Hemoglobin: A mechanism for the generation of hydroxyl radicals
Oxyhemoglobin (HbO 2) reduces Fe(III) NTA aerobically to become methemoglobin (metHb) and Fe(II)NTA. These conditions are favorable for the generation via Fenton chemistry of the hydroxyl radical that was measured by HPLC using salicylate as a probe. The levels of hydroxyl radicals generated are a f...
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| Veröffentlicht in: | Free radical biology & medicine 1996, Vol.20 (7), p.985-989 |
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| container_title | Free radical biology & medicine |
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| creator | Van Dyke, Bruce R. Saltman, Paul |
| description | Oxyhemoglobin (HbO
2) reduces Fe(III) NTA aerobically to become methemoglobin (metHb) and Fe(II)NTA. These conditions are favorable for the generation via Fenton chemistry of the hydroxyl radical that was measured by HPLC using salicylate as a probe. The levels of hydroxyl radicals generated are a function of both the percent metHb formed and the chemical nature of the buffer. The rates of formation of both metHb and hydroxyl radicals were dependent upon the concentration of Fe(III)NTA. Of the buffers tested, HEPES was the most effective scavenger of hydroxyl radicals while the other buffers scavenged in the order: HEPES > Tris > MOPS > NaCl ≈ unbuffered. The addition of catalase to remove H
20
2 or bathophenanthroline to chelate Fe(II) inhibited virtually all hydroxyl radical formation. Carbonyl formation from free radical oxidation of amino acids was found to be 0.1 mol/mol of hemoglobin. These experiments demonstrate the ability of hemoglobin to participate directly in the generation of hydroxyl radicals mediated by redox metals, and provide insight into potential oxidative damage from metals released into the blood during some pathologic disorders including iron overload. |
| doi_str_mv | 10.1016/0891-5849(95)02186-8 |
| format | Article |
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2) reduces Fe(III) NTA aerobically to become methemoglobin (metHb) and Fe(II)NTA. These conditions are favorable for the generation via Fenton chemistry of the hydroxyl radical that was measured by HPLC using salicylate as a probe. The levels of hydroxyl radicals generated are a function of both the percent metHb formed and the chemical nature of the buffer. The rates of formation of both metHb and hydroxyl radicals were dependent upon the concentration of Fe(III)NTA. Of the buffers tested, HEPES was the most effective scavenger of hydroxyl radicals while the other buffers scavenged in the order: HEPES > Tris > MOPS > NaCl ≈ unbuffered. The addition of catalase to remove H
20
2 or bathophenanthroline to chelate Fe(II) inhibited virtually all hydroxyl radical formation. Carbonyl formation from free radical oxidation of amino acids was found to be 0.1 mol/mol of hemoglobin. These experiments demonstrate the ability of hemoglobin to participate directly in the generation of hydroxyl radicals mediated by redox metals, and provide insight into potential oxidative damage from metals released into the blood during some pathologic disorders including iron overload.</description><identifier>ISSN: 0891-5849</identifier><identifier>EISSN: 1873-4596</identifier><identifier>DOI: 10.1016/0891-5849(95)02186-8</identifier><identifier>PMID: 8743985</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acids - chemistry ; Buffers ; Carbonyl formation ; Electron Transport ; Free radical scavengers ; Free radicals ; Hemoglobin ; Hemoglobins - chemistry ; Hydroxybenzoates - metabolism ; Hydroxyl radical ; Hydroxyl Radical - metabolism ; Oxidation-Reduction ; Redox metals</subject><ispartof>Free radical biology & medicine, 1996, Vol.20 (7), p.985-989</ispartof><rights>1996</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c423t-c436baa00a709cbd41ecadcf98269a4a2babebaa99bf5ca58096bc15971151393</citedby><cites>FETCH-LOGICAL-c423t-c436baa00a709cbd41ecadcf98269a4a2babebaa99bf5ca58096bc15971151393</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0891-5849(95)02186-8$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,4024,27923,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8743985$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Van Dyke, Bruce R.</creatorcontrib><creatorcontrib>Saltman, Paul</creatorcontrib><title>Hemoglobin: A mechanism for the generation of hydroxyl radicals</title><title>Free radical biology & medicine</title><addtitle>Free Radic Biol Med</addtitle><description>Oxyhemoglobin (HbO
2) reduces Fe(III) NTA aerobically to become methemoglobin (metHb) and Fe(II)NTA. These conditions are favorable for the generation via Fenton chemistry of the hydroxyl radical that was measured by HPLC using salicylate as a probe. The levels of hydroxyl radicals generated are a function of both the percent metHb formed and the chemical nature of the buffer. The rates of formation of both metHb and hydroxyl radicals were dependent upon the concentration of Fe(III)NTA. Of the buffers tested, HEPES was the most effective scavenger of hydroxyl radicals while the other buffers scavenged in the order: HEPES > Tris > MOPS > NaCl ≈ unbuffered. The addition of catalase to remove H
