A reversible NO complex of FeII(TIM): An S=1/2{FeNO}7 nitrosyl

Inorganica Chimica Acta

Volumn 260, Issue 2, 1997, Pages 163-172

  Chen, Ya ^a   Sweetland, Michael A ^a   Shepherd, Rex E ^a  

^a UNIVERSITY OF PITTSBURGH   (United States)

Author keywords

Azamacrocycle complexes; Iron complexes; Nitrosyl complexes

Indexed keywords

ELECTRON SPIN RESONANCE SPECTROSCOPY; GROUND STATE; LIGANDS;

2 ,3-BUTANEDIONE; AZAMACROCYCLE COMPLEXES; FORMATION CONSTANTS; IRON COMPLEX; N-O COMPLEXES; NITROSYL COMPLEX; SIX-COORDINATE COMPLEX; STERIC INFLUENCE;

IRON COMPOUNDS;

EID: 0000772063     PISSN: 00201693     EISSN: None     Source Type: Journal    
DOI: 10.1016/s0020-1693(96)05562-4     Document Type: Article

References (75)

1. V. Zang and R. van Eldik, Inorg. Chem., 29 (1990) 4462.
2. E.K. Pham and S.G. Chang, Nature, 369 (1994) 139.
3. S.E. Schwartz and W.H. White in S.E. Schwartz (ed.), Trace Atmospheric Constituents: Properties, Transformation and Fates, Wiley, New York, 1983, pp. 1-117.
4. S.P. Flicker, Platinum Met. Rev., 39 (1995) 150.
5. C. Nathan, FASEB J., 6 (1993) 3051.
6. S. Moncada, R.M. Palmer and E.A. Higgs, Pharmacol. Rev.,43 ( 1991 ) 109.
7. S.H. Snyder and D.S. Bredt, Sci. Am., (1992) 68.
8. P.L. Feldman, O.W. Griffith and D.J. Stuehr, Special Report: The Surprising Life of Nitric Oxide, Chem. Eng. News, Dec. 20 1993, pp. 26-38.
9. D.J. Steuhr and O.W. Griffith, Adv. Eng., 65 (1992) 287.
10. J.R. Lancaster, Am. Sci., 80 (1992) 248.
11. S. Moncada, R.M. Palmer and E.A. Higgs, Biochem. Pharmacol., 38 (1989) 1709.
12. M.A. Marietta, Chem. Res. Toxicol, 1 (1988) 249.
13. (a) R.M.J. Palmer, D.S. Ashon and S. Moncado, Nature, 333 (1988) 664;
14. (b) R.M.J. Palmer, A.G. Ferringe and S. Moncada, Nature, 327 (1987) 524;
15. (c) L.J. Ignarro, G.M. Bugar, K.S. Woods, R.F. Byrns and G. Chaudhuri, Proc. Natl. Acad. Sci. U.S.A., 84 (1987) 9264;
16. (d) J.J. Sneddon and J.R. Vane, Proc. Natl. Acad. Sci. U.S.A., 85 (1988) 2800.
17. (a) M. Hoffman, Science, 252 (1991) 1788;
18. (b) J. Garthwaite in S. Moncada and E.A. Higgs (eds.), Nitric Oxide from L-Arginine: A Bioregulatory System, Excerpta Medica, Amsterdam, 1990, pp. 115-137;
19. (c) J.A. Gaily, P.R. Montague, G.N. Reeke and G.M. Edelman, Proc. Natl. Acad. Sci. U.S.A., 87 (1990) 3547.
20. R. Iyengar, D. Stuehr and M.A. Marietta, Proc. Natl. Acad. Sci. U.S.A., 84 (1987) 6369.
21. J.B. Hibbs, R.R. Taintor, Z. Vavrin, D.L. Granger, J.-C. Drapier and I.A. Amber in S. Moncada and E.A. Higgs (eds.), Nitric Oxide from L-Arginine: A Bioregulatory System, Excerpta Medica, Amsterdam, 1990, pp. 189-224, and the first 114 Refs. therein.
22. (a) J.B. Hibbs, R.R. Taintor, Z. Vavrin and E.M Rachlin, Biochem. Biophys. Res. Commun., 157 (1988) 87;
23. (b) D.S. Bredt and S.H. Snyder, Neuron, 8 (1992) 3.
24. J.R. Lancaster and J.B. Hibbs, Proc. Natl. Acad. Sci. U.S.A., 87 (1990) 1223.
25. J.A. Corbett, R.G. Tilton, K. Chang, K.S. Hasan, Y. Ido, M.A. Sweetland, J.R. Lancaster, J.R. Williamson and M.L. McDaniel, Diabetes, 41 (1992) 552.
26. T.L. Lomis, S. Chalasani, J. Rhoads, C. Siffring, J. Manuaby, S. Yank and B. Renafarje, Proc. American College of Surgeons XLVI, 1995, p. 106.
27. (a) M.P. Doyle and J.W.J. Hockstra, Inorg. Biochem., 14 (1981) 351;
28. (b) M.P. Doyle, R.A. Pickering and B.R. Cook, Inorg. Biochem., 19 (1983) 329;
29. M.P. Doyle and S.N. Mahaptro, J. Am. Chem. Soc., 106 (1984) 3678.
30. M. Kelm, M. Freelisch, R. Spahr, H.-M. Piper, E. Noack and J. Schrader, Biochem. Biophys. Res. Commun., 154 (1988) 236.
31. J.S. Beckman, W. Tanya, J. Chen, P.A. Marshall and B.A. Freeman, Proc. Natl. Acad. Sci. U.S.A., 87 (1990) 1620.
