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Enzymatic oxidation of mercury vapor by erythrocytes

Journal Article:

Abstract

The formation of glutathione radicals, the evolution of nascent oxygen or the peroxidatic reaction with catalase complex I are considered as possible mechanisms for the oxidation of mercury vapor by red blood cells. To select among these, the uptake of atomic mercury by erythrocytes from different species was studied and related to their various activities of catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase, EC 1.11.1.6) and glutathione peroxidase (glutathione:hydrogen-peroxide oxidoreductase, EC 1.11.1.9). A slow and continuouus infusion of diluted H/sub 2/O/sub 2/ was used to maintain steady concentrations of complex I. 1% red cell suspensions were found most suitable showing high rates of Hg uptake and yielding still enough cells for subsequent determinations. The results indicate that the oxidation of mercury depends upon the H/sub 2/O/sub 2/-generation rate and upon the specific acticity of red-cell catalase. The oxidation occurred in a range of the catalase-H/sub 2/O/sub 2/ reaction where the evolution of oxygen could be excluded. Compounds reacting with complex I were shown to be effective inhibitors of the mercury uptake. GSH-peroxidase did not participate in the oxidation but rather, was found to inhibit it by competing with catalase for hydrogen peroxide. These findings support the view that elemental mercury is oxidized in erythrocytes  More>>
Publication Date:
Jan 01, 1978
Product Type:
Journal Article
Reference Number:
ERA-05-004946; EDB-80-002301
Resource Relation:
Journal Name: Biochim. Biophys. Acta; (Netherlands); Journal Volume: 523
Subject:
59 BASIC BIOLOGICAL SCIENCES; 63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; ERYTHROCYTES; BIOCHEMICAL REACTION KINETICS; MERCURY; OXIDATION; PEROXIDASES; CATALASE; HYDROGEN PEROXIDE; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY FLUIDS; CARBOXYLIC ACIDS; CHEMICAL REACTIONS; ELEMENTS; ENZYMES; HETEROCYCLIC ACIDS; HETEROCYCLIC COMPOUNDS; HYDROGEN COMPOUNDS; KINETICS; METALS; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC NITROGEN COMPOUNDS; OXIDOREDUCTASES; OXYGEN COMPOUNDS; PEROXIDES; PORPHYRINS; REACTION KINETICS; 550200* - Biochemistry; 550500 - Metabolism; 560301 - Chemicals Metabolism & Toxicology- Cells- (-1987)
OSTI ID:
5775346
Research Organizations:
Univ. of Rochester, NY
Country of Origin:
Netherlands
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: BBACA
Submitting Site:
TIC
Size:
Pages: 525-531
Announcement Date:

Journal Article:

Citation Formats

Halbach, S, and Clarkson, T W. Enzymatic oxidation of mercury vapor by erythrocytes. Netherlands: N. p., 1978. Web.
Halbach, S, & Clarkson, T W. Enzymatic oxidation of mercury vapor by erythrocytes. Netherlands.
Halbach, S, and Clarkson, T W. 1978. "Enzymatic oxidation of mercury vapor by erythrocytes." Netherlands.
@misc{etde_5775346,
title = {Enzymatic oxidation of mercury vapor by erythrocytes}
author = {Halbach, S, and Clarkson, T W}
abstractNote = {The formation of glutathione radicals, the evolution of nascent oxygen or the peroxidatic reaction with catalase complex I are considered as possible mechanisms for the oxidation of mercury vapor by red blood cells. To select among these, the uptake of atomic mercury by erythrocytes from different species was studied and related to their various activities of catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase, EC 1.11.1.6) and glutathione peroxidase (glutathione:hydrogen-peroxide oxidoreductase, EC 1.11.1.9). A slow and continuouus infusion of diluted H/sub 2/O/sub 2/ was used to maintain steady concentrations of complex I. 1% red cell suspensions were found most suitable showing high rates of Hg uptake and yielding still enough cells for subsequent determinations. The results indicate that the oxidation of mercury depends upon the H/sub 2/O/sub 2/-generation rate and upon the specific acticity of red-cell catalase. The oxidation occurred in a range of the catalase-H/sub 2/O/sub 2/ reaction where the evolution of oxygen could be excluded. Compounds reacting with complex I were shown to be effective inhibitors of the mercury uptake. GSH-peroxidase did not participate in the oxidation but rather, was found to inhibit it by competing with catalase for hydrogen peroxide. These findings support the view that elemental mercury is oxidized in erythrocytes by a peroxidatic reaction with complex I only.}
journal = {Biochim. Biophys. Acta; (Netherlands)}
volume = {523}
journal type = {AC}
place = {Netherlands}
year = {1978}
month = {Jan}
}