20
2 or bathophenanthroline to chelate Fe(II) inhibited virtually all hydroxyl radical formation. Carbonyl formation from free radical oxidation of amino acids was found to be 0.1 mol/mol of hemoglobin. These experiments demonstrate the ability of hemoglobin to participate directly in the generation of hydroxyl radicals mediated by redox metals, and provide insight into potential oxidative damage from metals released into the blood during some pathologic disorders including iron overload.</description><subject>Amino Acids - chemistry</subject><subject>Buffers</subject><subject>Carbonyl formation</subject><subject>Electron Transport</subject><subject>Free radical scavengers</subject><subject>Free radicals</subject><subject>Hemoglobin</subject><subject>Hemoglobins - chemistry</subject><subject>Hydroxybenzoates - metabolism</subject><subject>Hydroxyl radical</subject><subject>Hydroxyl Radical - metabolism</subject><subject>Oxidation-Reduction</subject><subject>Redox metals</subject><issn>0891-5849</issn><issn>1873-4596</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1OwzAQhC0EKuXnDUDyCcEhYMd2YnMAVQgoUiUucLZsZ9MaJXGxU0TfnpRWHLnsHHZmVvshdEbJNSW0uCFS0UxIri6VuCI5lUUm99CYypJlXKhiH43_LIfoKKUPQggXTI7QSJacKSnG6H4KbZg3wfruFk9wC25hOp9aXIeI-wXgOXQQTe9Dh0ONF-sqhu91g6OpvDNNOkEH9SBwutNj9P70-PYwzWavzy8Pk1nmeM76YbLCGkOIKYlytuIUnKlcrWReKMNNbo2FwaCUrYUzQhJVWEeFKikVlCl2jC62vcsYPleQet365KBpTAdhlXQpcyYlEYORb40uhpQi1HoZfWviWlOiN9z0BoreQNFK6F9uWg6x813_yrZQ_YV2oIb93XYPw5NfHqJOzkPnoPIRXK-r4P8_8AMD9XzQ</recordid><startdate>1996</startdate><enddate>1996</enddate><creator>Van Dyke, Bruce R.</creator><creator>Saltman, Paul</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>1996</creationdate><title>Hemoglobin: A mechanism for the generation of hydroxyl radicals</title><author>Van Dyke, Bruce R. ; Saltman, Paul</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c423t-c436baa00a709cbd41ecadcf98269a4a2babebaa99bf5ca58096bc15971151393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Amino Acids - chemistry</topic><topic>Buffers</topic><topic>Carbonyl formation</topic><topic>Electron Transport</topic><topic>Free radical scavengers</topic><topic>Free radicals</topic><topic>Hemoglobin</topic><topic>Hemoglobins - chemistry</topic><topic>Hydroxybenzoates - metabolism</topic><topic>Hydroxyl radical</topic><topic>Hydroxyl Radical - metabolism</topic><topic>Oxidation-Reduction</topic><topic>Redox metals</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Van Dyke, Bruce R.</creatorcontrib><creatorcontrib>Saltman, Paul</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Free radical biology & medicine</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Van Dyke, Bruce R.</au><au>Saltman, Paul</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Hemoglobin: A mechanism for the generation of hydroxyl radicals</atitle><jtitle>Free radical biology & medicine</jtitle><addtitle>Free Radic Biol Med</addtitle><date>1996</date><risdate>1996</risdate><volume>20</volume><issue>7</issue><spage>985</spage><epage>989</epage><pages>985-989</pages><issn>0891-5849</issn><eissn>1873-4596</eissn><abstract>Oxyhemoglobin (HbO
2) reduces Fe(III) NTA aerobically to become methemoglobin (metHb) and Fe(II)NTA. These conditions are favorable for the generation via Fenton chemistry of the hydroxyl radical that was measured by HPLC using salicylate as a probe. The levels of hydroxyl radicals generated are a function of both the percent metHb formed and the chemical nature of the buffer. The rates of formation of both metHb and hydroxyl radicals were dependent upon the concentration of Fe(III)NTA. Of the buffers tested, HEPES was the most effective scavenger of hydroxyl radicals while the other buffers scavenged in the order: HEPES > Tris > MOPS > NaCl ≈ unbuffered. The addition of catalase to remove H
20
2 or bathophenanthroline to chelate Fe(II) inhibited virtually all hydroxyl radical formation. Carbonyl formation from free radical oxidation of amino acids was found to be 0.1 mol/mol of hemoglobin. These experiments demonstrate the ability of hemoglobin to participate directly in the generation of hydroxyl radicals mediated by redox metals, and provide insight into potential oxidative damage from metals released into the blood during some pathologic disorders including iron overload.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>8743985</pmid><doi>10.1016/0891-5849(95)02186-8</doi><tpages>5</tpages></addata></record> |
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| ispartof | Free radical biology & medicine, 1996, Vol.20 (7), p.985-989 |
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| language | eng |
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| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Amino Acids - chemistry Buffers Carbonyl formation Electron Transport Free radical scavengers Free radicals Hemoglobin Hemoglobins - chemistry Hydroxybenzoates - metabolism Hydroxyl radical Hydroxyl Radical - metabolism Oxidation-Reduction Redox metals |
| title | Hemoglobin: A mechanism for the generation of hydroxyl radicals |
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