Temperature dependence of Q-band electron paramagnetic resonance spectra of nitrosyl heme proteins

Biophysical Journal

Volumn 73, Issue 6, 1997, Pages 3225-3229

  Flores, Marco ^a   Wajnberg, Eliane ^a   Bemski, George ^a  

^a CENTRO BRASILEIRO DE PESQUISAS FÍSICAS   (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN; HEMOPROTEIN; MYOGLOBIN;

ARTICLE; ELECTRON SPIN RESONANCE; HUMAN; PROTEIN CONFORMATION; PROTEIN VARIANT; TEMPERATURE DEPENDENCE;

EID: 0030819745     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78347-4     Document Type: Article

References (24)

1. Ansari, A., C. M. Jones, E. R. Henry, J. Hofrichter, and W. A. Eaton. 1994. Conformational relaxation and ligand binding in myoglobin. Biochemistry. 33:5128-5145.
2. Austin, R. H., K. W. Beeson, L. Eisenstein, H. Frauenfelder, and I. C. Gunsalus. 1975. Dynamics of ligand binding to myoglobin. Biochemistry. 14:5355-5373.
3. Belford, R. L., and M. J. Nilges. 1979. Computer simulation of powder spectra. EPR Symposium, 21st Rocky Mountain Conference, Denver, CO.
4. Bizarri, A. R., and S. Cannistraro. 1993. Solvent modulation of the structural hetrogeneity in FeIII myoglobin samples: a low temperature EPR investigation. Eur. Biophys. J. 22:259-267.
5. Caracelli, I., N. C. Meirelles, M. Tabak, O. B. Filho, and O. R. Nascimento. 1988. An ESR study of nitrosyl Aplysia brasiliana myoglobin and nitrosyl annelidae Glossoscolex paulistus erythrocruorin. Biochim. Biophys. Acta. 955:315-320.
6. Chevion, M., J. M. Salhany, J. Peisach, W. E. Blumberg, and S. Simon. 1978. Analogous effect of protons and inositol hexaphosphate on the alteration of structure of nitrosyl fetal human hemoglobin. Biochemistry. 17:1745-1750.
7. Cupane, A., M. Leone, and E. Vitrano. 1993. Protein dynamics: conformational disorder, vibrational coupling and anharmonicity in deoxyhemoglobin and myoglobin. Eur. Biophys. J. 21:385-391.
8. Frauenfelder, H., S. G. Sligar, and P. G. Wolynes. 1991. The energy landscapes and motions of proteins. Science. 254:1598-1603.
9. Henry, Y., and R. Banerjee. 1973. Electron paramagnetic studies of nitric oxide haemoglobin derivatives: isolated subunits and nitric oxide hybrids. J. Mol. Biol. 73:469-482.
10. Honeycutt, J. D., and D. Thirumalai. 1990. Metastability of the folded states of globular proteins. Proc. Natl. Acad. Sci. USA. 87:3526-3529.
11. Hong, M. K., D. Braunstein, B. R. Cowen, H. Frauenfelder, I. E. T. Iben, J. R. Mourant, P. Ormos, R. Scholl, A. Schulte, P. J. Steinbach, A. H. Xie, and R. D. Young. 1990. Conformational substates and motions in myoglobin. Biophys. J. 58:429-436.
12. Hori, H., M. Ikeda-Saito, and T. Yonetani. 1981. Single crystal EPR of myoglobin nitroxide. J. Biol. Chem. 256:7849-7855.
13. Hüttermann, J., C. Burgard, and R. Kappl. 1994. Proton ENDOR from randomly oriented NO-ligated haemoglobin: approaching the structural basis for the R-T transition. J. Chem. Soc. Faraday Trans. 90: 3077-3087.
14. Jia, L., C. Bonaventura, J. Bonaventura, and J. S. Stamler. 1996. S-Nitrosohaemoglobin: a dynamic activity of blood involved in vascular control. Nature. 380:221-226.
15. Lim, M., T. Jackson, and P. Anfinrud. 1995. Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O. Science. 269:962-966.
16. Louro, J. R. W., P. C. Ribeiro, and G. Bemski. 1981. EPR spectral changes of nitrosyl hemes and their relation to the hemoglobin T-R transition. Biochim. Biophys. Acta. 670:56-63.
17. Morse, R. H., and S. I. Chan. 1980. Electron paramagnetic resonance studies of nitrosyl ferrous heme complexes. J. Biol. Chem. 255: 7876-7882.
18. 14N hyperfine interaction accompanying R → T transition in nitrosylhemoglobin. Proc. Natl. Acad. Sci. USA. 76:4842-4846.
19. Neto, L. M., O. R. Nascimento, M. Tabak, and I. Caracelli. 1988. The mechanism of reaction of nitrosyl with met- and oxymyoglobin: an ESR study. Biochim. Biophys. Acta. 956:189-196.
20. Perutz, M. A., J. V. Kilmartm, K. Nagai, A. Szabo, and S. R. Symon. 1976. Influence of globin structures on the state of the heme. Ferrous low spin derivatives. Biochemistry. 15:378-387.
21. Potter, W. T., J. H. Hazzard, M. G. Choc, M. P. Tucker, and W. S. Caughey. 1990. Infrared spectra of carbonyl hemoglobins: characterization of dynamic heme pocket conformers. Biochemistry. 29:6283-6295.
22. Shiga, T., K. Hwang, and I. Tyuma. 1969. Electron paramagnetic resonance studies of nitric oxide hemoglobin derivatives. I. Human hemoglobin subunits. Biochemistry. 8:378-383.
23. Wajnberg, E., G. Bemski, L. J. El-Jaick, and O. C. Alves. 1996. Nitrosyl hemoglobins: EPR above 80 K. Int. J. Biol. Macromol. 18:231-235.
24. Wajnberg, E., M. P. Linhares, L. J. El-Jaick, and G. Bemski. 1992. Nitrosyl hemoglobin: EPR components at low temperatures. Eur. Biophys. J. 21:57-61.