Harmonizing outdoor recreation and bird conservation targets in protected areas: Applying available monitoring data to facilitate collaborative management at the regional scale.

In protected areas managers have to achieve conservation targets while providing opportunities for outdoor recreation. This dual mandate causes conflicts in choosing between management options. Furthermore, the persistence of a protected species within the management unit often depends on how conservation areas elsewhere in the region are managed.

Rapid electrochemical screening of NAD-dependent dehydrogenases in a 96-well format.

The electrochemical detection of dehydrogenase activity in crude cell lysates is performed simultaneously using 96 carbon electrodes modified with electrografted phenazines. The method is applied to the screening of a library of formate dehydrogenase mutants obtained by directed evolution.

Oxygen binding to partially nitrosylated hemoglobin.

Reactions of nitric oxide (NO) with hemoglobin (Hb) are important elements in protection against nitrosative damage. NO in the vasculature is depleted by the oxidative reaction with oxy Hb or by binding to deoxy Hb to generate partially nitrosylated Hb (Hb-NO). Many aspects of the formation and persistence of Hb-NO are yet to be clarified.

A 96-well electrochemical method for the screening of enzymatic activities.

The rapid electrochemical screening of enzyme activities in bioelectronics is still a challenging issue. In order to solve this problem, we propose to use a 96-well electrochemical assay. This system is composed of 96 screen-printed electrodes on a printed circuit board adapted from a commercial system (carbon is used as the working electrode and silver chloride as the counter/reference electrode).

Molecular controls of the oxygenation and redox reactions of hemoglobin.

Significance: The broad classes of O(2)-binding proteins known as hemoglobins (Hbs) carry out oxygenation and redox functions that allow organisms with significantly different physiological demands to exist in a wide range of environments. This is aided by allosteric controls that modulate the protein's redox reactions as well as its O(2)-binding functions.

Recent Advances: The controls of Hb's redox reactions can differ appreciably from the molecular controls for Hb oxygenation and come into play in elegant mechanisms for dealing with nitrosative stress, in the malarial resistance conferred by sickle cell Hb, and in the as-yet unsuccessful designs for safe and effective blood substitutes.