Assignment of the hyperfine-shifted 1H-NMR signals of the heme in the oxygen sensor FixL from Rhizobium meliloti

Chemistry and Biology

Volumn 3, Issue 7, 1996, Pages 561-566

  Bertolucci, Craig ^a   Ming, Li June ^a   Gonzalez, Gonzalo ^b   Gilles Gonzalez, Marie A ^b  

^a UNIVERSITY OF SOUTH FLORIDA   (United States)

^b OHIO STATE UNIVERSITY   (United States)

Author keywords

FixL; myoglobin; nitrogen fixation; NMR; sensor kinase

Indexed keywords

BACTERIA (MICROORGANISMS); RHIZOBIUM; SINORHIZOBIUM MELILOTI;

EID: 0029830156     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(96)90147-7     Document Type: Article

References (29)

1. 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.
2. Gilles-Gonzalez, M.A. & 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.
3. 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.
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. 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.
6. Goldberg, M.A. & Schneider, T.J. (1994). Similarities between the oxygen-sensing mechanisms regulating the expression of vascular endothelial growth factor and erythropoietin. J. Biol. Chem. 269, 4355-4359.
7. Vinogradov, S.N., Walz, D.A., Pohajdak, B., Moens, L., Kapp, O.H., Suzuki, T. & Trotman, C.N.A. (1993). Adventitious variability? The amino acid sequences of nonvertebrate globins. Comp. Biochem. Physiol. 106B, 1-26.
8. Monson, E.K., Ditta, G.S. & Helinski, D.R. (1995). The oxygen sensor FixL of Rhizobium meliloti. Role of histidine residues in heme binding, phosphorylation and signal transduction. J. Biol. Chem. 270, 5243-5250.
9. Wuthrich, K. (1986). NMR of Proteins and Nucleic Acids. Wiley, New York.
10. Clore, G.M. & Gronenborn, A.M. (1993). NMR of Proteins. CRC Press, Boca Raton, Florida.
11. Bertini, I. & Luchinat, C. (1986). NMR of Paramagnetic Molecules in Biological Systems. Benjamin/Cummings, Menlo Park, California.
12. Berliner, L.J. & Reuben, J., eds. (1992). NMR of Paramagnetic Molecules. Plenum Press, New York.
13. La Mar, G.N., Horrocks, W.D. Jr & Holm, R.H., eds (1973). NMR of Paramagnetic Molecules: Principles and Applications. Academic Press, New York.
14. La Mar, G.N., ed. (1995). Nuclear Magnetic Resonance of Paramagnetic Macromolecules. Kluner, Dordrecht.
15. 1H-NMR studies of the paramagnetic metalloenzyme copper-nickel Superoxide dismutase. Inorg. Chem. 31, 4433-4435.
16. 1H-NMR studies of the active site of iron(II) Superoxide dismutase from Escherichia coli. Inorg. Chem. 33, 83-87.
17. 1H-NMR studies of Ca(II)-binding sites in proteins using paramagnetic lanthanides(III) as probes; Yb(III)-substituted bovine α-lactalbumin as an example. Magn. Reson. Chem. 31, 5104-5109.
18. Ming, L.-J. (1995). Paramagnetic lanthanides(III) ions as NMR probes for biomolecular structure and function. In Nuclear Magnetic Resonance of Paramagnetic Macromolecules. (La Mar, G.N., ed.), pp. 245-264, Kluner, Dordrecht.
19. Bertini, I., Turano, P. & Vila, A.J. (1994). Nuclear magnetic resonance of paramagnetic metalloproteins. Chem. Rev. 93, 2833-2932.
20. Noggle, J.H. & Schirmer, R.E. (1971). The Nuclear Overhauser Effect. Academic Press, New York.
21. Ernst, R.R., Bodenhausen, G. & Wokaun, A. (1987). Principles of Nuclear Magnetic Resonance in One and Two Dimensions. Clarendon, Oxford.
22. Neuhaus, D. & Williamson, M.P. (1989) The Nuclear Overhauser Effect in Structural and Conformational Analysis. VCH, New York.
23. Peyton, D.H., La Mar, G.N., Ramaprasad S., Unger, S.W., Sankar, S. & Gersonde, K. (1991). Proton nuclear magnetic resonance study of the solution distal histidine orientation in monomeric Chironomus thummi thummi cyanomet hemoglobins. J. Mol. Biol. 221, 1015-1026.
24. Cutnell, J.D., La Mar, G.N., & Kong, S.B. (1981). Proton nuclear magnetic resonance study of the relaxation behavior and kinetic lability of exchangeable protons in the heme pocket of cyanometmyoglobin. J. Am. Chem. Soc. 103, 3567-3572.
25. 1H-NMR resonance assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: application to Aplysia cyano-metmyoglobin. J. Biomol. NMR. 2, 597-618.
26. Alam, S.L. & Satterlee, J.D. (1994). Complete heme proton hyperfine resonance assignments of the Glycera dibranchiata component IV metcyano monomer hemoglobin. Biochemistry 33, 4008-4018.
27. Alam, S.L. & Satterlee, J.D. (1995). Unambiguous heme proton hyperfine resonance assignments of a monomeric hemoglobin from Glycera dibranchiata facilitated with a completely deuterated protein. J. Am. Chem. Soc. 117, 49-53.
28. 67(E10) in modulation of ligand tilt. Biophys. J. 65, 2178-2190.
29. Quillin, M.L., Arduini, R.M., Olson, J.S. & Philips, G.N. (1993). High-resolution crystal structures of distal histidine mutants of sperm whale myoglobin. J. Mol. Biol. 234, 140-155.