{"title":"酶改变引起的汞毒性——综述。","authors":"Ruby A Ynalvez, Rene A Rangel, Jose A Gutierrez","doi":"10.1007/s10534-025-00663-z","DOIUrl":null,"url":null,"abstract":"<p><p>Mercury is widely known for its detrimental effects on living organisms, whether in its elemental or bonded states. Recent comparative studies have shed light on the biochemical implications of mercury ingestion, both in low, persistent concentrations and in elevated acute dosages. Studies have presented models that elucidate how mercury disrupts healthy cells. Mercury's unique ability to interfere with crucial enzymatic processes at deposition sites is a vital feature of these models. The strong affinity for the sulfhydryl moieties of enzyme catalytic sites leads to enzyme inactivation through permanent covalent modifications. This inactivation can have catastrophic effects on an organism's metabolic functions. Moreover, it has been found that mercury's binding to sulfhydryl moieties is highly nonspecific and can occur in various ways. This review aimed to explore the effects of mercury on a broad spectrum of enzymes with a specific focus on how these alterations can detrimentally affect several metabolic pathways.</p>","PeriodicalId":491,"journal":{"name":"Biometals","volume":" ","pages":""},"PeriodicalIF":4.1000,"publicationDate":"2025-01-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Mercury toxicity resulting from enzyme alterations- minireview.\",\"authors\":\"Ruby A Ynalvez, Rene A Rangel, Jose A Gutierrez\",\"doi\":\"10.1007/s10534-025-00663-z\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Mercury is widely known for its detrimental effects on living organisms, whether in its elemental or bonded states. Recent comparative studies have shed light on the biochemical implications of mercury ingestion, both in low, persistent concentrations and in elevated acute dosages. Studies have presented models that elucidate how mercury disrupts healthy cells. Mercury's unique ability to interfere with crucial enzymatic processes at deposition sites is a vital feature of these models. The strong affinity for the sulfhydryl moieties of enzyme catalytic sites leads to enzyme inactivation through permanent covalent modifications. This inactivation can have catastrophic effects on an organism's metabolic functions. Moreover, it has been found that mercury's binding to sulfhydryl moieties is highly nonspecific and can occur in various ways. This review aimed to explore the effects of mercury on a broad spectrum of enzymes with a specific focus on how these alterations can detrimentally affect several metabolic pathways.</p>\",\"PeriodicalId\":491,\"journal\":{\"name\":\"Biometals\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":4.1000,\"publicationDate\":\"2025-01-16\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biometals\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1007/s10534-025-00663-z\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biometals","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1007/s10534-025-00663-z","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Mercury toxicity resulting from enzyme alterations- minireview.
Mercury is widely known for its detrimental effects on living organisms, whether in its elemental or bonded states. Recent comparative studies have shed light on the biochemical implications of mercury ingestion, both in low, persistent concentrations and in elevated acute dosages. Studies have presented models that elucidate how mercury disrupts healthy cells. Mercury's unique ability to interfere with crucial enzymatic processes at deposition sites is a vital feature of these models. The strong affinity for the sulfhydryl moieties of enzyme catalytic sites leads to enzyme inactivation through permanent covalent modifications. This inactivation can have catastrophic effects on an organism's metabolic functions. Moreover, it has been found that mercury's binding to sulfhydryl moieties is highly nonspecific and can occur in various ways. This review aimed to explore the effects of mercury on a broad spectrum of enzymes with a specific focus on how these alterations can detrimentally affect several metabolic pathways.
期刊介绍:
BioMetals is the only established journal to feature the important role of metal ions in chemistry, biology, biochemistry, environmental science, and medicine. BioMetals is an international, multidisciplinary journal singularly devoted to the rapid publication of the fundamental advances of both basic and applied research in this field. BioMetals offers a forum for innovative research and clinical results on the structure and function of:
- metal ions
- metal chelates,
- siderophores,
- metal-containing proteins
- biominerals in all biosystems.
- BioMetals rapidly publishes original articles and reviews.
BioMetals is a journal for metals researchers who practice in medicine, biochemistry, pharmacology, toxicology, microbiology, cell biology, chemistry, and plant physiology who are based academic, industrial and government laboratories.