Investigating the effects of predator removal and habitat management on nest success and breeding population size of a farmland passerine: a case study

Passerines are especially vulnerable to predation at the pre-independence stage. Although the role of nest success in British farmland passerine declines is contentious, improvement in nest success through sympathetic management could play a role in their reversal. Because habitat is known to interact with predation, management options for mitigation will need to consider effects of nest predation. We present results from an observational study of a population of Common Blackbird Turdus merula on a farm which has experienced a range of agri-environment and game-management options, including a period with nest predator control, as a case study to address some of these issues. We used an information theoretic model comparison procedure to look for evidence of interactions between habitat and nest predation, and then asked whether habitat management and nest predator abundances could explain population trends at the site through their effects on nest success. Interactions were detected between measures of predator abundance and habitat variables, and these varied with nest stage - habitat within the vicinity of the nest appeared to be important at the egg stage, and nest-placement characteristics were important at the nestling stage. Although predator control appeared to have a positive influence on Blackbird breeding population size, the non-experimental set-up meant we could not eliminate other potential explanations. Variation in breeding population size did not appear to be influenced by variation in nest success alone. Our study demonstrates that observational data can only go so far in detection of such effects, and we discuss how it might be taken further. Agri-environment and game-management techniques are likely to influence nest predation pressure on farmland passerines, but the patterns, mechanisms and importance to population processes remain not wholly understood.

Thermodynamic analysis of ferrous ion binding to Escherichia coli ferritin EcFtnA

Iron oxidation in the bacterial ferritin EcFtnA from Escherichia coli shows marked differences from its homologue human H-chain ferritin (HuHF). While the amino acid residues that constitute the dinuclear center in these proteins are highly conserved, EcFtnA has a third iron-binding site (C site) in close proximity to the dinuclear center that is seemingly responsible for these differences. Here, we describe the first thermodynamic study of Fe2+ binding to EcFtnA and its variants to determine the location of the primary ferrous ion-binding sites on the protein and to better understand the role of the third C site in iron binding. Isothermal titration calorimetric analyses of the wild-type protein reveal the presence of two main classes of binding sites in the pH range of 6.5-7.5, ascribed to Fe2+ binding, first at the A and then the B sites. Site-directed mutagenesis of ligands in the A, B, or C sites affects the apparent Fe2+-binding stoichiometries at the unaltered sites. The data imply some degree of inter- and intrasubunit negative cooperative interaction between sites. Unlike HuHF where only the A site initially binds Fe2+, both A and B sites in EcFtnA bind Fe2+, implying a role for the C site in influencing the binding of Fe2+ at the B site of the di-iron center of EcFtnA. The ITC equations describing a binding model for three classes of independent binding sites are reported here for the first time.

The effect of a new drag-law parameterization on ice shelf water plume dynamics

A drag law accounting for Ekman rotation adjacent to a flat, horizontal bou ndary is proposed for use in a plume model that is written in terms of the depth-mean velocity. The drag l aw contains a variable turning angle between the mean velocity and the drag imposed by the turbulent bound ary layer. The effect of the variable turning angle in the drag law is studied for a plume of ice shelf wat er (ISW) ascending and turning beneath an Antarctic ice shelf with draft decreasing away from the groundi ng line. As the ISW plume ascends the sloping ice shelf–ocean boundary, it can melt the ice shelf, wh ich alters the buoyancy forcing driving the plume motion. Under these conditions, the typical turning ang le is of order 10° over most of the plume area for a range of drag coefficients (the minus sign arises for th e Southern Hemisphere). The rotation of the drag with respect to the mean velocity is found to be signifi cant if the drag coefficient exceeds 0.003; in this case the plume body propagates farther along and across the b ase of the ice shelf than a plume with the standard quadratic drag law with no turning angle.

The Functionality of the three-sited Ferroxidase center of E. coli Bacterial Ferritin (EcFtnA)

At least three ferritins are found in the bacterium Escherichia coli, the heme-containing bacterioferritin (EcBFR) and two non-heme bacterial ferritins (EcFtnA and EcFtnB). In addition to the conserved A- and B-sites of the diiron ferroxidase center, EcFtnA has a third iron-binding site (the C-site) of unknown function that is nearby the diiron site. In the present work, the complex chemistry of iron oxidation and deposition in EcFtnA has been further defined through a combination of oximetry, pH stat, stopped-flow and conventional kinetics, UV-visible, fluorescence and EPR spectroscopic measurements on the wildtype protein and site-directed variants of the A-, B- and C-sites. The data reveal that, while H2O2 is a product of dioxygen reduction in EcFtnA and oxidation occurs with a stoichiometry of Fe(II)/O2 ~ 3:1, most of the H2O2 produced is consumed in subsequent reactions with a 2:1 Fe(II)/H2O2 stoichiometry, thus suppressing hydroxyl radical formation. While the A- and B-sites are essential for rapid iron oxidation, the C-site slows oxidation and suppresses iron turnover at the ferroxidase center. A tyrosyl radical, assigned to Tyr24 near the ferroxidase center, is formed during iron oxidation and its possible significance to the function of the protein is discussed. Taken as a whole, the data indicate that there are multiple iron-oxidation pathways in EcFtnA with O2 and H2O2 as oxidants. Furthermore, the data are inconsistent with the C-site being a transit site, providing iron to the A- and B-sites, and does not support a universal mechanism for iron oxidation in all ferritins as recently proposed.