Revealing the position of the substrate in nickel superoxide dismutase: A model study

Angewandte Chemie - International Edition

Volumn 50, Issue 13, 2011, Pages 2946-2950

  Tietze, Daniel ^a   Voigt, Stephan ^a   Mollenhauer, Doreen ^c   Tischler, Marco ^a   Imhof, Diana ^b   Gutmann, Torsten ^a   González, Leticia ^b   Ohlenschläger, Oliver ^d   Breitzke, Hergen ^a   Görlach, Matthias ^d   Buntkowsky, Gerd ^a  

^a DARMSTADT UNIVERSITY OF TECHNOLOGY   (Germany)

^b FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

^c FREIE UNIVERSITÄT BERLIN   (Germany)

^d FRITZ LIPMANN INSTITUTE   (Germany)

Author keywords

Density functional calculations; Enzyme catalysis; Solid state NMR spectroscopy; Substrate binding; Superoxide dismutase

Indexed keywords

DENSITY-FUNCTIONAL CALCULATIONS; ENZYME CATALYSIS; SOLID-STATE NMR SPECTROSCOPY; SUBSTRATE BINDING; SUPEROXIDE DISMUTASE;

CATALYSIS; CYANIDES; DENSITY FUNCTIONAL THEORY; ENZYMES; MOLECULES; OXYGEN; SOLID STATE PHYSICS; SUBSTRATES;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

NICKEL; ORGANOMETALLIC COMPOUND; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; STEREOISOMERISM;

MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR CONFORMATION; NICKEL; ORGANOMETALLIC COMPOUNDS; REACTIVE OXYGEN SPECIES; STEREOISOMERISM; SUPEROXIDE DISMUTASE;

EID: 79952663832     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201005027     Document Type: Article

References (41)

