|Reference : The diversity of clostridial hydrogenases revealed by genome sequencing projects|
|Scientific congresses and symposiums : Poster|
|Life sciences : Microbiology|
|The diversity of clostridial hydrogenases revealed by genome sequencing projects|
|Calusinska, Magdalena [Université de Liège - ULg > > Centre d'ingénierie des protéines >]|
|Wilmotte, Annick [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes >]|
|Joris, Bernard [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes >]|
|Benelux Bioinformatics Conference|
|14-15 december 2009|
|[en] clostridium ; hydrogenases|
|[en] Molecular hydrogen is a key intermediate in metabolomic interactions of a wide range of microorganisms. Hydrogen is also regarded as a key component in future energy systems as it is a sustainable, clean, and transportable energy carrier.
Some microorganisms can produce hydrogen during a reversible reduction of protons to dihydrogen, a reaction which is catalyzed by the enzyme hydrogenases. On the basis of their bimetallocenter composition, hydrogenases are divided into three main groups, phylogenetically not related: [NiFe] hydrogenases, [Fe] only hydrogenases and FeS cluster free hydrogenases. The latter were described in methanogenic Archaea only. [NiFe] hydrogenases, composed of at least two subunits are well characterized and widely distributed between Archaea and Bacteria. However, only a few representatives of Clostridium sp. possess this type of enzyme. On the other hand, much less is known about the [Fe] only hydrogenases, that are usually monomeric enzymes and restricted to Bacteria and a few eukaryotic species. Genome sequencing projects gave a completely new insight into the diversity of forms of putative [Fe] only hydrogenases within the genus Clostridium. With the use of bioinformatic tools, we have described the unusual modularity of forms of these enzymes, from monomeric to tetrameric with a different number of accessory domains reacting with diverse redox partners. This fact seems to support the central role of hydrogenases in cell metabolism and quick adaptation of the host to changing environmental conditions. Moreover, the presence of multiple putative operons encoding for multisubunit [FeFe] hydrogenases is highlighting the fact that hydrogen metabolism is very complex in the Clostridium genus.
|Researchers ; Students|
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