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M Fontecave

Showing results (51-60 of 107) with videos related to

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Biochemical and Biophysical Research Communications|June 10, 1998
The flavoprotein component of the Escherichia coli sulfite reductase can act as a cytochrome P450c17 reductaseM Zeghouf, G Defaye, M Fontecave, et al.
The Journal of Biological Chemistry|June 22, 1999
The NAD(P)H:flavin oxidoreductase from Escherichia coli. Evidence for a new mode of binding for reduced pyridine nucleotidesV Nivière, F Fieschi, J L Dećout, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 21, 1997
Ribonucleotide reductase in the archaeon Pyrococcus furiosus: a critical enzyme in the evolution of DNA genomes?J Riera, F T Robb, R Weiss, et al.
Biochemical and Biophysical Research Communications|February 14, 1991
Vitamin E derivatives as new potent inhibitors of microsomal lipid peroxidationJ P Battioni, M Fontecave, M Jaouen, et al.
European Journal of Biochemistry|October 1, 1993
Abduction of iron(III) from the soluble methane monooxygenase hydroxylase and reconstitution of the binuclear site with iron and manganeseM Atta, M Fontecave, P C Wilkins, et al.
The Journal of Biological Chemistry|July 12, 1996
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 residueV Nivière, F Fieschi, J L Décout, et al.
Biochemistry|August 26, 1998
Reaction of the NAD(P)H:flavin oxidoreductase from Escherichia coli with NADPH and riboflavin: identification of intermediatesV Nivière, M A Vanoni, G Zanetti, et al.
FEBS Letters|May 30, 2001
Pulse radiolysis studies on superoxide reductase from Treponema pallidumV Nivière, M Lombard, M Fontecave, et al.
The Journal of Biological Chemistry|October 15, 1992
Substitution of manganese for iron in ribonucleotide reductase from Escherichia coli. Spectroscopic and crystallographic characterizationM Atta, P Nordlund, A Aberg, et al.
The Biochemical Journal|August 24, 1999
Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chlorideJ Covès, C Lebrun, G Gervasi, et al.
Pageof 11

Showing results (51-60 of 107) with videos related to

Sort By:
Pageof 11
Biochemical and Biophysical Research Communications|June 10, 1998
The flavoprotein component of the Escherichia coli sulfite reductase can act as a cytochrome P450c17 reductaseM Zeghouf, G Defaye, M Fontecave, et al.
The Journal of Biological Chemistry|June 22, 1999
The NAD(P)H:flavin oxidoreductase from Escherichia coli. Evidence for a new mode of binding for reduced pyridine nucleotidesV Nivière, F Fieschi, J L Dećout, et al.
Proceedings of the National Academy of Sciences of the United States of America|January 21, 1997
Ribonucleotide reductase in the archaeon Pyrococcus furiosus: a critical enzyme in the evolution of DNA genomes?J Riera, F T Robb, R Weiss, et al.
Biochemical and Biophysical Research Communications|February 14, 1991
Vitamin E derivatives as new potent inhibitors of microsomal lipid peroxidationJ P Battioni, M Fontecave, M Jaouen, et al.
European Journal of Biochemistry|October 1, 1993
Abduction of iron(III) from the soluble methane monooxygenase hydroxylase and reconstitution of the binuclear site with iron and manganeseM Atta, M Fontecave, P C Wilkins, et al.
The Journal of Biological Chemistry|July 12, 1996
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 residueV Nivière, F Fieschi, J L Décout, et al.
Biochemistry|August 26, 1998
Reaction of the NAD(P)H:flavin oxidoreductase from Escherichia coli with NADPH and riboflavin: identification of intermediatesV Nivière, M A Vanoni, G Zanetti, et al.
FEBS Letters|May 30, 2001
Pulse radiolysis studies on superoxide reductase from Treponema pallidumV Nivière, M Lombard, M Fontecave, et al.
The Journal of Biological Chemistry|October 15, 1992
Substitution of manganese for iron in ribonucleotide reductase from Escherichia coli. Spectroscopic and crystallographic characterizationM Atta, P Nordlund, A Aberg, et al.
The Biochemical Journal|August 24, 1999
Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chlorideJ Covès, C Lebrun, G Gervasi, et al.
Pageof 11