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Biotin synthase is a pyridoxal phosphate-dependent cysteine desulfurase.
Ollagnier-De-Choudens S, Mulliez E, Hewitson KS, Fontecave M. Ollagnier-De-Choudens S, et al. Biochemistry. 2002 Jul 23;41(29):9145-52. doi: 10.1021/bi0122011. Biochemistry. 2002. PMID: 12119030
Reduction of the small subunit of Escherichia coli ribonucleotide reductase by hydrazines and hydroxylamines.
Gerez C, Fontecave M. Gerez C, et al. Biochemistry. 1992 Jan 28;31(3):780-6. doi: 10.1021/bi00118a020. Biochemistry. 1992. PMID: 1310046
-M. (1990) Nature 345, 593-598] have shown that both the radical and the diiron site are deeply buried inside the protein and thus strongly support the hypothesis of long-range electron-transfer processes within protein R2. ...
-M. (1990) Nature 345, 593-598] have shown that both the radical and the diiron site are deeply buried inside the protein and thus st …
The NADPH: sulfite reductase of Escherichia coli is a paraquat reductase.
Gaudu P, Fontecave M. Gaudu P, et al. Eur J Biochem. 1994 Dec 1;226(2):459-63. doi: 10.1111/j.1432-1033.1994.tb20070.x. Eur J Biochem. 1994. PMID: 8001563
Ferric reductases or flavin reductases?
Fontecave M, Covès J, Pierre JL. Fontecave M, et al. Biometals. 1994 Jan;7(1):3-8. doi: 10.1007/BF00205187. Biometals. 1994. PMID: 8118169 Review.
Abduction of iron(III) from the soluble methane monooxygenase hydroxylase and reconstitution of the binuclear site with iron and manganese.
Atta M, Fontecave M, Wilkins PC, Dalton H. Atta M, et al. Eur J Biochem. 1993 Oct 1;217(1):217-23. doi: 10.1111/j.1432-1033.1993.tb18236.x. Eur J Biochem. 1993. PMID: 8223558
The results of this study indicate that the M. capsulatus (Bath) hydroxylase contains a single diiron site....
The results of this study indicate that the M. capsulatus (Bath) hydroxylase contains a single diiron site....
Reduction and mobilization of iron by a NAD(P)H:flavin oxidoreductase from Escherichia coli.
Coves J, Fontecave M. Coves J, et al. Eur J Biochem. 1993 Feb 1;211(3):635-41. doi: 10.1111/j.1432-1033.1993.tb17591.x. Eur J Biochem. 1993. PMID: 8436123
This system has been previously purified and characterized as a NAD(P)H:flavin oxidoreductase [Fontecave, M., Eliasson, R. and Reichard, P. (1987) J. ...
This system has been previously purified and characterized as a NAD(P)H:flavin oxidoreductase [Fontecave, M., Eliasson, R. and …
Is the NAD(P)H:flavin oxidoreductase from Escherichia coli a member of the ferredoxin-NADP+ reductase family?. Evidence for the catalytic role of serine 49 residue.
Nivière V, Fieschi F, Décout JL, Fontecave M. Nivière V, et al. J Biol Chem. 1996 Jul 12;271(28):16656-61. doi: 10.1074/jbc.271.28.16656. J Biol Chem. 1996. PMID: 8663185
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