Nonsteric factors dominate binding of nitric oxide, azide, imidazole, cyanide, and fluoride to the rhizobial heme-based oxygen sensor FixL

Chemistry and Biology

Volumn 3, Issue 10, 1996, Pages 841-850

  Winkler, Wade C ^a   Gonzalez, Gonzalo ^b   Wittenberg, Jonathan B ^c   Hille, Russ ^a   Dakappagari, Naveen ^b   Jacob, Anand ^c   Gonzalez, Leyla A ^a   Gilles Gonzalez, Marie A ^a  

^a Plant Biotechnology Center   (United States)

^b OHIO STATE UNIVERSITY   (United States)

^c ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

EPR; FixL; myoglobin; nitric oxide; oxygen sensor

Indexed keywords

BACTERIA (MICROORGANISMS); SINORHIZOBIUM MELILOTI;

EID: 0030265676     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(96)90070-8     Document Type: Article

References (26)

1. David, M. & Kahn, D., et al., (1988) Cascade regulation of nif gene expression in Rhizobium meliloti. Cell 54, 671-683.
2. Gilles-Gonzalez, M.A., Ditta, G. & Helinski, D.R. (1991) A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti. Nature 350, 170-172.
3. Gilles-Gonzalez, MA & Gonzalez, G. (1993) Regulation of the kinase activity of heme protein FixL from the two-component system FixL/FixJ of Rhizobium meliloti. J. Biol. Chem. 268, 16293-16297.
4. Agron, P.G., Ditta, G.S. & Helinski, D.R. (1993) Oxygen regulation of nifA transcription in vitro. Proc. Natl. Acad. Sci. USA 90, 3506-3510.
5. Reyrat, J.-M., David, M., Blonski, Q., Boistard, P. & Batut, J. (1993) Oxygen-regulated in vitro transcription of Rhizobium meliloti nif A and fixK genes. J. Bacteriol. 175, 6867-6872.
6. Gilles-Gonzalez, M.A., Gonzalez, G. & Perutz, M.F. (1995) Kinase activity of oxygen sensor FixL depends on the spin state of its heme iron. Biochemistry 34, 232-236.
7. Gilles-Gonzalez, M.A., Gonzalez, G., Perutz, M.F., Kiger, L., Marden, M. & Poyart, C. (1994) Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation. Biochemistry 33, 8067-8073.
8. Rodgers, K.R., Lukat-Rodgers, G.S. & Barron, J.A. (1996) Structural basis for ligand discrimination and response initiation in the heme-based oxygen sensor FixL. Biochemistry 35, 9539-9548.
9. 1H-NMR signals of the heme in the oxygen sensor FixL from Rhizobium meliloti. Chemistry & Biology 3, 561-566.
10. Shikama, K. & Matsuoka, A. (1989) Spectral properties unique to the myoglobins lacking the usual distal histidine residue. J. Mol. Biol. 209, 489-491.
11. Quillin, M.L., Arduini, R.M., Olson, J.S. & Phillips, G.N. (1993) High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. J. Mol. Biol. 234, 140-155.
12. Monson, E.K., Ditta, G.S. & Helinski, D.R. (1995) The oxygen sensor protein, FixL, of Rhizobium meliloti. Role of histidine residues in heme binding, phosphorylation, and signal transduction. J. Biol. Chem, 270, 5243-5250.
13. Springer, B.A., Sligar, S.G., Olson, J.S. & Phillips, G.N., Jr. (1994) Mechanisms of ligand recognition in myoglobin. Chem. Rev. 94, 699-714.
14. Brancaccio, A. & Olson, J.S., et al., (1994). Structural factors governing azide and cyanide binding to mammalian metmyoglobins. J. Biol. Chem. 269, 13843-13853.
15. Dou, Y., Olson, J.S., Wilkinson, A.J. & Ikeda-Saito, M. (1996) Mechanism of hydrogen cyanide binding to myoglobin. Biochemistry 35, 7107-7113.
16. Eich, R.F. & Olson, J.S., et al., (1996) Mechanism of NO-induced oxidation of myoglobin and hemoglobin. Biochemistry 35, 6976-6983.
17. Chan, Y-K. & Wheatcroft, R. (1992) Detection of a nitrous oxide reductase structural gene in Rhizobium meliloti strains and its location on the nod megaplasmid of JJ1 c10 and Su47. J. Bacteriol. 175, 19-26.
18. Mintorovich, J. & Satterlee, J.D. (1988) Anomalously slow cyanide binding to Glycera dibranchiata monomer methemoglobin component II: implication for the equilibrium constant. Biochemistry 27, 8045-8050.
19. Perutz, M.F. & Winkler, H., et al., (1978) Interactions between the quaternary structure of the globin and the spin state of the heme in ferric mixed spin derivatives of hemoglobin. Biochemistry 17, 3640-3651.
20. Mille, R., Olson, J.S. & Palmer, G. (1979) Spectral transitions of nitrosyl hemes during ligand binding to hemoglobin. J. Biol. Chem. 254, 12110-12120.
21. Conti, E. & Bolognesi, M., et al., (1993) X-ray crystal structure of ferric Aplysia limacina myoglobin in different liganded states. J. Mol. Biol. 233, 498-508.
22. Smerdon, S.J. & Olson, J.S., et al., (1995) Interactions among residues CD3, E7, E10, and E11 in myoglobins: attempts to simulate the ligand-binding properties of Aplysia myoglobin. Biochemistry 34, 8715-8725.
23. Antonini, E. & Brunori, M. (1971) Hemoglobin and Myoglobin in Their Reactions With Ligands. American Elsevier Publishing Co., New York.
24. Wittenberg, B.A., Brunori, M., Antonini, E., Wittenberg, J.B. & Wyman, J. (1965) Kinetics of the reactions of Aplysia myoglobin with oxygen and carbon monoxide. Arch. Biochem. Biophys. 111, 576-579.
25. Wittenberg, J.B., Appleby, C.A. & Wittenberg, B.A. (1972) The kinetics of the reactions of leghemoglobin with oxygen and carbon monoxide. J. Biol. Chem. 247, 527-531.
26. Springer, B.A., Egeberg, K.D., Sligar, S.G., Rohlfs, R.J., Mathews, A.J. & Olson, J.S. (1989) Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. Site-directed mutagenesis of the distal histidine. J. Biol. Chem. 264, 3057-3060.