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Mini-review: toxicity of mercury as a consequence of enzyme alteration
Biometals, 2016-10, Vol.29 (5), p.781-788
[Peer Reviewed Journal]
Springer Science+Business Media New York 2016 ;ISSN: 0966-0844 ;EISSN: 1572-8773 ;DOI: 10.1007/s10534-016-9967-8 ;PMID: 27591997
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Title:
Mini-review: toxicity of mercury as a consequence of enzyme alteration
Author:
Ynalvez, Ruby
;
Gutierrez, Jose
;
Gonzalez-Cantu, Hector
Subjects:
Alterations
;
Animals
;
Binding
;
Biochemistry
;
Biomedical and Life Sciences
;
Cell Biology
;
Comparative studies
;
Disasters
;
Enzymes
;
Enzymes - metabolism
;
Humans
;
Ingestion
;
Life Sciences
;
Medicine/Public Health
;
Mercury
;
Mercury (metal)
;
Mercury - adverse effects
;
Mercury - chemistry
;
Mercury - metabolism
;
Mercury - toxicity
;
Microbiology
;
Organisms
;
Pharmacology/Toxicology
;
Plant Physiology
;
Toxicity
Is Part Of:
Biometals, 2016-10, Vol.29 (5), p.781-788
Description:
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.
Publisher:
Dordrecht: Springer Netherlands
Language:
English;Dutch
Identifier:
ISSN: 0966-0844
EISSN: 1572-8773
DOI: 10.1007/s10534-016-9967-8
PMID: 27591997
Source:
AUTh Library subscriptions: ProQuest Central
MEDLINE
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