Kinetics of Spanish broom peroxidase obeys a Ping-Pong Bi–Bi mechanism with competitive inhibition by substrates
In plants, adverse conditions often induce an increase in reactive oxygen species (ROS) such as hydrogen peroxide (H2O2). H2O2 is reduced to water, and thus becomes detoxified by enzymes such as Cytisus multiflorus peroxidase (CMP). Here, the steady-state kinetics of the H2O2-supported oxidation of...
Gespeichert in:
| Veröffentlicht in: | International journal of biological macromolecules 2015-11, Vol.81, p.1005-1011 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1011 |
|---|---|
| container_issue | |
| container_start_page | 1005 |
| container_title | International journal of biological macromolecules |
| container_volume | 81 |
| creator | Pérez Galende, Patricia Hidalgo Cuadrado, Nazaret Kostetsky, Eduard Ya Roig, Manuel G. Villar, Enrique Shnyrov, Valery L. Kennedy, John F. |
| description | In plants, adverse conditions often induce an increase in reactive oxygen species (ROS) such as hydrogen peroxide (H2O2). H2O2 is reduced to water, and thus becomes detoxified by enzymes such as Cytisus multiflorus peroxidase (CMP). Here, the steady-state kinetics of the H2O2-supported oxidation of different organic substrates by CMP was investigated. Analysis of the initial rates vs. H2O2 and reducing substrate concentrations proved to be consistent with a substrate-inhibited Ping-Pong Bi–Bi reaction mechanism. The phenomenological approach expresses the peroxidase Ping-Pong mechanism in the form of the Michaelis–Menten equation and affords an interpretation of the effects in terms of the kinetic parameters KmH2O2, KmAH2, kcat, KSIH2O, KSIAH2 and of the microscopic rate constants, k1 and k3, of the shared three-step catalytic cycle of peroxidases. |
| doi_str_mv | 10.1016/j.ijbiomac.2015.09.042 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1751492032</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0141813015006571</els_id><sourcerecordid>1751492032</sourcerecordid><originalsourceid>FETCH-LOGICAL-c368t-4316d8ca2fe04f8bb00f193c22888ca95b03a31ff1e0feb954cdc3240b6730ba3</originalsourceid><addsrcrecordid>eNqFkM1u1DAQxy1U1C6lr1D52EvC2E6yyY22ooCoRCXgbNnOuDurTZza2dK98Q68IU-CV9ty5TSj0f9D82PsXEApQDTv1iWtLYXBuFKCqEvoSqjkK7YQ7bIrAEAdsQWIShStUHDC3qS0ztemFu0xO5FNJRqpugWLX2jEmVziwfNvkxkprbiNIQx8whieqDcJebC4S9zwOxrvi7sw3vMr-vPr9xXxAd1qbxr4T5pX3IVhynEzPSKncUU2r2HkdsfT1qY5mhnTW_bam03Cs-d5yn7cfPh-_am4_frx8_XlbeFU085FpUTTt85Ij1D51loALzrlpGzbfO5qC8oo4b1A8Gi7unK9U7IC2ywVWKNO2cUhd4rhYYtp1gMlh5uNGTFskxbLWlSdBCWztDlIXQwpRfR6ijSYuNMC9J63XusX3nrPW0OnM-9sPH_u2NoB-3-2F8BZ8P4gwPzpI2HUyRGODnuK6GbdB_pfx19MWZdd</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1751492032</pqid></control><display><type>article</type><title>Kinetics of Spanish broom peroxidase obeys a Ping-Pong Bi–Bi mechanism with competitive inhibition by substrates</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><creator>Pérez Galende, Patricia ; Hidalgo Cuadrado, Nazaret ; Kostetsky, Eduard Ya ; Roig, Manuel G. ; Villar, Enrique ; Shnyrov, Valery L. ; Kennedy, John F.</creator><creatorcontrib>Pérez Galende, Patricia ; Hidalgo Cuadrado, Nazaret ; Kostetsky, Eduard Ya ; Roig, Manuel G. ; Villar, Enrique ; Shnyrov, Valery L. ; Kennedy, John F.</creatorcontrib><description>In plants, adverse conditions often induce an increase in reactive oxygen species (ROS) such as hydrogen peroxide (H2O2). H2O2 is reduced to water, and thus becomes detoxified by enzymes such as Cytisus multiflorus peroxidase (CMP). Here, the steady-state kinetics of the H2O2-supported oxidation of different organic substrates by CMP was investigated. Analysis of the initial rates vs. H2O2 and reducing substrate concentrations proved to be consistent with a substrate-inhibited Ping-Pong Bi–Bi reaction mechanism. The phenomenological approach expresses the peroxidase Ping-Pong mechanism in the form of the Michaelis–Menten equation and affords an interpretation of the effects in terms of the kinetic parameters KmH2O2, KmAH2, kcat, KSIH2O, KSIAH2 and of the microscopic rate constants, k1 and k3, of the shared three-step catalytic cycle of peroxidases.