1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure

Journal of Inorganic Biochemistry

Volumn 103, Issue 1, 2009, Pages 10-19

  Ma, Li Hua ^a   Liu, Yangzhong ^a   Zhang, Xuhong ^b   Yoshida, Tadashi ^b   La Mar, Gerd N ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b YAMAGATA UNIVERSITY   (Japan)

Author keywords

Azide complex; Dipolar shifts; H bonding; Magnetic anisotropies; Neisseria meningitidis heme oxygenase

Indexed keywords

AZIDE; CYANIDE; HEME OXYGENASE; BACTERIAL PROTEIN; GRANULOCYTE COLONY STIMULATING FACTOR; HEMIN; HEMO PROTEIN, NEISSERIA MENINGITIDIS; JAK2 PROTEIN, RAT; JANUS KINASE 2; LIGAND; STAT PROTEIN;

ANISOTROPY; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME STRUCTURE; HYDROGEN BOND; MOLECULAR INTERACTION; NEISSERIA MENINGITIDIS; NONHUMAN; PH MEASUREMENT; PROTON NUCLEAR MAGNETIC RESONANCE; ANIMAL; APOPTOSIS; CHEMISTRY; CORONARY ARTERY DISEASE; DISEASE MODEL; ENZYMOLOGY; FAT EMBOLISM; HEART MUSCLE; MALE; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PATHOLOGY; PROTEIN CONFORMATION; RAT; SIGNAL TRANSDUCTION; SPRAGUE DAWLEY RAT;

NEISSERIA MENINGITIDIS;

ANIMALS; APOPTOSIS; AZIDES; BACTERIAL PROTEINS; CORONARY ARTERY DISEASE; CYANIDES; DISEASE MODELS, ANIMAL; EMBOLISM, CHOLESTEROL; GRANULOCYTE COLONY-STIMULATING FACTOR; HEME OXYGENASE (DECYCLIZING); HEMIN; HYDROGEN BONDING; JANUS KINASE 2; LIGANDS; MALE; MYOCARDIUM; NEISSERIA MENINGITIDIS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; RATS; RATS, SPRAGUE-DAWLEY; SIGNAL TRANSDUCTION; STAT TRANSCRIPTION FACTORS;

EID: 56649088140     PISSN: 01620134     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jinorgbio.2008.08.012     Document Type: Article

References (59)

