Mechanism for the autoxidation of hemoglobin by phenols, nitrite and “oxidant” drugs. Peroxide formation by one electron donation to bound dioxygen
The reaction of HbO 2 with phenols to produce metHb shows inverse rate dependence upon [H +], direct dependence upon [HbO 2] and [phenol], and a rate that correlates with the electron donor characteristics of the reagents. Thus, the availability of an electron from an external agent permits facile r...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1975-02, Vol.62 (3), p.561-567 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Wallace, William J. Caughey, Winslow S. |
| description | The reaction of HbO
2 with phenols to produce metHb shows inverse rate dependence upon [H
+], direct dependence upon [HbO
2] and [phenol], and a rate that correlates with the electron donor characteristics of the reagents. Thus, the availability of an electron from an external agent permits facile reduction of O
2 to O
2
= and the reaction of HbO
2 with phenols gives rise to metHb and peroxide as reaction products. In contrast, with nucleophiles such as azide O
2 is displaced as superoxide. Since reduction of bound O
2 is seen to occur only by reductive displacement or by reaction with a single electron donor, Hb apparently owes its normal resistance to autoxidation to the isolation of the binding site from electron donors and nucleophiles and not to an unique kind of iron-O
2 bonding. Such reasoning explains the effects of structural abnormality that render M-type Hbs susceptible to oxidation. Also the oxidation of HbO
2 upon exposure to “oxidant drugs” is explicable in terms of the drugs acting as one electron reducing agents towards bound dioxygen. |
| doi_str_mv | 10.1016/0006-291X(75)90435-0 |
| format | Article |
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2 with phenols to produce metHb shows inverse rate dependence upon [H
+], direct dependence upon [HbO
2] and [phenol], and a rate that correlates with the electron donor characteristics of the reagents. Thus, the availability of an electron from an external agent permits facile reduction of O
2 to O
2
= and the reaction of HbO
2 with phenols gives rise to metHb and peroxide as reaction products. In contrast, with nucleophiles such as azide O
2 is displaced as superoxide. Since reduction of bound O
2 is seen to occur only by reductive displacement or by reaction with a single electron donor, Hb apparently owes its normal resistance to autoxidation to the isolation of the binding site from electron donors and nucleophiles and not to an unique kind of iron-O
2 bonding. Such reasoning explains the effects of structural abnormality that render M-type Hbs susceptible to oxidation. Also the oxidation of HbO
2 upon exposure to “oxidant drugs” is explicable in terms of the drugs acting as one electron reducing agents towards bound dioxygen.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(75)90435-0</identifier><identifier>PMID: 1120068</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Azides ; Binding Sites ; Electron Transport ; Hemoglobins ; Humans ; Hydroquinones ; Iron ; Nitrites ; Nitrophenols ; Oxidation-Reduction ; Peroxides ; Phenols ; Protein Binding ; Protein Conformation ; Resorcinols ; Salicylates</subject><ispartof>Biochemical and biophysical research communications, 1975-02, Vol.62 (3), p.561-567</ispartof><rights>1975</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c338t-c8cc8c9ac941b169e8a7ca5fbe837cc624524c15a2e61fe623dacf45edb9284d3</citedby><cites>FETCH-LOGICAL-c338t-c8cc8c9ac941b169e8a7ca5fbe837cc624524c15a2e61fe623dacf45edb9284d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0006-291X(75)90435-0$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1120068$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wallace, William J.</creatorcontrib><creatorcontrib>Caughey, Winslow S.</creatorcontrib><title>Mechanism for the autoxidation of hemoglobin by phenols, nitrite and “oxidant” drugs. Peroxide formation by one electron donation to bound dioxygen</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The reaction of HbO
2 with phenols to produce metHb shows inverse rate dependence upon [H
+], direct dependence upon [HbO
2] and [phenol], and a rate that correlates with the electron donor characteristics of the reagents. Thus, the availability of an electron from an external agent permits facile reduction of O
2 to O
2
= and the reaction of HbO
2 with phenols gives rise to metHb and peroxide as reaction products. In contrast, with nucleophiles such as azide O
2 is displaced as superoxide. Since reduction of bound O
2 is seen to occur only by reductive displacement or by reaction with a single electron donor, Hb apparently owes its normal resistance to autoxidation to the isolation of the binding site from electron donors and nucleophiles and not to an unique kind of iron-O
