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Updated: Feb 9, 2026

An Anaerobic Biosensor Assay for the Detection of Mercury and Cadmium
Published on: December 17, 2018
Mini-review: toxicity of mercury as a consequence of enzyme alteration
Ruby Ynalvez1, Jose Gutierrez2, Hector Gonzalez-Cantu2
1Department of Biology and Chemistry, Texas A&M International University, 5201 University Blvd., Laredo, TX, 78041, USA. rynalvez@tamiu.edu.
Abstract:
Mercury, in both its elemental and bonded states, is noted for its negative effects on biological organisms. Recent anthropogenic and environmental disasters have spurred numerous comparative studies. These studies attempted to detail the biochemical implications of mercury ingestion, in low, persistent concentrations as well as elevated acute dosages. The studies propose models for mercuric action on healthy cells; which is centered on the element's disruption of key enzymatic processes at deposition sites. Mercury's high affinity for the sulfhydryl moieties of enzyme catalytic sites is a common motif for enzyme inactivation. These permanent covalent modifications inactivate the enzyme, thereby inducing devastating effects on an organism's metabolic functions. Mercury has been shown to be highly nonspecific in its binding to sulfhydryl moieties, and highly varied in terms of how it is encountered by living organisms. This review focuses on mercury's effects on a wide swath of enzymes, with emphasis on how these alterations deleteriously affect several metabolic pathways.
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