The ingestion of aluminum from food containers such as cookware, cans, utensils and wrappings and its subsequent release into the environment is a growing public health concern. Aluminum is widely used in manufacturing cookware due to its malleability, high heat conductivity, light weight, durability, availability and affordability. This paper therefore gives a review of most relevant literatures on the benefits and risks of the various types of aluminum cookware in use, the composition and the public health effects of aluminum ingestion. Studies that reported the leaching of aluminum from cookware into food and environmental effects of aluminum leaching were also reviewed. In the developing countries, aluminum cookwares are produced from scrap metals and has been reported to leach harmful substances including heavy metals such as: nickel, arsenic, copper, cadmium, lead, and aluminum into cooked food. Several factors have been reported to increase the rate of leaching of metals from aluminum cookwares. Exposure to metals from aluminum cookware and the public health effects have not been well studied, hence, our recommendation for more studies to elucidate the health effect of this practice. This review also presents measures that can limit exposure to the risks that may arise from the use of aluminum cookware.
The volume of pharmaceuticals discharged into the environment increases daily as a consequence of human life. In the present study, the seasonal variation of ibuprofen in sediment, biota, water, and their exposure risk were investigated in River Owena and Ogbese, Nigeria. The high-performance liquid chromatography coupled to a mass spectrometer (HPLC-MS/MS) was used to analyze the samples after clean up and pre-concentration by solid-phase extraction. The mean concentration of IBU in the samples spanned a range of 1.75 - 2.75 μg/g in sediment, 0.01 – 15.00 μg/g in fish, and 0.00002 – 0.005 μg/ml in water. The measurement of IBU in the sediment and water was significantly elevated in the dry season than the wet season, whereas the opposite was the case in biota. There was a significant interaction between season, media, and rivers with respect to IBU occurrence in the sampled rivers. The calculated bio-water accumulation factor (BWAF) was as high as 750,000 μg/g in fish, proving IBU is extremely bio-accumulative. The ecotoxicological risk assessment for average and worst possible outcome showed that the risk quotient (RQ) for IBU present in the water was sufficient to cause toxicity to fish in both freshwater bodies. The potential bioavailability of IBU to aquatic fauna for prolonged periods spanning several months can result in its circling back into the food web afterward. The baseline info provided by this study in these freshwaters may provide valuable information for the implementation of safety limits for the management of IBU influx into the environment.
The number of transition metal ions which are essential to life - also often called trace elements - increased steadily over the years. In parallel, the list of biological functions in which transition metals are involved, has grown, and is still growing tremendously. Significant progress has been made in understanding the chemistry operating at the biological sites where metal ions have been discovered. Early on, based on the application of physical, chemical, and biological techniques, it became likely that numerous of these metal centers carry sulfur ligands in their coordination sphere, such as sulfide (S2- ), cysteine (RS- ), or methionine (RSCH3). Notably, the structure and the reactivity of the metal active sites turned out to be quite different from anything previously observed in simple coordination complexes. Consequently, the prediction of active-site structures, based on known properties of transition metal ion complexes, turned out to be difficult and incorrect in many cases. Yet, biomimetic inorganic chemistry, via synthesis and detailed structural and electronic characterization of synthetic analogues, became an important factor and helped to understand the properties of the metal active sites. Striking advances came from molecular biology techniques and protein crystallography, as documented by the publication of the first high-resolution structures of iron-sulfur proteins and the blue copper protein plastocyanin approximately five decades ago. In this volume of METAL IONS IN LIFE SCIENCES the focus will be on some of the most intriguing, in our view, transition metal-sulfur sites discovered in living organisms. These include the type 1 Cu mononuclear center, the purple mixed-valent [Cu1.5+ -(Cys)2-Cu1.5+ ] CuA, the tetranuclear copper-sulfide catalytic center of nitrous oxide reductase, the heme-thiolate site in cytochrome P450, the iron-sulfur proteins with bound inorganic (S2- ) and organic (Cys-) sulfur, the pterin dithiolene cofactor (Moco) coordinated to either molybdenum or tungsten, the [8Fe-7S] P-cluster and the [Mo-7Fe-9S-C]-homocitrate catalytic site of nitrogenase, the siroheme-[4Fe-4S] center involved in the reduction of sulfite (SO32-) to hydrogen sulfide (H2S), the NiFeS sites of hydrogenases and CO dehydrogenase, and the zinc finger domains. We apologize to all researchers and their associates who have made tremendous contributions to our current knowledge of the steadily increasing transition metal sulfur sites in proteins and enzymes but are not mentioned here. These omissions are by no means intentional but merely the consequence of time and space. We are fully aware of the excellent books and authoritative reviews on various aspects of the subject, however, it is our motivation to cover in one single volume this exciting domain of bioinorganic chemistry.
In nature, sulfur exists in a range of oxidation states and the two-electron reduced form is the most commonly found in biomolecules like the sulfur-containing amino acids cysteine and methionine, some cofactors, and polysaccharides. Sulfur is reduced through two pathways: dissimilation, where sulfite (SO23 -) is used as terminal electron acceptor; and assimilation, where sulfite is reduced to sulfide (S2-) for incorporation into biomass. The pathways are independent, but share the sulfite reductase function, in which a single enzyme reduces sulfite by six electrons to make sulfide. With few exceptions, sulfite reductases from either pathway are iron metalloenzymes with structurally diverse configurations that range from monomers to tetramers. The hallmark of sulfite reductase is its catalytic center made of an iron-containing porphyrinoid called siroheme that is covalently coupled to a [4Fe-4S] cluster through a shared cysteine ligand. The substrate evolves through a push-pull mechanism, where electron transfer is coupled to three dehydration steps. Siroheme is an isobacteriochlorin that is more readily oxidized than protoporphyin IX-derived hemes. It is synthesized from uroporphyrinogen III in three steps (methylation, a dehydrogenation, and ferrochelation) that are performed by enzymes with homology to those involved in cobalamin synthesis. Future research will need to address how the siroheme-[4Fe-4S] clusters are assembled into apo-sulfite and nitrite reductases. The chapter will discuss how environmental microbes use sulfite reductase to survive in a range of ecosystems; how atomic-resolution structures of dissimilatory and assimilatory sulfite reductases reveal their ancient homology; how the siroheme-[4Fe-4S] cluster active site catalyzes the six-electron reduction of sulfite to sulfide; and how siroheme is synthesized across diverse microrganisms.