A large and functionally diverse group of enzymes that require iron, typically in the form of a heme group or iron-sulfur cluster, to catalyze essential biochemical reactions within the human body. These iron-dependent enzymes are indispensable for fundamental processes such as cellular respiration, DNA synthesis, and the metabolism of numerous hormones and neurotransmitters. Examples include cytochromes in the electron transport chain and hydroxylase enzymes crucial for steroid and thyroid hormone production. A compromised iron status directly impairs the function of these critical cofactors, leading to systemic metabolic and endocrine disruption.
Origin
This term is rooted in biochemistry and metalloenzyme science, combining ‘iron cofactor,’ the non-protein chemical compound necessary for enzyme activity, and ‘enzymes,’ the biological catalysts. The discovery of iron’s role in vital enzymatic processes dates back to early studies of cellular respiration and oxygen transport. This concept underscores the essential link between micronutrient status and core physiological function.
Mechanism
The iron atom within the enzyme structure functions as a reversible electron carrier or as a site for binding and activating substrates, particularly oxygen. In the case of hydroxylases, iron facilitates the addition of a hydroxyl group to a substrate, a critical step in the biosynthesis of steroid hormones like cortisol and sex hormones. For the cytochromes, the iron atom cycles between ferrous (Fe²⁺) and ferric (Fe³⁺) states, enabling the efficient transfer of electrons down the respiratory chain to generate ATP. The precise coordination of iron within the active site is vital for maintaining the enzyme’s catalytic efficiency.
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