ANR projects

Molybdoenzymes from the DMSO reductase family.

Among molybdoenzymes, the subclass called “DMSO reductase family” collects bacterial enzymes of diverse functions despite housing similar active sites. They all contain a conserved catalytic subunit where the active site Mo is bound by two pterin molecules, resulting in a minimal coordination of the metal by four thiolates (picture above). These enzymes are frequently involved in oxo transfer reactions: they may catalyse the reduction of nitrate, DMSO, chlorate or selenate, or the oxidation of arsenite or nitrite. We study particularly the periplasmic nitrate reductase from Rhodobacter sphaeroides and the membrane bound nitrate reductase from Escherichia coli. En savoir plus…


Hydrogenases catalyze a reaction that is essential in the energetics of most bacteria and has promising technological applications: the reversible conversion between H2 and protons. The hydrogenases that contain iron-sulfur (FeS) clusters have been classified according to whether their active site is a dinuclear cluster of nickel and iron, or iron only. We study the NiFe enzymes from Desulfovibrio fructosovorans and Aquifex aeolicus and the FeFe hydrogenase from Clostridium acetobutylicum. En savoir plus…

Heme enzymes.

The cytochrome c nitrite reductase (we study the enzyme from Desulfovibrio desulfuricans) houses 5 hemes, one of which is the active site for the 6-electron reduction of nitrite into amonia.

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