Covès J - Search Results

1

Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module.

Gruez A, Pignol D, Zeghouf M, Covès J, Fontecave M, Ferrer JL, Fontecilla-Camps JC. Gruez A, et al. Among authors: coves j. J Mol Biol. 2000 May 26;299(1):199-212. doi: 10.1006/jmbi.2000.3748. J Mol Biol. 2000. PMID: 10860732

2

NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction.

Eschenbrenner M, Covès J, Fontecave M. Eschenbrenner M, et al. Among authors: coves j. FEBS Lett. 1995 Oct 23;374(1):82-4. doi: 10.1016/0014-5793(95)01081-o. FEBS Lett. 1995. PMID: 7589518 Free article.

3

The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. A new model for the protein structure.

Eschenbrenner M, Covès J, Fontecave M. Eschenbrenner M, et al. Among authors: coves j. J Biol Chem. 1995 Sep 1;270(35):20550-5. doi: 10.1074/jbc.270.35.20550. J Biol Chem. 1995. PMID: 7657631 Free article.

4

Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli.

Coves J, Zeghouf M, Macherel D, Guigliarelli B, Asso M, Fontecave M. Coves J, et al. Biochemistry. 1997 May 13;36(19):5921-8. doi: 10.1021/bi9623744. Biochemistry. 1997. PMID: 9153434

5

The flavoprotein component of the Escherichia coli sulfite reductase: expression, purification, and spectral and catalytic properties of a monomeric form containing both the flavin adenine dinucleotide and the flavin mononucleotide cofactors.

Zeghouf M, Fontecave M, Macherel D, Covès J. Zeghouf M, et al. Among authors: coves j. Biochemistry. 1998 Apr 28;37(17):6114-23. doi: 10.1021/bi9728699. Biochemistry. 1998. PMID: 9558350

6

The flavoprotein component of the Escherichia coli sulfite reductase can act as a cytochrome P450c17 reductase.

Zeghouf M, Defaye G, Fontecave M, Coves J. Zeghouf M, et al. Among authors: coves j. Biochem Biophys Res Commun. 1998 May 29;246(3):602-5. doi: 10.1006/bbrc.1998.8671. Biochem Biophys Res Commun. 1998. PMID: 9618257

7

The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: crystallization and preliminary X-ray analysis.

Gruez A, Zeghouf M, Bertrand J, Eschenbrenner M, Covès J, Fontecave M, Pignol D, Fontecilla-Camps JC. Gruez A, et al. Among authors: coves j. Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):135-6. doi: 10.1107/s090744499701069x. Acta Crystallogr D Biol Crystallogr. 1998. PMID: 9761836

8

31P nuclear magnetic resonance study of the flavoprotein component of the Escherichia coli sulfite reductase.

Evrard A, Zeghouf M, Fontecave M, Roby C, Covès J. Evrard A, et al. Among authors: coves j. Eur J Biochem. 1999 Apr;261(2):430-7. doi: 10.1046/j.1432-1327.1999.00274.x. Eur J Biochem. 1999. PMID: 10215853 Free article.

This protein was reported previously as a reliable simplified model for native SiR-FP [Zeghouf, M., Fontecave, M., Macherel, D., & Coves, J. (1998) Biochemistry 37, 6117-6123]. SiR-FP60 was examined in its native form, as a complex with NADP+ and after monoelect …

This protein was reported previously as a reliable simplified model for native SiR-FP [Zeghouf, M., Fontecave, M., Macherel, D., & Co …

9

A simplifed functional version of the Escherichia coli sulfite reductase.

Zeghouf M, Fontecave M, Coves J. Zeghouf M, et al. Among authors: coves j. J Biol Chem. 2000 Dec 1;275(48):37651-6. doi: 10.1074/jbc.M005619200. J Biol Chem. 2000. PMID: 10984484 Free article.

Whereas alpha spontaneously polymerizes, we have been able to produce SiR-FP60, a monomeric but fully active truncated version of it, lacking the N-terminal part (Zeghouf, M., Fontecave, M., Macherel, D., and Coves, J. (1998) Biochemistry 37, 6114-6123). Here we rep …

Whereas alpha spontaneously polymerizes, we have been able to produce SiR-FP60, a monomeric but fully active truncated version of it, lackin …

10

NADPH-sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase.

Covès J, Nivière V, Eschenbrenner M, Fontecave M. Covès J, et al. J Biol Chem. 1993 Sep 5;268(25):18604-9. J Biol Chem. 1993. PMID: 8360156 Free article.

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