Direct Electrochemistry Reveals the Functional Diversity of Hydrogenases
The comparison of homologous metalloenzymes, in which the same inorganic active site is surrounded by a variable protein matrix, has demonstrated that residues that are remote from the active site may have a great influence on catalytic properties. Recent work identifies the diverse molecular mechanisms by which the protein matrix may define the oxygen tolerance, catalytic directionality and catalytic reversibility of hydrogenases, enzymes that catalyse the oxidation and evolution of H2. These mechanisms involve residues in the second coordination sphere of the active site metal ion, more distant residues affecting protein flexibility through their side chains, residues lining the gas channel and even accessory subunits. Such long-distance effects contribute to making enzymes efficient, robust and different from one another.
Short bio
Christophe Léger obtained his PhD in physical chemistry from the University of Bordeaux and was a postdoc in the group of Fraser Armstrong in Oxford. He has been a CNRS
researcher in Marseille since 2002. He is interested in structure-function relationships in various families of metalloenzymes that are involved in the biological recycling of small molecules such as H2 and CO2.
Laboratory of the speaker
Laboratoire de Bioénergétique et Ingénierie des Protéines, CNRS, Marseille
Invited by
Olivier Berteau