</description><identifier>ISSN: 0141-8130</identifier><identifier>EISSN: 1879-0003</identifier><identifier>DOI: 10.1016/j.ijbiomac.2015.09.042</identifier><identifier>PMID: 26416239</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Biocatalysis ; Cytisus - enzymology ; Guaiacol - metabolism ; Heme peroxidase ; Hydrogen Peroxide - metabolism ; Kinetics ; Microscopic constants ; Models, Molecular ; Oxidation-Reduction ; Peroxidase - antagonists & inhibitors ; Peroxidase - metabolism ; Ping-Pong Bi–Bi Mechanism ; Substrate Specificity</subject><ispartof>International journal of biological macromolecules, 2015-11, Vol.81, p.1005-1011</ispartof><rights>2015 Elsevier B.V.</rights><rights>Copyright © 2015 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-4316d8ca2fe04f8bb00f193c22888ca95b03a31ff1e0feb954cdc3240b6730ba3</citedby><cites>FETCH-LOGICAL-c368t-4316d8ca2fe04f8bb00f193c22888ca95b03a31ff1e0feb954cdc3240b6730ba3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ijbiomac.2015.09.042$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26416239$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pérez Galende, Patricia</creatorcontrib><creatorcontrib>Hidalgo Cuadrado, Nazaret</creatorcontrib><creatorcontrib>Kostetsky, Eduard Ya</creatorcontrib><creatorcontrib>Roig, Manuel G.</creatorcontrib><creatorcontrib>Villar, Enrique</creatorcontrib><creatorcontrib>Shnyrov, Valery L.</creatorcontrib><creatorcontrib>Kennedy, John F.</creatorcontrib><title>Kinetics of Spanish broom peroxidase obeys a Ping-Pong Bi–Bi mechanism with competitive inhibition by substrates</title><title>International journal of biological macromolecules</title><addtitle>Int J Biol Macromol</addtitle><description>In plants, adverse conditions often induce an increase in reactive oxygen species (ROS) such as hydrogen peroxide (H2O2). H2O2 is reduced to water, and thus becomes detoxified by enzymes such as Cytisus multiflorus peroxidase (CMP). Here, the steady-state kinetics of the H2O2-supported oxidation of different organic substrates by CMP was investigated. Analysis of the initial rates vs. H2O2 and reducing substrate concentrations proved to be consistent with a substrate-inhibited Ping-Pong Bi–Bi reaction mechanism. The phenomenological approach expresses the peroxidase Ping-Pong mechanism in the form of the Michaelis–Menten equation and affords an interpretation of the effects in terms of the kinetic parameters KmH2O2, KmAH2, kcat, KSIH2O, KSIAH2 and of the microscopic rate constants, k1 and k3, of the shared three-step catalytic cycle of peroxidases.</description><subject>Biocatalysis</subject><subject>Cytisus - enzymology</subject><subject>Guaiacol - metabolism</subject><subject>Heme peroxidase</subject><subject>Hydrogen Peroxide - metabolism</subject><subject>Kinetics</subject><subject>Microscopic constants</subject><subject>Models, Molecular</subject><subject>Oxidation-Reduction</subject><subject>Peroxidase - antagonists & inhibitors</subject><subject>Peroxidase - metabolism</subject><subject>Ping-Pong Bi–Bi Mechanism</subject><subject>Substrate Specificity</subject><issn>0141-8130</issn><issn>1879-0003</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1u1DAQxy1U1C6lr1D52EvC2E6yyY22ooCoRCXgbNnOuDurTZza2dK98Q68IU-CV9ty5TSj0f9D82PsXEApQDTv1iWtLYXBuFKCqEvoSqjkK7YQ7bIrAEAdsQWIShStUHDC3qS0ztemFu0xO5FNJRqpugWLX2jEmVziwfNvkxkprbiNIQx8whieqDcJebC4S9zwOxrvi7sw3vMr-vPr9xXxAd1qbxr4T5pX3IVhynEzPSKncUU2r2HkdsfT1qY5mhnTW_bam03Cs-d5yn7cfPh-_am4_frx8_XlbeFU085FpUTTt85Ij1D51loALzrlpGzbfO5qC8oo4b1A8Gi7unK9U7IC2ywVWKNO2cUhd4rhYYtp1gMlh5uNGTFskxbLWlSdBCWztDlIXQwpRfR6ijSYuNMC9J63XusX3nrPW0OnM-9sPH_u2NoB-3-2F8BZ8P4gwPzpI2HUyRGODnuK6GbdB_pfx19MWZdd</recordid><startdate>201511</startdate><enddate>201511</enddate><creator>Pérez Galende, Patricia</creator><creator>Hidalgo Cuadrado, Nazaret</creator><creator>Kostetsky, Eduard Ya</creator><creator>Roig, Manuel G.</creator><creator>Villar, Enrique</creator><creator>Shnyrov, Valery L.</creator><creator>Kennedy, John F.