Fontecave M - Search Results

1

Deoxyribonucleotide synthesis in anaerobic microorganisms: the class III ribonucleotide reductase.

Fontecave M, Mulliez E, Logan DT. Fontecave M, et al. Prog Nucleic Acid Res Mol Biol. 2002;72:95-127. doi: 10.1016/s0079-6603(02)72068-0. Prog Nucleic Acid Res Mol Biol. 2002. PMID: 12206460 Review.

2

Reduction of the small subunit of Escherichia coli ribonucleotide reductase by hydrazines and hydroxylamines.

Gerez C, Fontecave M. Gerez C, et al. Among authors: fontecave m. Biochemistry. 1992 Jan 28;31(3):780-6. doi: 10.1021/bi00118a020. Biochemistry. 1992. PMID: 1310046

3

8-Azidoadenosine and ribonucleotide reductase.

Roy B, Lepoivre M, Decout JL, Lhomme J, Fontecave M. Roy B, et al. Among authors: fontecave m. Biochem Biophys Res Commun. 1992 Aug 31;187(1):432-7. doi: 10.1016/s0006-291x(05)81511-6. Biochem Biophys Res Commun. 1992. PMID: 1520331

4

The redox centers of ribonucleotide reductase of Escherichia coli.

Fontecave M, Nordlund P, Eklund H, Reichard P. Fontecave M, et al. Adv Enzymol Relat Areas Mol Biol. 1992;65:147-83. doi: 10.1002/9780470123119.ch4. Adv Enzymol Relat Areas Mol Biol. 1992. PMID: 1570768 Review. No abstract available.

5

Reduction of the Fe(III)-tyrosyl radical center of Escherichia coli ribonucleotide reductase by dithiothreitol.

Fontecave M, Gerez C, Mansuy D, Reichard P. Fontecave M, et al. J Biol Chem. 1990 Jul 5;265(19):10919-24. J Biol Chem. 1990. PMID: 2113527 Free article.

MetB2 is an inactive form that lacks the tyrosine radical but retains the Fe(III) center. We earlier reported (Fontecave, M., Eliasson, R., and Reichard, P. (1989) J. Biol. Chem. 264, 9164-9170) that enzymes from E. coli interconvert B2 and metB2, possibly as part o …

MetB2 is an inactive form that lacks the tyrosine radical but retains the Fe(III) center. We earlier reported (Fontecave, M., …

6

Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli.

Mulliez E, Ollagnier S, Fontecave M, Eliasson R, Reichard P. Mulliez E, et al. Among authors: fontecave m. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8759-62. doi: 10.1073/pnas.92.19.8759. Proc Natl Acad Sci U S A. 1995. PMID: 7568012 Free PMC article.

7

Enzymic and chemical reduction of the iron center of the Escherichia coli ribonucleotide reductase protein R2. The role of the C-terminus.

Covès J, Delon B, Climent I, Sjöberg BM, Fontecave M. Covès J, et al. Among authors: fontecave m. Eur J Biochem. 1995 Oct 1;233(1):357-63. doi: 10.1111/j.1432-1033.1995.357_1.x. Eur J Biochem. 1995. PMID: 7588767 Free article.

8

The mechanism of the anaerobic Escherichia coli ribonucleotide reductase investigated with nuclear magnetic resonance spectroscopy.

Eliasson R, Reichard P, Mulliez E, Ollagnier S, Fontecave M, Liepinsh E, Otting G. Eliasson R, et al. Among authors: fontecave m. Biochem Biophys Res Commun. 1995 Sep 5;214(1):28-35. doi: 10.1006/bbrc.1995.2252. Biochem Biophys Res Commun. 1995. PMID: 7669047

9

Inhibition of ribonucleotide reductase by nitric oxide derived from thionitrites: reversible modifications of both subunits.

Roy B, Lepoivre M, Henry Y, Fontecave M. Roy B, et al. Among authors: fontecave m. Biochemistry. 1995 Apr 25;34(16):5411-8. doi: 10.1021/bi00016a012. Biochemistry. 1995. PMID: 7727399

10

Flavodoxin is required for the activation of the anaerobic ribonucleotide reductase.

Bianchi V, Eliasson R, Fontecave M, Mulliez E, Hoover DM, Matthews RG, Reichard P. Bianchi V, et al. Among authors: fontecave m. Biochem Biophys Res Commun. 1993 Dec 15;197(2):792-7. doi: 10.1006/bbrc.1993.2548. Biochem Biophys Res Commun. 1993. PMID: 8267617 Free article.

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