2 bonding. Such reasoning explains the effects of structural abnormality that render M-type Hbs susceptible to oxidation. Also the oxidation of HbO
2 upon exposure to “oxidant drugs” is explicable in terms of the drugs acting as one electron reducing agents towards bound dioxygen.</description><subject>Azides</subject><subject>Binding Sites</subject><subject>Electron Transport</subject><subject>Hemoglobins</subject><subject>Humans</subject><subject>Hydroquinones</subject><subject>Iron</subject><subject>Nitrites</subject><subject>Nitrophenols</subject><subject>Oxidation-Reduction</subject><subject>Peroxides</subject><subject>Phenols</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Resorcinols</subject><subject>Salicylates</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1975</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9Uc1qFTEYDaLU2-obKGQlFpyaZDI_2RSktCpU2oWCu5BJvrk3ZSa5JpnSu-tbdKMv1ycx0yl1JwQ-kvMTvnMQekPJESW0_kgIqQsm6M_3TXUoCC-rgjxDK0oEKRgl_DlaPVFeov0YrwihlNdiD-1RyjLUrtDdN9Ab5Wwcce8DThvAakr-xhqVrHfY93gDo18PvrMOdzu83YDzQ_yAnU3Bpkx3Bt_f_n6QuHR_-webMK3jEb6EMD_CbDwublnvHWAYQKeQ78a7BUged37KTsb6m90a3Cv0oldDhNeP8wD9ODv9fvKlOL_4_PXk03mhy7JNhW51PkJpwWlHawGtarSq-g7astG6ZrxiXNNKMahpDzUrjdI9r8B0grXclAfo3eK7Df7XBDHJ0UYNw6Ac-CnKljUtI6LJRL4QdfAxBujlNthRhZ2kRM59yDlsOYctm0o-9CFJlr199J-6Ecw_0VJAxo8XHPKS1xaCjNqC02BsyCFJ4-3_P_gLNhSgEg</recordid><startdate>19750203</startdate><enddate>19750203</enddate><creator>Wallace, William J.</creator><creator>Caughey, Winslow S.</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>19750203</creationdate><title>Mechanism for the autoxidation of hemoglobin by phenols, nitrite and “oxidant” drugs. Peroxide formation by one electron donation to bound dioxygen</title><author>Wallace, William J. ; Caughey, Winslow S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c338t-c8cc8c9ac941b169e8a7ca5fbe837cc624524c15a2e61fe623dacf45edb9284d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1975</creationdate><topic>Azides</topic><topic>Binding Sites</topic><topic>Electron Transport</topic><topic>Hemoglobins</topic><topic>Humans</topic><topic>Hydroquinones</topic><topic>Iron</topic><topic>Nitrites</topic><topic>Nitrophenols</topic><topic>Oxidation-Reduction</topic><topic>Peroxides</topic><topic>Phenols</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Resorcinols</topic><topic>Salicylates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wallace, William J.</creatorcontrib><creatorcontrib>Caughey, Winslow S.</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>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wallace, William J.</au><au>Caughey, Winslow S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Mechanism for the autoxidation of hemoglobin by phenols, nitrite and “oxidant” drugs. Peroxide formation by one electron donation to bound dioxygen</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1975-02-03</date><risdate>1975</risdate><volume>62</volume><issue>3</issue><spage>561</spage><epage>567</epage><pages>561-567</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The reaction of HbO
2 with phenols to produce metHb shows inverse rate dependence upon [H
+], direct dependence upon [HbO
2] and [phenol], and a rate that correlates with the electron donor characteristics of the reagents. Thus, the availability of an electron from an external agent permits facile reduction of O
2 to O
2
= and the reaction of HbO
2 with phenols gives rise to metHb and peroxide as reaction products. In contrast, with nucleophiles such as azide O
2 is displaced as superoxide. Since reduction of bound O
2 is seen to occur only by reductive displacement or by reaction with a single electron donor, Hb apparently owes its normal resistance to autoxidation to the isolation of the binding site from electron donors and nucleophiles and not to an unique kind of iron-O
2 bonding. Such reasoning explains the effects of structural abnormality that render M-type Hbs susceptible to oxidation. Also the oxidation of HbO
2 upon exposure to “oxidant drugs” is explicable in terms of the drugs acting as one electron reducing agents towards bound dioxygen.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>1120068</pmid><doi>10.1016/0006-291X(75)90435-0</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Biochemical and biophysical research communications, 1975-02, Vol.62 (3), p.561-567 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_82782097 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Azides Binding Sites Electron Transport Hemoglobins Humans Hydroquinones Iron Nitrites Nitrophenols Oxidation-Reduction Peroxides Phenols Protein Binding Protein Conformation Resorcinols Salicylates |
| title | Mechanism for the autoxidation of hemoglobin by phenols, nitrite and “oxidant” drugs. Peroxide formation by one electron donation to bound dioxygen |
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