32. W.H. Koppenol, J.J. Moreno, W.S. Pryor, H. Ischiropoulos and J.S. Beckman, Chem. Rev. Toxicol., 5 (1992) 894.
33. M.A. Marletta, P.S. Yoon, R. Iyengar, C.D. Leaf and J.S. Wishnok, Biochemistry, 27 (1988) 8706.
34. D.J. Steuhr and M.A. Marlatta, Proc. Natl. Acad. Sci. U.S.A., 82 (1985) 7738.
35. K.L. Crossin, Trends Biol. Sci., 16 (1991) 81.
36. Q. Wang, J. Jacobs, J. DeLec, H. Kruszna, R. Smith and D. Wilcox, Life Sci., 49 (1991) 55.
37. H. Kosaka, M. Watanabe, H. Yoshihara, N. Harada and T. Shiga, Biochem. Biophys. Res. Commun., 184 (1992) 1119.
38. E. Antonini and M. Brunori, Hemoglobin and Myoglobin in their Interactions with Ligands, North-Holland, Amsterdam, 1971, p. 236.
39. R.E. Shepherd, M.A. Sweetland and D.E. Junker, J. Inorg. Biochem., 65 (1997) 1.
40. Y.-M. Chiou and L. Que, J. Am. Chem. Soc., 117 (1995) 3999.
41. Y.-M. Chiou and L. Que, Inorg. Chem., 34 (1995) 3270.
42. (a) T.E. Westre, A. DiCicco, A. Filipponi, C.R. Natoli, B. Hedman, E.I. Solomon and K.O. Hodgson, J. Am. Chem. Soc., 116 (1994) 6757;
43. (b) Y. Zhang, M.A. Pavlosky, C.A. Brown, T.E. Westre, B. Hedman, K.O. Hodgson and E.I. Solomon, J. Am. Chem. Soc., 114 (1992) 9189.
44. (a) F. Hojland, H. Taftlund and S. Yde-Anders, Acta Chem. Scand., Ser. A, 37 (1983) 251;
45. (b) H. Toftlund and S. Yde-Andersen, Acta Chem. Scand., Ser. A, 35 (1981) 575.
46. V. Zang, M. Kotowski and R. van Eldik, Inorg. Chem., 27 (1988) 3279.
47. R.E. Shepherd, T.K. Myser and M.G. Elliott, Inorg. Chem., 27 (1988) 916.
48. C.R. Johnson, T.K. Myser and R.E. Shepherd, Inorg. Chem., 27(1988) 1089.
49. D.A. Baldwin, R.M. Pfeiffer, D.W. Reichgott and NJ. Rose, J Am. Chem. Soc., 95 (1973) 5152.
50. D. Kovacs and R.E. Shepherd, J. Inorg. Biochem., 10 (1919) 67.
51. Y. Sugiura and K. Ishizer, J. Inorg. Biochem., 11 (1979) 171.
52. A.W. Shaw and A.J. Vosper, J. Chem. Soc., Faraday Trans. I, 73 (1977) 1239.
53. R.W. Cargill (ed.), IUPAC Solubility Data Series, Carbon Monoxide, Vol. 43, Pergamon, New York, 1990, pp. 263-273.
54. L.C. Dickenson and J.C.W. Chien, J. Am. Chem. Soc., 93 (1971) 5036.
55. H. Kon, J. Biol. Chem., 243 (1968) 4350.
56. J.C.W. Chien, J. Chem. Phys., 51 (1969) 4220.
57. H. Kon, Biochim. Biophys. Acta, 379 (1975) 103.
58. D.W. Reichgott and N.J. Rose, J. Am. Chem. Soc., 99 (1977) 1813.
59. R.G. Goel, P.M. Henry and P.C. Polyzou, Inorg. Chem., 18 (1979) 2148.
60. T. Traylor, Acc. Chem. Res., 14 (1981) 102.
61. T. Hashimoto, R.C. Dyer, M.J. Crossley, J.E. Baldwin and F. Basolo, J. Am. Chem. Soc., 104 (1982) 2101.
62. J. Geibel, J. Cannon, D. Campbell and T.G. Traylor, J. Am. Chem. Soc., 100 (1978) 3575.
63. M. Rougee and D Brault, Biochemistry, 14 (1975) 4100.
64. D.K. White, J.B. Cannon and T. Traylor, J. Am. Chem. Soc., 101 (1979) 2443.
65. (a) M. Shimazu, F. Basolo, M.N. Vallejo and J.E. Baldwin, Inorg. Chim Acta, 91 (1984) 247;
66. (b) Inorg. Chim Acta, 91 (1984) 251.
67. R.W. Romberg and R.J. Kassner, Biochemistry, 18 (1979) 5387.
68. E.J. Rose and B.M. Hoffman, J. Am. Chem. Soc., 105 (1983) 2866.
69. T.G. Traylor and V.S. Sharma, Biochemistry, 31 (1992) 2847.
70. A.B. Ya, S. Hu, T.G. Spiro and J.N. Burstyn, J. Am. Chem Soc., 116 (1994) 4117.
71. K.D. Hodges, R.G. Wollman, S.L. Kessel, D.N. Hendrickson, D.G. Deweer and E.K. Barefield, J. Am. Chem. Soc., 101 (1979) 906.
72. (a) J.H. Enemark, R.D. Feltham, B.T. Huie, P.L. Johnson and K.B. Swedo, J. Am. Chem. Soc., 99 (1977) 3285;
73. (b) K.J. Holler, P.L. Johnson, R.D. Feltham and J. Enemark, Inorg. Chim. Acta, 33 (1979) 119;
74. (c) R.E. Eisenberg and C.D. Meyer, Acc. Chem. Res., 8 (1975) 26.
75. H.R. Mahler and E.H. Cordes, Biological Chemistry, Harper and Row, New York, 1966, p. 211.