Oxidation of the mercurous ion by peroxidase
The kinetics of oxidation of the mercurous ion by peroxidase have been measured by following the disappearance of mercurous ion using cold-vapour atomic absorption spectroscopy. Pseudo-first-order kinetics are observed with respect to mercurous ion, and the pseudo-first-order rate constants are line...
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Veröffentlicht in: | Canadian journal of chemistry 1986-05, Vol.64 (5), p.969-972 |
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description | The kinetics of oxidation of the mercurous ion by peroxidase have been measured by following the disappearance of mercurous ion using cold-vapour atomic absorption spectroscopy. Pseudo-first-order kinetics are observed with respect to mercurous ion, and the pseudo-first-order rate constants are linearly related to peroxidase concentration, showing first-order dependence on peroxidase. This behaviour is identical to oxidation of elemental mercury, and the second-order rate constant, 1.44 × 10
4
M
−1
s
−1
at 23 °C, is also, within experimental error, the same as that for elemental mercury oxidation. The data are interpreted in terms of peroxidase-induced disproportionation of the mercurous dimer, followed by two-electron oxidation of zero-valent mercury. |
doi_str_mv | 10.1139/v86-162 |
format | Article |
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4
M
−1
s
−1
at 23 °C, is also, within experimental error, the same as that for elemental mercury oxidation. The data are interpreted in terms of peroxidase-induced disproportionation of the mercurous dimer, followed by two-electron oxidation of zero-valent mercury.</description><identifier>ISSN: 0008-4042</identifier><identifier>EISSN: 1480-3291</identifier><identifier>DOI: 10.1139/v86-162</identifier><identifier>CODEN: CJCHAG</identifier><language>eng</language><publisher>Ottawa, Canada: NRC Research Press</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Oxidoreductases</subject><ispartof>Canadian journal of chemistry, 1986-05, Vol.64 (5), p.969-972</ispartof><rights>1987 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://cdnsciencepub.com/doi/pdf/10.1139/v86-162$$EPDF$$P50$$Gnrcresearch$$H</linktopdf><linktohtml>$$Uhttps://cdnsciencepub.com/doi/full/10.1139/v86-162$$EHTML$$P50$$Gnrcresearch$$H</linktohtml><link.rule.ids>314,780,784,2932,27924,27925,64428,65234</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=8188223$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Wigfield, Donald C</creatorcontrib><creatorcontrib>Tse, Season</creatorcontrib><title>Oxidation of the mercurous ion by peroxidase</title><title>Canadian journal of chemistry</title><addtitle>Revue canadienne de chimie</addtitle><description>The kinetics of oxidation of the mercurous ion by peroxidase have been measured by following the disappearance of mercurous ion using cold-vapour atomic absorption spectroscopy. Pseudo-first-order kinetics are observed with respect to mercurous ion, and the pseudo-first-order rate constants are linearly related to peroxidase concentration, showing first-order dependence on peroxidase. This behaviour is identical to oxidation of elemental mercury, and the second-order rate constant, 1.44 × 10
4
M
−1
s
−1
at 23 °C, is also, within experimental error, the same as that for elemental mercury oxidation. The data are interpreted in terms of peroxidase-induced disproportionation of the mercurous dimer, followed by two-electron oxidation of zero-valent mercury.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Oxidoreductases</subject><issn>0008-4042</issn><issn>1480-3291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1986</creationdate><recordtype>article</recordtype><recordid>eNp1z01Lw0AQBuBFFIxV_As5iIIYnZl87R6l-AWFXvQcNptZGmmTsJuK_ffd0tKD4GmY4eEdXiGuER4RU_X0I4sECzoREWYSkpQUnooIAGSSQUbn4sL777CWQHkkHua_baPHtu_i3sbjguMVO7N2_drHu2O9iQd2_Q55vhRnVi89Xx3mRHy9vnxO35PZ_O1j-jxLDEkak6bOQFpWlmpGSMusMGywbNBqzkkpVSqtGRuTgU6plJJyJAuNrSWBpSKdiLt9rnG9945tNbh2pd2mQqh2JatQsgolg7zZy0F7o5fW6c60_sglhnBKA7vds84Zx561M4sjOmRVQ2MDvP8f_n2-BZsna8g</recordid><startdate>19860501</startdate><enddate>19860501</enddate><creator>Wigfield, Donald C</creator><creator>Tse, Season</creator><general>NRC Research Press</general><general>National Research Council of Canada</general><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>19860501</creationdate><title>Oxidation of the mercurous ion by peroxidase</title><author>Wigfield, Donald C ; Tse, Season</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c282t-db408fe9f2be103746cec17d1fae5299979aae1dc40a327882512f0dfb820f263</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1986</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Oxidoreductases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wigfield, Donald C</creatorcontrib><creatorcontrib>Tse, Season</creatorcontrib><collection>Pascal-Francis</collection><collection>CrossRef</collection><jtitle>Canadian journal of chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wigfield, Donald C</au><au>Tse, Season</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Oxidation of the mercurous ion by peroxidase</atitle><jtitle>Canadian journal of chemistry</jtitle><addtitle>Revue canadienne de chimie</addtitle><date>1986-05-01</date><risdate>1986</risdate><volume>64</volume><issue>5</issue><spage>969</spage><epage>972</epage><pages>969-972</pages><issn>0008-4042</issn><eissn>1480-3291</eissn><coden>CJCHAG</coden><abstract>The kinetics of oxidation of the mercurous ion by peroxidase have been measured by following the disappearance of mercurous ion using cold-vapour atomic absorption spectroscopy. Pseudo-first-order kinetics are observed with respect to mercurous ion, and the pseudo-first-order rate constants are linearly related to peroxidase concentration, showing first-order dependence on peroxidase. This behaviour is identical to oxidation of elemental mercury, and the second-order rate constant, 1.44 × 10
4
M
−1
s
−1
at 23 °C, is also, within experimental error, the same as that for elemental mercury oxidation. The data are interpreted in terms of peroxidase-induced disproportionation of the mercurous dimer, followed by two-electron oxidation of zero-valent mercury.</abstract><cop>Ottawa, Canada</cop><pub>NRC Research Press</pub><doi>10.1139/v86-162</doi><tpages>4</tpages></addata></record> |
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subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Oxidoreductases |
title | Oxidation of the mercurous ion by peroxidase |
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