) The hydroxylase component of soluble methane monooxygenase from Methylococcus capsulatus (Bath) exists in several forms as shown by electrospray­ionisation mass spectrometry. Eur. J. Biochem. 254, 602-609.
  24. Coufal, D.E., Tavares, P., Pereira, A.S., Hyunh, B.­H. and Lippard, S.J. (1999) Reactions of nitric oxide with the reduced non­heme diiron center of the soluble methane monooxygenase hydroxylase. Biochemistry 38, 4504-4513.
  25. Covès, J., Le Hir de Fallois, L., Le Pape, L., Décout, J.­L. and Fontecave, M. (1996) Inactivation of Escherichia coli ribonucleotide reductase by 2'­deoxy­2'­mercaptouridine 5'­diphosphate. Electron paramagnetic resonance evidence for a transient protein perthiyl radical. Biochemistry 35, 8595-8602.
  26. Davydov, A., Davydov, R., Gräslund, A., Lipscomb, J.D. and Andersson, K.K. (1997) Radiolytic reduction of methane monooxygenase dinuclear iron cluster at 77 K. EPR evidence for conformational change upon reduction or binding of component B to the diferric state. J. Biol. Chem. 272, 7022-7026.
  27. Davydov, R., Kuprin, S., Gräslund, A. and Ehrenberg, A. (1994) Electron paramagnetic resonance study of the mixed­valent diiron center in Escherichia coli ribonucleotide reductase produced by reduction of radical­free protein R2 at 77 K. J. Am. Chem. Soc. 116, 11120-11128.
  28. Davydov, R., Sahlin, M., Kuprin, S., Gräslund, A. and Ehrenberg, A. (1996) Effect of the tyrosyl radical on the reduction and stucture of the Escherichia coli ribonucleotide reductase protein R2 diferric site as probed by EPR on the mixed­valent state. Biochemistry 35, 5571-5576.
  29. Davydov, R., Valentine, A.M., Komar­Panicucci, S., Hoffman, B.M. and Lippard, S.J. (1999) An EPR study of the dinuclear iron site in the soluble methane monooxygenase from Methylococcus capsulatus (Bath) reduced by one electron at 77 K: The effects of component interactions and the binding of small molecules to the diiron(III) center. Biochemistry 38, 4188-4197.
  30. DeRose, V.J., Liu, K.E., Kurtz, D.M., Jr., Hoffman, B.M. and Lippard, S.J. (1993) Protein ENDOR identification of bridging hydroxide ligands in mixed­valent diiron centers of proteins: methane monooxygenase and semimet azidohemerythrin. J. Am. Chem. Soc. 115, 6440-6441.
  31. DeRose, V.J., Liu, K.E., Lippard, S.J. and Hoffman, B.M. (1996) Investigation of the dinuclear Fe center of methane monooxygenase by advanced paramagnetic resonance techniques: On the geometry of DMSO binding. J. Am. Chem. Soc. 118, 121-134.
  32. Ehrenberg, A. and Reichard, P. (1972) Electron spin resonance of the iron­containing protein B2 from ribonucleotide reductase. J. Biol. Chem. 247, 3485-3488.
  33. Elango, N., Radhakrishnan, R., Froland, W.A., Wallar, B.J., Earhart, C.A., Lipscomb, J.D. and Ohlendorf, D.H. (1997) Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b. Protein Science 6, 556-568.
  34. Elleingand, E., Gerez, C., Un, S., Knüpling, M., Lu, G., Salem, J., Rubin, H., Sauge­Merle, S., Laulhère, J.­P. and Fontecave, M. (1998) Reactivity studies of the tyrosyl radical in ribonucleotide reductase from Mycobacterium tuberculosis and Arabidopsis thaliana. Comparison with Escherichia coli and mouse. Eur. J. Biochem. 258, 485-490.
  35. Eriksson, M., Jordan, A. and Eklund, H. (1998) Structure of Salmonella typhimurium nrdF ribonucleotide reductase in its oxidized and reduced forms. Biochemistry 37, 13359-13369.
  36. Fontecave, M., Gerez, C., Atta, M. and Jeunet, A. (1990) High valent iron oxo intermediates might be involved during activation of ribonucleotide reductase: single oxygen atom donors generate the tyrosyl radical. Biochem. Biophys. Res. Commun. 168, 659-664.
  37. Fox, B.G., Surerus, K.K., Münck, E. and Lipscomb, J.D. (1988) Evidence for a µ­oxo­bridged binuclear iron cluster in the hydroxylase component of methane monooxygenase. Mössbauer and EPR studies. J. Biol. Chem. 263, 10553-10556.
  38. Fox, B.G., Hendrich, M.P., Surerus, K.K., Andersson, K.K., Froland, W.A., Lipscomb, J.D. and Münck, E. (1993a) Mössbauer, EPR, and ENDOR studies of the hydroxylase and reductase components of methane monooxygenase from Methylosinus trichosporium OB3b. J. Am. Chem. Soc. 115, 3688-3701.
  39. Fox, B.G., Shanklin, J., Somerville, C. and Münck, E. (1993b) Stearoyl­acyl carrier protein delta9­desaturase from Ricinus communis is a diiron­oxo protein. Proc. Natl. Acad. Sci. USA 90, 2486-2490.
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  41. Froland, W.A., Dyer, D.H., Radhakrishnan, R., Earhart, C.A., Lipscomb, J.D. and Ohlendorf, D.H. (1994) Preliminary crystallographic analysis of methane mono­oxygenase hydroxylase from Methylosinus trichosporium OB3b. J. Mol. Biol. 236, 379-381.
  42. Gallagher, S.C., Cammack, R. and Dalton, H. (1997) Alkene monooxygenase from Nocardia corallina B­276 is a member of the class of dinuclear iron proteins capable of stereospecific epoxygenation reactions. Eur. J. Biochem. 247, 635-641.
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  44. Hamman, S., Atta, M., Ehrenberg, A., Wilkins, P.C., Dalton, H., Beguin, C. and Fontecave, M. (1993) 19F NMR study of the interaction of fluoride ion with ribonucleotide reductase and methane monooxygenase. Biochem. Biophys. Res. Commun. 195, 594-599.
  45. Han, J.­Y., Gräslund, A., Thelander, L. and Sykes, A.G. (1997) Kinetic studies on the reduction of the R2 subunit of mouse ribonucleotide reductase with hydroxyurea, hydrazine, phenylhydrazine and hydroxylamine. J. Biol. Inorg. Chem. 2, 287-294.
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  48. Hoganson, C.W., Sahlin, M., Sjöberg, B.­M. and Babcock, G.T. (1996) Electron magnetic resonance of the tyrosyl radical in ribonucleotide reductase from Escherichia coli. J. Am. Chem. Soc. 118, 4672-4679.
  49. Ivancich, A., Barynin, V.V. and Zimmermann, J.L. (1995) Pulsed EPR studies of the binuclear Mn(III)Mn(IV) center in catalase from Thermus thermophilus. Biochemistry 34, 6628-6639.
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  51. Kauffmann, K.E., Popescu, C.V., Dong, Y., Lipscomb, J.D., Que, L., Jr. and Münck, E. (1998) Mössbauer evidence for antisymmetric exchange in a diferric synthetic complex and diferric methane monooxygenase. J. Am. Chem. Soc. 120, 8739-8746.
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Reviews on ribonucleotide reductase R2­type proteins