1. Tenhunen R., Marver H.S., and Schmid R. J. Biol. Chem. 244 (1969) 6388-6394
2. Yoshida T., and Migita C.T. J. Inorg. Biochem. 82 (2000) 33-41
3. Wilks A. Antioxid. Redox Sig. 4 (2002) 603-614
4. Ortiz de Montellano P.R., and Auclair K. In: Kadish K.M., Smith K.M., and Guilard R. (Eds). The Porphryin Handbook. Heme Oxygenase Structure and Mechanism vol. 12 (2003), Elsevier Science, San Diego, CA 175-202
5. Rivera M., and Zeng Y. J. Inorg. Biochem. 99 (2005) 337-354
6. Unno M., Matsui T., and Ikeda-Saito M. Nat. Prod. Rep. 24 (2007) 553-570
7. Schuller D.J., Wilks A., Ortiz de Montellano P.R., and Poulos T.L. Nat. Struct. Biol. 6 (1999) 860-867
8. Lad L., Wang J., Li H., Friedman J., Bhaskar B., Ortiz de Montellano P.R., and Poulos T.L. J. Mol. Biol. 330 (2003) 527-538
9. Li Y., Syvitski R.T., Auclair K., Wilks A., Ortiz de Montellano P.R., and La Mar G.N. J. Biol. Chem. 277 (2002) 33018-33031
10. Li Y., Syvitski R.T., Auclair K., Ortiz de Montellano P.R., and La Mar G.N. J. Am. Chem. Soc. 125 (2003) 13392-13403
11. Syvitski R.T., Li Y., Auclair K., Ortiz de Montellano P.R., and La Mar G.N. J. Am. Chem. Soc. 124 (2002) 14296-14297
12. Ogura H., Evans J.P., Ortiz de Montellano P.R., and La Mar G.N. Biochemistry 47 (2008) 421-430
13. Sugishima M., Sakamoto H., Higashimoto Y., Omata Y., Hayashi S., Noguchi M., and Fukuyama K. J. Biol. Chem. (2002) 45086-45090
14. Sugishima M., Sakamoto H., Higashimoto Y., Noguchi M., and Fukuyama K. J. Biol. Chem. 278 (2003) 32352-32358
15. Sugishima M., Migita C.T., Zhang X., Yoshida T., and Fukuyama K. Eur. J. Biochem. 271 (2004) 4517-4525
16. Li Y., Syvitski R.T., Auclair K., Ortiz de Montellano P.R., and La Mar G.N. J. Biol. Chem. 279 (2003) 10195-10205
17. Chu G.C., Tomita T., Sönnichsen F.D., Yoshida T., and Ikeda-Saito M. J. Biol. Chem. 274 (1999) 24490-24496
18. Schuller D.J., Zhu W., Stojiljkovic I., Wilks A., and Poulos T.L. Biochemistry 40 (2001) 11552-11558
19. Friedman J.M., Lad L., Deshmukh R., Li H.Y., Wilks A., and Poulos T.L. J. Biol. Chem. 278 (2003) 34654-34659
20. Liu Y., Zhang X., Yoshida T., and La Mar G.N. Biochemistry 43 (2004) 10112-10126
21. Liu Y., Zhang X., Yoshida T., and La Mar G.N. J. Am. Chem. Soc. 127 (2005) 6409-6422
22. Liu Y., Ma L.-H., Satterlee J.D., Zhang X., Yoshida T., and La Mar G.N. Biochemistry 45 (2006) 3875-3886
23. Ma L.-H., Liu Y., Zhang X., Yoshida T., and La Mar G.N. J. Am. Chem. Soc. 128 (2006) 6657-6668
24. Liu Y., Ma L.-H., Zhang X., Yoshida T., Satterlee J.D., and La Mar G.N. Biochemistry 45 (2006) 13875-13888
25. Zeng Y., Caignan G.A., Bunce R.A., Rodriguez J.C., Wilks A., and Rivera M. J. Am. Chem. Soc. 127 (2005) 9794-9807
26. Deshmukh R., Zeng Y., Furci L.M., Huang H.-w., Morgan B.N., Sander S., Alontaga A.Y., Bunce R.A., Moenne-Loccoz P., Rivera M., and Wilks A. Biochemistry 44 (2005) 13713-13723
27. Unno M., Matsui T., Chu G.C., Coutoure M., Yoshida T., Rousseau D.L., Olson J.S., and Ikeda-Saito M. J. Biol. Chem. 279 (2004) 21055-21061
28. Zeng Y., Deshmukh R., Caignan G.A., Bunce R.A., Rivera M., and Wilks A. Biochemistry 43 (2004) 5222-5238
29. Friedman J., Lad L., Li H., Wilks A., and Poulos T.L. Biochemistry 43 (2004) 5239-5245
30. Caignan G.A., Deshmukh R., Wilks A., Zeng Y., Huang H.-W., Moenne-Loccoz P., Bunce R.A., Eastman M.A., and Rivera M. J. Am. Chem. Soc. 124 (2002) 14879-14892
31. Caignan G.A., Deshmukh R., Zeng Y., Wilks A., Bunce R.A., and Rivera M. J. Am. Chem. Soc. 125 (2003) 11842-11852
32. Rodriguez J.C., Wilks A., and Rivera M. Biochemistry 45 (2006) 4578-4592
33. Davydov R.M., Yoshida T., Ikeda-Saito M., and Hoffman B.M. J. Am. Chem. Soc. 121 (1999) 10656-10657
34. Li Y., Syvitski R.T., Chu G.C., Ikeda-Saito M., and La Mar G.N. J. Biol. Chem. 279 (2003) 6651-6663
35. Liu Y., Ma L.-H., Zhang X., Yoshida T., Langry K.C., Smith K.M., and La Mar G.N. J. Am. Chem. Soc. 128 (2006) 6391-6399
36. Koenigs Lightning L., Huang H.-W., Moënne-Loccoz P., Loehr T.M., Schuller D.J., Poulos T.L., and Ortiz de Montellano P.R. J. Biol. Chem. 276 (2001) 10612-10619
37. Fujii H., Zhang X., Tomita T., Ikeda-Saito M., and Yoshida T. J. Am. Chem. Soc. 123 (2001) 6475-6484
38. Matsui T., Furukawa M., Unno M., Tomita T., and Ikeda-Saito M. J. Biol. Chem. 280 (2005) 2981-2989
39. La Mar G.N., Satterlee J.D., and de Ropp J.S. In: Kadish K.M., Smith K.M., and Guilard R. (Eds). The Porphyrins Handbook. NMR of Hemoproteins vol. 5 (2000), Academic Press, San Diego 185-298
40. Sugishima M., Sakamoto H., Noguchi M., and Fukuyama K. Biochemistry 42 (2003) 9898-9905
41. Sandström J. Dynamic NMR Spectroscopy (1982), Academic Press, New York
42. Peyton D.H. Biochem. Biophys. Res. Commun. 175 (1991) 515-519
43. Yamamoto Y., Inoue Y., and Suzuki T. Magn. Reson. Chem. 31 (1993) S8-S16
44. Frankenberg-Dinkel N. Antoxidants Redox Signal 6 (2004) 825-834
45. Zuiderweg E.R.P. Biochemistry 43 (2000) 5222-5238
46. Bertini I., and Luchinat C. Coord. Chem. Rev. 150 (1996) 1-296
47. Williams G., Clayden N.J., Moore G.R., and Williams R.J.P. J. Mol. Biol. 183 (1985) 447-460
48. Emerson S.D., and La Mar G.N. Biochemistry 29 (1990) 1556-1566
49. Johnston P.D., Figueroa N., and Redfield A.G. Proc. Natl. Acad. Sci. USA 76 (1979) 3130-3134
50. Piotto M., Sandek V., and Sklenar V. J. Biomol. NMR 2 (1992) 661-666
51. Jeener J., Meier B.H., Bachmann P., and Ernst R.R. J. Chem. Phys. 71 (1979) 4546-4553
52. Griesinger C., Otting G., Wüthrich K., and Ernst R.R. J. Am. Chem. Soc. 110 (1988) 7870-7872
53. Neal S., Nip A.M., Zhang H., and Wishart D.S. J. Biomol. NMR 26 (2003) 215-240
54. Shrager R.I. J. Assoc. Comput. Machin. 17 (1970) 446-452
55. Press W.H., Flannery B.P., Teukolsky S.A., and Vetterlin W.T. Numerical Recipes (1986), Cambridge University Press, Cambridge
56. Xia Z., Nguyen B.D., Brunori M., Cutruzzola F., and La Mar G.N. Biophys. J. 89 (2005) 4149-4158
57. Wüthrich K. NMR of Proteins and Nucleic Acids (1986), Wiley & Sons, New York
58. Rodriguez J.C., Zeng Y., Wilks A., and Rivera M. J. Am. Chem. Soc. (2007) 11730-11742
59. Englander S.W., and Kallenbach N.R. Quart. Rev. Biophys. 16 (1984) 521-655