|Reference : The diversity of Clostridial hydrogenases and biohydrogen production|
|Scientific congresses and symposiums : Poster|
|Life sciences : Microbiology|
|The diversity of Clostridial hydrogenases and biohydrogen production|
|Calusinska, Magdalena [Université de Liège - ULg > > Centre d'ingénierie des protéines >]|
|Savichtcheva, Olga [ > > ]|
|Masset, Julien [Université de Liège - ULg > Département des sciences de la vie > Biochimie et microbiologie industrielles >]|
|Hamilton, Christopher [Université de Liège - ULg > > Centre Wallon de biologie industrielle >]|
|Thonart, Philippe [Université de Liège - ULg > Département des sciences de la vie > Biochimie et microbiologie industrielles >]|
|Wilmotte, Annick [Université de Liège - ULg > Département des sciences de la vie > Physiologie et génétique bactériennes >]|
|International Symposium on Anaerobic Microbiology, ISAM 2009.|
|17-20 June 2009|
|The Czech Republic Academy of Sciences|
|[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 hydrogenases . Hydrogenases belong to an iron – sulphur protein family, that contains active sites consisting of inorganic sulfide and iron atoms bound to the polypeptide chain. On the basis of their bimetallocenter composition hydrogenases are divided into three main groups, phylogenetically not related: [NiFe] hydrogenases, [Fe] only hydrogenases and ‘metal – free hydrogenases’ which were described in methanogenic Archaea only. [NiFe] hydrogenases, composed of at least two subunits are well characterized and widely distributed between Archaea and Bacteria but only a few representatives of Clostridium possess this type of enzyme. On the other hand, [Fe] only hydrogenases, being usually monomeric enzymes and restricted to Bacteria and a few eukaryotic species are far less described. These proteins, being omnipresent catalysts of many biological reactions, are especially abundant in Clostridia. The physiological function of Clostridial [Fe] only hydrogenases is to dispose under the form of hydrogen, of the excess of reducing power generated during the fermentation of carbohydrates. The unusual diversity of forms of [Fe] only hydrogenases within Clostridia seems to support the central role of this enzyme in cell metabolism and to facilitate the quick adaptation of the host to changing environmental conditions. Moreover, the presence of multiple putative operons encoding for multisubunit [Fe] only hydrogenases in the genomes of sequenced Clostridium spp. is highlighting the need to study the new, not yet described function of these ostensibly simple proteins.
In this project, we have focused our effort on the molecular characterization of key enzymes involved in the process of biohydrogen production with a special interest in Clostridium species. By applying molecular techniques on samples from different kinds of bioreactors, we want to select highly productive species in terms of hydrogen generation. We also believe that gene expression profiling will provide new data on the possible function and activity of different hydrogenases involved in the process. The better understanding of hydrogen metabolism is essential for its sustainable production.
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