SEDIMENT OXYGEN DEMAND IN THE ARROYO COLORADO RIVER1

ABSTRACT: The lower reaches of the Arroyo Colorado have historically failed to meet their use under subsection 303(b) of the U.S. Clean Water Act due to fecal coliform bacteria and low dissolved oxygen (DO). Fish kills, especially at the tidal confluence at the Port of Harlingen, Texas, have been reported. Oxygen demand from sediment (SOD) for a river typically has two states‐diffusion limited SOD (SOD) and potential SOD (pSOD), expressed when sediment is resuspended through increased flow or other disturbances. The objective of this research was to measure SOD in the Arroyo Colorado River in situ, estimate pSOD ex situ, and evaluate the relationship between SOD and the depositional environment. We measured SOD and pSOD in the Arroyo Colorado River at up to eight sites over three sampling events. We identified the sample sites based on a modified Rosgen geomorphic index for streambed stabilization. Sites with high sediment deposition potential had high SOD. The average values of SOD between sites were 0.62 g/m²/day (standard deviation 0.38 g/m²/day) and ranged from 0.13 to 1.2 g/m²/day. Potential SOD values ranged from as low as 19.2 to as high as 2,779 g/m³ sediment/ day. Potential SOD can serve as an indicator of the possible impact of SOD from resuspended sediment in stream systems.     

The role of chromatin damage in nickel-induced carcinogenesis. A review of recent developments

Over the last years, we have been testing a hypothesis that molecular mechanisms of nickel-induced carcinogenesis include interactions of this metal with major chromatin components; DNA, histones, and protamines. Our investigations using synthetic peptide models have resulted in identification of nickel-binding sites in core histones H3 and H2A and in protamine P2. These are: the internal -Cys110-AIH- motif in histone H3: the C-terminal-E121-SHHKAKGK "tail" motif in histone H2A; and the N-terminal RTH- motif in protamine P2. Ni(II) bound to the H3 and P2 motifs enhances oxidative DNA base damage by H2O2. In contrast, Ni(II) complex with the H2A "tail" is not redox active. However, at pH 7.4, it undergoes hydrolysis yielding a new complex, Ni(II)-SHHKAKGK, reactive with H2O2 and capable of mediating DNA oxidation. The "tail" cutting of H2A has also been observed in cells cultured with Ni(II). In Ni(II) complex with the protamine P2 peptides, H2O2 causes degradation of the metal-binding His3 and the distant Tyr8 residues. This site-specificity results from a long-range structuring effect of Ni(II) on its protamine ligand. In conclusion, Ni(II) binding to some chromatin proteins in somatic and sperm cells may result in oxidative and structural damage to the proteins and DNA. These effects may alter the fidelity of DNA replication and gene expression and thus facilitate carcinogenesis, including paternally-mediated cancer in the progeny.