A resonance Raman study of substrate and inhibitor binding to protocatechuate-3,4-dioxygenase
Resonance Raman spectra were obtained for complexes of protocatechuate-3,4-dioxygenase with substrate and hydroxybenzoate inhibitors. The data establish metal coordination by these bound species and demonstrate further that tyrosine ligation, present in the resting enzyme, is not altered in the comp...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1978-11, Vol.85 (2), p.844-850 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Felton, R.H. Cheung, L.D. Phillips, Robert S. May, Sheldon W. |
| description | Resonance Raman spectra were obtained for complexes of protocatechuate-3,4-dioxygenase with substrate and hydroxybenzoate inhibitors. The data establish metal coordination by these bound species and demonstrate further that tyrosine ligation, present in the resting enzyme, is not altered in the complexes. For the inhibitors, 3-chloro-4-hydroxybenzoate and 3-fluoro-4-hydroxybenzoate, the data are interpreted as indicating iron ligation by the phenolate functionality. For the substrate, 3,4-dihydroxyphenylproprionate, chelation via the
o-dihydroxy grouping is proposed. In all three complexes tyrosine ligands present in the resting enzyme are not displaced. The inhibitor scattering intensity was utilized as an internal standard to estimate that two tyrosines are coordinated to the iron at the active site. |
| doi_str_mv | 10.1016/0006-291X(78)91239-1 |
| format | Article |
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o-dihydroxy grouping is proposed. In all three complexes tyrosine ligands present in the resting enzyme are not displaced. The inhibitor scattering intensity was utilized as an internal standard to estimate that two tyrosines are coordinated to the iron at the active site.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(78)91239-1</identifier><identifier>PMID: 736941</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Anaerobiosis ; Hydroxybenzoates - pharmacology ; Ligands ; Oxygenases - metabolism ; Protein Binding ; Protocatechuate-3,4-Dioxygenase - metabolism ; Spectrum Analysis, Raman</subject><ispartof>Biochemical and biophysical research communications, 1978-11, Vol.85 (2), p.844-850</ispartof><rights>1978</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c356t-f1f3faaf2325df9dc319d38ee39653b7d211bfa30b4cd716d83fdc178b7135393</citedby><cites>FETCH-LOGICAL-c356t-f1f3faaf2325df9dc319d38ee39653b7d211bfa30b4cd716d83fdc178b7135393</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X78912391$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/736941$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Felton, R.H.</creatorcontrib><creatorcontrib>Cheung, L.D.</creatorcontrib><creatorcontrib>Phillips, Robert S.</creatorcontrib><creatorcontrib>May, Sheldon W.</creatorcontrib><title>A resonance Raman study of substrate and inhibitor binding to protocatechuate-3,4-dioxygenase</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Resonance Raman spectra were obtained for complexes of protocatechuate-3,4-dioxygenase with substrate and hydroxybenzoate inhibitors. The data establish metal coordination by these bound species and demonstrate further that tyrosine ligation, present in the resting enzyme, is not altered in the complexes. For the inhibitors, 3-chloro-4-hydroxybenzoate and 3-fluoro-4-hydroxybenzoate, the data are interpreted as indicating iron ligation by the phenolate functionality. For the substrate, 3,4-dihydroxyphenylproprionate, chelation via the
o-dihydroxy grouping is proposed. In all three complexes tyrosine ligands present in the resting enzyme are not displaced. The inhibitor scattering intensity was utilized as an internal standard to estimate that two tyrosines are coordinated to the iron at the active site.</description><subject>Anaerobiosis</subject><subject>Hydroxybenzoates - pharmacology</subject><subject>Ligands</subject><subject>Oxygenases - metabolism</subject><subject>Protein Binding</subject><subject>Protocatechuate-3,4-Dioxygenase - metabolism</subject><subject>Spectrum Analysis, Raman</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1978</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtLxDAQx4P4Wle_gYecRMFqpum2zUUQ8QULgih4kZAmE43sJpqk4n57u6549DJz-D-Y-RGyD-wEGNSnjLG6KAU8HTbtkYCSiwLWyAiYYEUJrFonoz_LNtlJ6Y0xgKoWW2Sz4bWoYESez2nEFLzyGum9mitPU-7NggZLU9-lHFVGqryhzr-6zuUQaee8cf6F5kDfY8hBDxb92g-z4MdVYVz4WrygVwl3yYZVs4R7v3tMHq8uHy5uiund9e3F-bTQfFLnwoLlVilb8nJirDCagzC8ReSinvCuMSVAZxVnXaVNA7VpuTUamrZrgE-44GNysOod7vnoMWU5d0njbKY8hj7JpuKsFT_GamXUMaQU0cr36OYqLiQwuYQql8TkkphsWvkDVcIQ2__t77s5mr_QiuIgn61kHH78dBhl0g4HosZF1Fma4P7v_wbq1IdH</recordid><startdate>19781129</startdate><enddate>19781129</enddate><creator>Felton, R.H.</creator><creator>Cheung, L.D.</creator><creator>Phillips, Robert S.</creator><creator>May, Sheldon W.</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>19781129</creationdate><title>A resonance Raman study of substrate and inhibitor binding to protocatechuate-3,4-dioxygenase</title><author>Felton, R.H. ; Cheung, L.D. ; Phillips, Robert S. ; May, Sheldon W.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c356t-f1f3faaf2325df9dc319d38ee39653b7d211bfa30b4cd716d83fdc178b7135393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1978</creationdate><topic>Anaerobiosis</topic><topic>Hydroxybenzoates - pharmacology</topic><topic>Ligands</topic><topic>Oxygenases - metabolism</topic><topic>Protein Binding</topic><topic>Protocatechuate-3,4-Dioxygenase - metabolism</topic><topic>Spectrum Analysis, Raman</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Felton, R.H.</creatorcontrib><creatorcontrib>Cheung, L.D.</creatorcontrib><creatorcontrib>Phillips, Robert S.</creatorcontrib><creatorcontrib>May, Sheldon W.</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>Felton, R.H.</au><au>Cheung, L.D.</au><au>Phillips, Robert S.</au><au>May, Sheldon W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A resonance Raman study of substrate and inhibitor binding to protocatechuate-3,4-dioxygenase</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1978-11-29</date><risdate>1978</risdate><volume>85</volume><issue>2</issue><spage>844</spage><epage>850</epage><pages>844-850</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Resonance Raman spectra were obtained for complexes of protocatechuate-3,4-dioxygenase with substrate and hydroxybenzoate inhibitors. The data establish metal coordination by these bound species and demonstrate further that tyrosine ligation, present in the resting enzyme, is not altered in the complexes. For the inhibitors, 3-chloro-4-hydroxybenzoate and 3-fluoro-4-hydroxybenzoate, the data are interpreted as indicating iron ligation by the phenolate functionality. For the substrate, 3,4-dihydroxyphenylproprionate, chelation via the
o-dihydroxy grouping is proposed. In all three complexes tyrosine ligands present in the resting enzyme are not displaced. The inhibitor scattering intensity was utilized as an internal standard to estimate that two tyrosines are coordinated to the iron at the active site.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>736941</pmid><doi>10.1016/0006-291X(78)91239-1</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1978-11, Vol.85 (2), p.844-850 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Anaerobiosis Hydroxybenzoates - pharmacology Ligands Oxygenases - metabolism Protein Binding Protocatechuate-3,4-Dioxygenase - metabolism Spectrum Analysis, Raman |
| title | A resonance Raman study of substrate and inhibitor binding to protocatechuate-3,4-dioxygenase |
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