</creator><general>Elsevier B.V</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>201511</creationdate><title>Kinetics of Spanish broom peroxidase obeys a Ping-Pong Bi–Bi mechanism with competitive inhibition by substrates</title><author>Pérez Galende, Patricia ; Hidalgo Cuadrado, Nazaret ; Kostetsky, Eduard Ya ; Roig, Manuel G. ; Villar, Enrique ; Shnyrov, Valery L. ; Kennedy, John F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-4316d8ca2fe04f8bb00f193c22888ca95b03a31ff1e0feb954cdc3240b6730ba3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Biocatalysis</topic><topic>Cytisus - enzymology</topic><topic>Guaiacol - metabolism</topic><topic>Heme peroxidase</topic><topic>Hydrogen Peroxide - metabolism</topic><topic>Kinetics</topic><topic>Microscopic constants</topic><topic>Models, Molecular</topic><topic>Oxidation-Reduction</topic><topic>Peroxidase - antagonists & inhibitors</topic><topic>Peroxidase - metabolism</topic><topic>Ping-Pong Bi–Bi Mechanism</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pérez Galende, Patricia</creatorcontrib><creatorcontrib>Hidalgo Cuadrado, Nazaret</creatorcontrib><creatorcontrib>Kostetsky, Eduard Ya</creatorcontrib><creatorcontrib>Roig, Manuel G.</creatorcontrib><creatorcontrib>Villar, Enrique</creatorcontrib><creatorcontrib>Shnyrov, Valery L.</creatorcontrib><creatorcontrib>Kennedy, John F.</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>International journal of biological macromolecules</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pérez Galende, Patricia</au><au>Hidalgo Cuadrado, Nazaret</au><au>Kostetsky, Eduard Ya</au><au>Roig, Manuel G.</au><au>Villar, Enrique</au><au>Shnyrov, Valery L.</au><au>Kennedy, John F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinetics of Spanish broom peroxidase obeys a Ping-Pong Bi–Bi mechanism with competitive inhibition by substrates</atitle><jtitle>International journal of biological macromolecules</jtitle><addtitle>Int J Biol Macromol</addtitle><date>2015-11</date><risdate>2015</risdate><volume>81</volume><spage>1005</spage><epage>1011</epage><pages>1005-1011</pages><issn>0141-8130</issn><eissn>1879-0003</eissn><abstract>In plants, adverse conditions often induce an increase in reactive oxygen species (ROS) such as hydrogen peroxide (H2O2). H2O2 is reduced to water, and thus becomes detoxified by enzymes such as Cytisus multiflorus peroxidase (CMP). Here, the steady-state kinetics of the H2O2-supported oxidation of different organic substrates by CMP was investigated. Analysis of the initial rates vs. H2O2 and reducing substrate concentrations proved to be consistent with a substrate-inhibited Ping-Pong Bi–Bi reaction mechanism. The phenomenological approach expresses the peroxidase Ping-Pong mechanism in the form of the Michaelis–Menten equation and affords an interpretation of the effects in terms of the kinetic parameters KmH2O2, KmAH2, kcat, KSIH2O, KSIAH2 and of the microscopic rate constants, k1 and k3, of the shared three-step catalytic cycle of peroxidases.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>26416239</pmid><doi>10.1016/j.ijbiomac.2015.09.042</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0141-8130 |
| ispartof | International journal of biological macromolecules, 2015-11, Vol.81, p.1005-1011 |
| issn | 0141-8130 1879-0003 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1751492032 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Biocatalysis Cytisus - enzymology Guaiacol - metabolism Heme peroxidase Hydrogen Peroxide - metabolism Kinetics Microscopic constants Models, Molecular Oxidation-Reduction Peroxidase - antagonists & inhibitors Peroxidase - metabolism Ping-Pong Bi–Bi Mechanism Substrate Specificity |
| title | Kinetics of Spanish broom peroxidase obeys a Ping-Pong Bi–Bi mechanism with competitive inhibition by substrates |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-13T22%3A00%3A21IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Kinetics%20of%20Spanish%20broom%20peroxidase%20obeys%20a%20Ping-Pong%20Bi%E2%80%93Bi%20mechanism%20with%20competitive%20inhibition%20by%20substrates&rft.jtitle=International%20journal%20of%20biological%20macromolecules&rft.au=P%C3%A9rez%20Galende,%20Patricia&rft.date=2015-11&rft.volume=81&rft.spage=1005&rft.epage=1011&rft.pages=1005-1011&rft.issn=0141-8130&rft.eissn=1879-0003&rft_id=info:doi/10.1016/j.ijbiomac.2015.09.042&rft_dat=%3Cproquest_cross%3E1751492032%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1751492032&rft_id=info:pmid/26416239&rft_els_id=S0141813015006571&rfr_iscdi=true |