Iron and Its Importance to Nutrition and Health

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It may be taken for granted the impact that the food we eat has to our overall health. The body absorbs nutrients, such as vitamins and minerals, from the food that is consumed and uses it in several functions. These vitamins and minerals play many vital roles in reactions and metabolic pathways. Dietary iron is a mineral that is essential to several functions of the body and deficiency will result in negative effects.

Iron is an element with the symbol Fe on the periodic table. Its atomic number is 26 and its atomic mass is 55.845 g/mol (8). Synonyms of iron include: ferrum, ferrous ion, ferryl ion, and ferric ion (1,8). Iron plays an important role in the human body “existing in complex forms bound to protein (hemoprotein), as heme compounds (hemoglobin or myoglobin), heme enzymes, or nonheme compounds (flavin-iron enzymes, transferrin, and ferritin)” (1). The importance of iron in the body stems from its ability to interconvert readily between two relatively stable oxidation states (Fe2+or ferrous iron and Fe3+or ferric iron). This ability makes iron a useful component of oxygen-binding molecules in hemoglobin and myoglobin, cytochrome and diverse enzymatic reactions including DNA synthesis, lipid metabolism and free radical scavenging.

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Iron plays a role in several metabolic pathways. “By exploiting the oxidation state, redox potential and electron spin state of iron, it is particularly suited to participate in a large number of useful biochemical reactions” (12). Iron is a cofactor; a non-protein essential molecule to enzymatic function. A specific enzyme that utilizes iron as a cofactor is tryptophan hydroxylase. This enzyme catalyzes the reaction of tryptophan hydroxylation to produce 5-hydroxytryptophan, which is the first step of the production of serotonin; a neurotransmitter that plays a role in regulating mood (12). Iron’s role in the reaction of tryptophan hydroxylation, “can be described in two parts: 1) reaction of the tetrahydropterin, oxygen, and the active site iron to form the reactive hydroxylating intermediate and 2) insertion of oxygen into the amino acid substrate” (12). The specific mechanism at the iron activation site involves the interaction of 4a-peroxypterin either as the formation of a Fe II-peroxypterin intermediate or the direct transfer of an oxygen atom (12). The result of hydroxylation of tryptophan is the addition of a hydroxyl group to the amino acid. Just as iron is a useful cofactor to tryptophan hydroxylase, it is a cofactor to several other enzymes as well such as: tyrosine hydroxylase, tryptophan hydroxylase, xanthine oxidase and ribonucleoside reductase (12). Without iron, these enzymes would not function properly and the reactions that they catalyze would be affected. Therefore, the body needs iron for the catalysis of metabolic reactions.

For the body to utilize iron, it must be consumed, absorbed and metabolized. Once iron is consumed, it is absorbed in the small intestine,

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