Impacts of forestry on nitrogen in upland and lowland catchments: a comparison of the River Severn at Plynlimon in mid-Wales and the Bedford Ouse in south-east England using the INCA Model

The impacts of afforestation at Plynlimon in the Severn catchment, mid-Wales. and in the Bedford Ouse catchment in south-east England are evaluated using the INCA model to simulate Nitrogen (N) fluxes and concentrations. The INCA model represents the key hydrological and N processes operating in catchments and simulates the daily dynamic behaviour as well as the annual fluxes. INCA has been applied to five years of data front the Hafren and Hore headwater sub-catchments (6.8 km(2) area in total) of the River Severn at Plytilimon and the model was calibrated and validated against field data. Simulation of afforestation is achieved by altering the uptake rate parameters in the model. INCA simulates the daily N behaviour in the catchments with good accuracy as well as reconstructing the annual budgets for N release following clearfelling a four-fold increase in N fluxes was followed by a slow recovery after re-afforestation. For comparison, INCA has been applied to the large (8380 km(2)) Bedford Ouse catchment to investigate the impact of replacing 20% arable land with forestry. The reduction in fertiliser inputs from arable farming and the N uptake by the forest are predicted to reduce the N flux reaching the main river system, leading to a 33% reduction in N-Nitrate concentrations in the river water.

EfeO-cupredoxins: major new members of the cupredoxin superfamily with roles in bacterial iron transport

The EfeUOB system of Escherichia coli is a tripartite, low pH, ferrous iron transporter. It resembles the high-affinity iron transporter (Ftr1p-Fet3p) of yeast in that EfeU is homologous to Ftr1p, an integral-membrane iron-permease. However, EfeUOB lacks an equivalent of the Fet3p component—the multicopper oxidase with three cupredoxin-like domains. EfeO and EfeB are periplasmic but their precise roles are unclear. EfeO consists primarily of a C-terminal peptidase-M75 domain with a conserved ‘HxxE’ motif potentially involved in metal binding. The smaller N-terminal domain (EfeO-N) is predicted to be cupredoxin (Cup) like, suggesting a previously unrecognised similarity between EfeO and Fet3p. Our structural modelling of the E. coli EfeO Cup domain identifies two potential metal-binding sites. Site I is predicted to bind Cu2+ using three conserved residues (C41 and 103, and E66) and M101. Of these, only one (C103) is conserved in classical cupredoxins where it also acts as a Cu ligand. Site II most probably binds Fe3+ and consists of four well conserved surface Glu residues. Phylogenetic analysis indicates that the EfeO-Cup domains form a novel Cup family, designated the ‘EfeO-Cup’ family. Structural modelling of two other representative EfeO-Cup domains indicates that different subfamilies employ distinct ligand sets at their proposed metal-binding sites. The ~100 efeO homologues in the bacterial sequence databases are all associated with various iron-transport related genes indicating a common role for EfeO-Cup proteins in iron transport, supporting a new copper-iron connection in biology.