Defining the involvement of HOCl or Cl sub(2) as enzyme-generated intermediates in chloroperoxidase-catalyzed reactions
Peroxidatic substrates, catechol (CAT) and 2,4,6-trimethylphenol (TMP) were used as probes of the chloride-dependent reactions catalyzed by chloroperoxidase (CPO). All data are consistent with a mechanism in which chloride competes with CAT for binding to both CPO compound I and the CPO chlorinating...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-01, Vol.267 (3), p.1769-1775 |
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| container_end_page | 1775 |
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| container_issue | 3 |
| container_start_page | 1769 |
| container_title | The Journal of biological chemistry |
| container_volume | 267 |
| creator | Libby, R D Shedd, AL Phipps, A K Beachy, T M Gerstberger, S M |
| description | Peroxidatic substrates, catechol (CAT) and 2,4,6-trimethylphenol (TMP) were used as probes of the chloride-dependent reactions catalyzed by chloroperoxidase (CPO). All data are consistent with a mechanism in which chloride competes with CAT for binding to both CPO compound I and the CPO chlorinating intermediate (EOCl). Chloride binding to CPO compound I leads to the formation of EOCl and initiates the CPO chloride-dependent pathway. When CAT binds to either compound I or EOCl, it is directly oxidized to product. When chloride binds to EOCl, it either induces release of HOCl or reacts with EOCl to produce Cl sub(2), which is released from the enzyme. TMP and CAT compete for reaction with the free oxidized halogen species. This is the first direct evidence for kinetically significant involvement of a free oxidized halogen species as an intermediate in any CPO-catalyzed reaction. |
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All data are consistent with a mechanism in which chloride competes with CAT for binding to both CPO compound I and the CPO chlorinating intermediate (EOCl). Chloride binding to CPO compound I leads to the formation of EOCl and initiates the CPO chloride-dependent pathway. When CAT binds to either compound I or EOCl, it is directly oxidized to product. When chloride binds to EOCl, it either induces release of HOCl or reacts with EOCl to produce Cl sub(2), which is released from the enzyme. TMP and CAT compete for reaction with the free oxidized halogen species. 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All data are consistent with a mechanism in which chloride competes with CAT for binding to both CPO compound I and the CPO chlorinating intermediate (EOCl). Chloride binding to CPO compound I leads to the formation of EOCl and initiates the CPO chloride-dependent pathway. When CAT binds to either compound I or EOCl, it is directly oxidized to product. When chloride binds to EOCl, it either induces release of HOCl or reacts with EOCl to produce Cl sub(2), which is released from the enzyme. TMP and CAT compete for reaction with the free oxidized halogen species. This is the first direct evidence for kinetically significant involvement of a free oxidized halogen species as an intermediate in any CPO-catalyzed reaction.</description><subject>2,4,6-trimethylphenol</subject><subject>catechol</subject><subject>chloride</subject><issn>0021-9258</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNqNi7tuwkAURLcAKTzyD7dCpLBkGxuFGojo0tCjxR7jjdZ7Ye-a19ezRT6AKWZ0pDMDNUrTPEtWefn9ocYif2lMscpG6rZBY5xxJwotyLgr2ys6uEDc0O53bYk9xZb-OM-_SAvBPR8dkhMcvA6o4ynAd6hNJIlEVWvZ8xme76bWgqTSQdvHM7oeugqGnUzVsNFW8Pm_EzX72e7Xu-Ts-dJDwqEzUsFa7cC9HLJlVi7LRbF4W3wBV3VQHw</recordid><startdate>19920101</startdate><enddate>19920101</enddate><creator>Libby, R D</creator><creator>Shedd, AL</creator><creator>Phipps, A K</creator><creator>Beachy, T M</creator><creator>Gerstberger, S M</creator><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope></search><sort><creationdate>19920101</creationdate><title>Defining the involvement of HOCl or Cl sub(2) as enzyme-generated intermediates in chloroperoxidase-catalyzed reactions</title><author>Libby, R D ; Shedd, AL ; Phipps, A K ; Beachy, T M ; Gerstberger, S M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-proquest_miscellaneous_161565343</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>2,4,6-trimethylphenol</topic><topic>catechol</topic><topic>chloride</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Libby, R D</creatorcontrib><creatorcontrib>Shedd, AL</creatorcontrib><creatorcontrib>Phipps, A K</creatorcontrib><creatorcontrib>Beachy, T M</creatorcontrib><creatorcontrib>Gerstberger, S M</creatorcontrib><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Libby, R D</au><au>Shedd, AL</au><au>Phipps, A K</au><au>Beachy, T M</au><au>Gerstberger, S M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Defining the involvement of HOCl or Cl sub(2) as enzyme-generated intermediates in chloroperoxidase-catalyzed reactions</atitle><jtitle>The Journal of biological chemistry</jtitle><date>1992-01-01</date><risdate>1992</risdate><volume>267</volume><issue>3</issue><spage>1769</spage><epage>1775</epage><pages>1769-1775</pages><issn>0021-9258</issn><abstract>Peroxidatic substrates, catechol (CAT) and 2,4,6-trimethylphenol (TMP) were used as probes of the chloride-dependent reactions catalyzed by chloroperoxidase (CPO). All data are consistent with a mechanism in which chloride competes with CAT for binding to both CPO compound I and the CPO chlorinating intermediate (EOCl). Chloride binding to CPO compound I leads to the formation of EOCl and initiates the CPO chloride-dependent pathway. When CAT binds to either compound I or EOCl, it is directly oxidized to product. When chloride binds to EOCl, it either induces release of HOCl or reacts with EOCl to produce Cl sub(2), which is released from the enzyme. TMP and CAT compete for reaction with the free oxidized halogen species. This is the first direct evidence for kinetically significant involvement of a free oxidized halogen species as an intermediate in any CPO-catalyzed reaction.</abstract></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1992-01, Vol.267 (3), p.1769-1775 |
| issn | 0021-9258 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_16156534 |
| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | 2,4,6-trimethylphenol catechol chloride |
| title | Defining the involvement of HOCl or Cl sub(2) as enzyme-generated intermediates in chloroperoxidase-catalyzed reactions |
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