1. a) J. J. Haddad, Cell. Signalling 2002, 14, 879-897;
2. b) J. M. Mates, J. M. Segura, C. Perez-Gomez, R. Rosado, L. Olalla, M. Blanca, F. M. Sanchez-Jimenez, Blood Cells Mol. Dis. 1999, 25, 103-109.
3. J. S. Valentine, D. L. Wertz, T. J. Lyons, L.-L. Liou, J. J. Goto, E. B. Gralla, Curr. Opin. Chem. Biol. 1998, 2, 253-262.
4. a) D. P. Barondeau, C. J. Kassmann, C. K. Bruns, J. A. Tainer, E. D. Getzoff, Biochemistry 2004, 43, 8038-8047;
5. b) K. P. Neupane, K. Gearty, A. Francis, J. Shearer, J. Am. Chem. Soc. 2007, 129, 14605-14618 ;
6. c) M. Schmidt, S. Zahn, M. Carella, O. Ohlenschläger, M. Görlach, E. Kothe, J. Weston, ChemBioChem 2008, 9, 2135-2146.
7. a) P. A. Bryngelson, S. E. Arobo, J. L. Pinkham, D. E. Cabelli, M. J. Maroney, J. Am. Chem. Soc. 2004, 126, 460-461;
8. b) S. B. Choudhury, J.W. Lee, G. Davidson, Y. I. Yim, K. Bose, M. L. Sharma, S. O. Kang, D. E. Cabelli, M. J. Maroney, Biochemistry 1999, 38, 3744-3752;
9. c) M. Cox, D. Nelson, A. Lehninger in Lehninger Biochemie, Vol. 3, Springer, Heidelberg, 2001.
10. a) T. Eitinger, J. Bacteriol. 2004, 186, 7821-7825 ;
11. b) A. Schmidt, G. Haferburg, E. Kothe, J. Basic Microbiol. 2007, 47, 56-62;
12. c) H. D. Youn, E. J. Kim, J. H. Roe, Y. C. Hah, S. O. Kang, Biochem. J. 1996, 318, 889-896.
13. J. Wuerges, J. W. Lee, Y. I. Yim, H. S. Yim, S. O. Kang, K. D. Carugo, Proc. Natl. Acad. Sci. USA 2004, 101, 8569-8574.
14. a) A. T. Fiedler, P. A. Bryngelson, M. J. Maroney, T. C. Brunold, J. Am. Chem. Soc. 2005, 127, 5449;
15. b) T. A. Jackson, T. C. Brunold, Acc. Chem. Res. 2004, 37, 461;
16. c) J. Wuerges, J. W. Lee, S. O. Kang, K. D. Carugo, Acta Crystallogr. Sect. D 2002, 58, 1220.
17. a) K. P. Neupane, J. Shearer, Inorg. Chem. 2006, 45, 10552;
18. b) M. Schmidt, Friedrich-Schiller-Universität Jena, 2007;
19. c) J. Shearer, A. Dehestani, F. Abanda, Inorg. Chem. 2008, 47, 2649;
20. d) J. Shearer, L. M. Long, Inorg. Chem. 2006, 45, 2358;
21. e) J. Shearer, N. F. Zhao, Inorg. Chem. 2006, 45, 9637.
22. D. Tietze, H. Breitzke, D. Imhof, E. Kothe, J. Weston, G. Buntkowsky, Chem. Eur. J. 2009, 15, 517-523.
23. G. Rotilio, Finazzia. A, Calabres. L, F. Bossa, Guerrier. P, B. Mondovi, Biochemistry 1971, 10, 616-621.
24. a) J. A. Fee, J. Peisach, W. B. Mims, J. Biol. Chem. 1981, 256, 1910-1914;
25. b) G. Rotilio, B. Mondovi, L. Morpurgo, L. Calabres, C. Giovagno, Biochemistry 1972, 11, 2187-2192;
26. c) H. L. Van Camp, R. H. Sands, J. A. Fee, Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. 1982, 704, 75-89.
27. J. Han, N. J. Blackburn, T. M. Loehr, Inorg. Chem. 1992, 31, 3223-3229.
28. K. D. Carugo, A. Battistoni, M. T. Carri, F. Polticelli, A. Desideri, G. Rotilio, A. Coda, M. Bolognesi, FEBS Lett. 1994, 349, 93-98.
29. J. A. Tainer, E. D. Getzoff, J. S. Richardson, D. C. Richardson, Nature 1983, 306, 284-287.
30. D. S. Shin, M. DiDonato, D. P. Barondeau, G. L. Hura, C. Hitomi, J. A. Berglund, E. D. Getzoff, S. C. Cary, J. A. Tainer, J. Mol. Biol. 2009, 385, 1534-1555.
31. a) P. Carloni, P. E. Bloechl, M. Parrinello, J. Phys. Chem. 1995, 99, 1338-1348;
32. b) M. Rosi, A. Sgamellotti, F. Tarantelli, I. Bertini, C. Luchinat, Inorg. Chem. 1986, 25, 1005-1008.
33. a) T. Gullion, Concepts Magn. Reson. 1998, 10, 277-289;
34. b) T. Gullion, J. Schaefer, J. Magn. Reson. 1989, 81, 196-200;
35. c) D. D. Laws, H. M. L. Bitter, A. Jerschow, Angew. Chem. 2002, 114, 3224;
36. Angew. Chem. Int. Ed. 2002, 41, 3096.
37. T. Emmler, I. Ayala, D. Silverman, S. Hafner, A. S. Galstyan, E.W. Knapp, G. Buntkowsky, Solid State Nucl. Magn. Reson. 2008, 34, 6-13.
38. K. Wüthrich, NMR of Proteins and Nucleic Acids, Wiley, New York, 1986.
39. R.W. Herbst, A. Guce, P. A. Bryngelson, K. A. Higgins, K. C. Ryan, D. E. Cabelli, S. C. Garman, M. J. Maroney, Biochemistry 2009, 48, 3354-3369.
40. K. T. Mueller, J. Magn. Reson. Ser. A 1995, 113, 81-93.
41. C. Bartels, T. H. Xia, M. Billeter, P. Guntert, K. Wüthrich, J. Biomol. NMR 1995, 6, 1-10.