One of the negative environmental impacts of the last armed conflict in Bosnia and Herzegovina was the use of radioactive ammunition containing depleted uranium. The United Nations Environment Programme measurements detected higher radioactivity at several examined sites in Bosnia and Herzegovina. One of those places is in the area of Hadzići, close to Sarajevo. This research included an evaluation of genetic load in human lymphocytes due to exposure to depleted uranium. The study included individuals who were located in the area of Hadzići and who were directly exposed to depleted uranium. The control blood samples were taken from individuals who lived in West Herzegovina which is considered environmentally uncontaminated. The results of the micronucleus cytochalasin-B test in peripheral blood lymphocytes showed increased micronuclei frequencies in the exposed group.

We investigated the potential role of the co-substrate, thiocyanate (SCN–), in modulating the catalytic activity of myeloperoxidase (MPO) and other members of the mammalian peroxidase superfamily (lactoperoxidase (LPO) and eosinophil peroxidase (EPO)). Pre-incubation of SCN– with MPO generates a more complex biological setting, because SCN– serves as either a substrate or inhibitor, causing diverse impacts on the MPO heme iron microenvironment. Consistent with this hypothesis, the relationship between the association rate constant of nitric oxide binding to MPO-Fe(III) as a function of SCN– concentration is bell-shaped, with a trough comparable with normal SCN– plasma levels. Rapid kinetic measurements indicate that MPO, EPO, and LPO Compound I formation occur at rates slower than complex decay, and its formation serves to simultaneously catalyze SCN– via 1e– and 2e– oxidation pathways. For the three enzymes, Compound II formation is a fundamental feature of catalysis and allows the enzymes to operate at a fraction of their possible maximum activities. MPO and EPO Compound II is relatively stable and decays gradually within minutes to ground state upon H2O2 exhaustion. In contrast, LPO Compound II is unstable and decays within seconds to ground state, suggesting that SCN– may serve as a substrate for Compound II. Compound II formation can be partially or completely prevented by increasing SCN– concentration, depending on the experimental conditions. Collectively, these results illustrate for the first time the potential mechanistic differences of these three enzymes. A modified kinetic model, which incorporates our current findings with the mammalian peroxidases classic cycle, is presented.

We propose a canonical labeling of proteome maps, which enables one to sort and catalog the maps in a simple way. The canonical label of a proteome map is based on the canonical labeling of vertexes of Hasse diagram embedded in the map resulting in the adjacency matrix, the rows of which when viewed as binary numbers are the smallest possible such numbers. The use of the approach in documentation is illustrated with the proteome maps of liver cells of healthy male Fisher F344 rats and the rats treated with different peroxisome proliferators.