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Mini-review: toxicity of mercury as a consequence of enzyme alteration

Mini-review: toxicity of mercury as a consequence of enzyme alteration 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png BioMetals Springer Journals

Mini-review: toxicity of mercury as a consequence of enzyme alteration

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References (25)

Publisher
Springer Journals
Copyright
Copyright © 2016 by Springer Science+Business Media New York
Subject
Life Sciences; Biochemistry, general; Pharmacology/Toxicology; Microbiology; Cell Biology; Plant Physiology; Medicine/Public Health, general
ISSN
0966-0844
eISSN
1572-8773
DOI
10.1007/s10534-016-9967-8
pmid
27591997
Publisher site
See Article on Publisher Site

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.

Journal

BioMetals – Springer Journals

Published: Sep 3, 2016

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