Structural dissection of two redox proteins from the shipworm symbiont Teredinibacter turnerae.

The discovery of lytic polysaccharide monooxygenases (LPMOs), a family of copper-dependent enzymes that play a major role in polysaccharide degradation, has revealed the importance of oxidoreductases in the biological utilization of biomass. In fungi, a range of redox proteins have been implicated as working in harness with LPMOs to bring about polysaccharide oxidation. In bacteria, less is known about the interplay between redox proteins and LPMOs, or how the interaction between the two contributes to polysaccharide degradation.

C-type cytochrome-initiated reduction of bacterial lytic polysaccharide monooxygenases.

The release of glucose from lignocellulosic waste for subsequent fermentation into biofuels holds promise for securing humankind's future energy needs. The discovery of a set of copper-dependent enzymes known as lytic polysaccharide monooxygenases (LPMOs) has galvanised new research in this area. LPMOs act by oxidatively introducing chain breaks into cellulose and other polysaccharides, boosting the ability of cellulases to act on the substrate.

Appraising the extractable tidal energy resource of the UK's western coastal waters.

A two-dimensional west coast tidal model, built on the ADCIRC platform (an unstructured grid two-dimensional depth-integrated shallow water model), has been developed to examine the scope for reliable and fully predictable electricity generation from UK coastal waters using an ambitious combination of estuary barrages, tidal lagoons and tidal stream generator arrays. The main emphasis has been towards conjunctive operation of major estuary barrages, initially including the presence of pilot-scale tidal stream developments, though ambitious exploitation of extensive tidal streams has also been explored.