Bioethanol.

Alternatives to petroleum-derived fuels are being sought in order to reduce the world's dependence on non-renewable resources. The most common renewable fuel today is ethanol derived from corn grain (starch) and sugar cane (sucrose). It is expected that there will be limits to the supply of these raw materials in the near future, therefore lignocellulosic biomass is seen as an attractive feedstock for future supplies of ethanol. However, there are technical and economical impediments to the development of a commercial processes utilizing biomass. Technologies are being developed that will allow cost-effective conversion of biomass into fuels and chemicals. These technologies include low-cost thermochemical pretreatment, highly effective cellulases and hemicellulases and efficient and robust fermentative microorganisms. Many advances have been made over the past few years that make commercialization more promising.

Crystal structure of substrate free form of glycerol dehydratase.

Glycerol dehydratase (GDH) and diol dehydratase (DDH) are highly homologous isofunctional enzymes that catalyze the elimination of water from glycerol and 1,2-propanediol (1,2-PD) to the corresponding aldehyde via a coenzyme B(12)-dependent radical mechanism. The crystal structure of substrate free form of GDH in complex with cobalamin and K(+) has been determined at 2.5 A resolution. Its overall fold and the subunit assembly closely resemble those of DDH. Comparison of this structure and the DDH structure, available only in substrate bound form, shows the expected change of the coordination of the essential K(+) from hexacoordinate to heptacoordinate with the displacement of a single coordinated water by the substrate diol. In addition, there appears to be an increase in the rigidity of the K(+) coordination (as measured by lower B values) upon the binding of the substrate. Structural analysis of the locations of conserved residues among various GDH and DDH sequences has aided in identification of residues potentially important for substrate preference or specificity of protein-protein interactions.