Cytochrome c-poly(acrylic acid) conjugates with improved peroxidase turnover number
Cytochrome c-poly(acrylic acid) (cyt c-PAA) conjugates with 34-fold enchancement in peroxidase turnover number (kcat) are reported. Cyt c-PAA conjugates were prepared by carbodiimide coupling. PAA with molecular weight (Mw) ranging from 1.8k to 250k g mol-1 were employed, and the effect of PAA Mw on...
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| Veröffentlicht in: | Organic & biomolecular chemistry 2019-04, Vol.17 (16), p.4043-4048 |
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| creator | Benson, K R Gorecki, J Nikiforov, A Tsui, W Kasi, R M Kumar, C V |
| description | Cytochrome c-poly(acrylic acid) (cyt c-PAA) conjugates with 34-fold enchancement in peroxidase turnover number (kcat) are reported. Cyt c-PAA conjugates were prepared by carbodiimide coupling. PAA with molecular weight (Mw) ranging from 1.8k to 250k g mol-1 were employed, and the effect of PAA Mw on peroxiodase kinetics was assessed. The kcat value increased with increased Mw of PAA, ranging from 0.077(±0.002) s-1 in the absence of PAA to 2.66(±0.08) s-1 for the conjugate of cyt c with 250k PAA. Enzymatic activity studies over pH 6-8 indicated improved activity for cyt c-PAA conjugates at neutral or slightly alkaline pH. Examination of the cyt c heme spectroscopy in the presence of H2O2 revealed that formation of compound III, a reactive intermediate that leads to enzyme inactivation, was supressed in cyt c-PAA conjugates. Thus, we suggest the kcat enhancement can be attributed to acidification of the pH microenvironment and inhibition of the formation of a reactive intermediate that deactivates cyt c during the catalytic cycle. |
| doi_str_mv | 10.1039/c9ob00541b |
| format | Article |
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Cyt c-PAA conjugates were prepared by carbodiimide coupling. PAA with molecular weight (Mw) ranging from 1.8k to 250k g mol-1 were employed, and the effect of PAA Mw on peroxiodase kinetics was assessed. The kcat value increased with increased Mw of PAA, ranging from 0.077(±0.002) s-1 in the absence of PAA to 2.66(±0.08) s-1 for the conjugate of cyt c with 250k PAA. Enzymatic activity studies over pH 6-8 indicated improved activity for cyt c-PAA conjugates at neutral or slightly alkaline pH. Examination of the cyt c heme spectroscopy in the presence of H2O2 revealed that formation of compound III, a reactive intermediate that leads to enzyme inactivation, was supressed in cyt c-PAA conjugates. Thus, we suggest the kcat enhancement can be attributed to acidification of the pH microenvironment and inhibition of the formation of a reactive intermediate that deactivates cyt c during the catalytic cycle.</description><identifier>ISSN: 1477-0520</identifier><identifier>EISSN: 1477-0539</identifier><identifier>DOI: 10.1039/c9ob00541b</identifier><identifier>PMID: 30950479</identifier><language>eng</language><publisher>England: Royal Society of Chemistry</publisher><subject>Acidification ; Acrylic acid ; Acrylic Resins - chemistry ; Acrylic Resins - metabolism ; Acrylics ; Carbodiimide ; Catalysis ; Conjugates ; Coupling (molecular) ; Cytochrome ; Cytochrome c ; Cytochromes ; Cytochromes c - chemistry ; Cytochromes c - metabolism ; Deactivation ; Enzymatic activity ; Ethyldimethylaminopropyl Carbodiimide - chemistry ; Heme ; Hydrogen peroxide ; Hydrogen Peroxide - chemistry ; Hydrogen-Ion Concentration ; Inactivation ; Kinetics ; Molecular Structure ; Molecular weight ; Peroxidase ; Peroxidases - metabolism ; pH effects ; Reaction kinetics ; Spectroscopy</subject><ispartof>Organic & biomolecular chemistry, 2019-04, Vol.17 (16), p.4043-4048</ispartof><rights>Copyright Royal Society of Chemistry 2019</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c315t-cf1b73b74a57950d4e7cfe4e42d97d7dfcfebf7d687cf8cb1ea00ca3694915053</citedby><cites>FETCH-LOGICAL-c315t-cf1b73b74a57950d4e7cfe4e42d97d7dfcfebf7d687cf8cb1ea00ca3694915053</cites><orcidid>0000-0001-9986-6696 ; 0000-0003-3872-1463</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30950479$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Benson, K R</creatorcontrib><creatorcontrib>Gorecki, J</creatorcontrib><creatorcontrib>Nikiforov, A</creatorcontrib><creatorcontrib>Tsui, W</creatorcontrib><creatorcontrib>Kasi, R M</creatorcontrib><creatorcontrib>Kumar, C V</creatorcontrib><title>Cytochrome c-poly(acrylic acid) conjugates with improved peroxidase turnover number</title><title>Organic & biomolecular chemistry</title><addtitle>Org Biomol Chem</addtitle><description>Cytochrome c-poly(acrylic acid) (cyt c-PAA) conjugates with 34-fold enchancement in peroxidase turnover number (kcat) are reported. Cyt c-PAA conjugates were prepared by carbodiimide coupling. PAA with molecular weight (Mw) ranging from 1.8k to 250k g mol-1 were employed, and the effect of PAA Mw on peroxiodase kinetics was assessed. The kcat value increased with increased Mw of PAA, ranging from 0.077(±0.002) s-1 in the absence of PAA to 2.66(±0.08) s-1 for the conjugate of cyt c with 250k PAA. Enzymatic activity studies over pH 6-8 indicated improved activity for cyt c-PAA conjugates at neutral or slightly alkaline pH. Examination of the cyt c heme spectroscopy in the presence of H2O2 revealed that formation of compound III, a reactive intermediate that leads to enzyme inactivation, was supressed in cyt c-PAA conjugates. Thus, we suggest the kcat enhancement can be attributed to acidification of the pH microenvironment and inhibition of the formation of a reactive intermediate that deactivates cyt c during the catalytic cycle.</description><subject>Acidification</subject><subject>Acrylic acid</subject><subject>Acrylic Resins - chemistry</subject><subject>Acrylic Resins - metabolism</subject><subject>Acrylics</subject><subject>Carbodiimide</subject><subject>Catalysis</subject><subject>Conjugates</subject><subject>Coupling (molecular)</subject><subject>Cytochrome</subject><subject>Cytochrome c</subject><subject>Cytochromes</subject><subject>Cytochromes c - chemistry</subject><subject>Cytochromes c - metabolism</subject><subject>Deactivation</subject><subject>Enzymatic activity</subject><subject>Ethyldimethylaminopropyl Carbodiimide - chemistry</subject><subject>Heme</subject><subject>Hydrogen peroxide</subject><subject>Hydrogen Peroxide - chemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>Inactivation</subject><subject>Kinetics</subject><subject>Molecular Structure</subject><subject>Molecular weight</subject><subject>Peroxidase</subject><subject>Peroxidases - metabolism</subject><subject>pH effects</subject><subject>Reaction kinetics</subject><subject>Spectroscopy</subject><issn>1477-0520</issn><issn>1477-0539</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkMtOwzAQRS0EoqWw4QOQJTYFKWAnTl0vacRLqtQFsI78mNBUSVzsBMjf49LSBat56MzVnYvQOSU3lCTiVgurCEkZVQdoSBnnEUkTcbjvYzJAJ96vCKGCT9gxGiREpIRxMUQvWd9avXS2Bqyjta36sdSur0qNpS7NFda2WXXvsgWPv8p2ict67ewnGLwGZ79LIz3gtnNN2DncdLUCd4qOCll5ONvVEXp7uH_NnqL54vE5u5tHOqFpG-mCKp4ozmTKgx3DgOsCGLDYCG64KcKkCm4m07CfakVBEqJlMhFM0DS8OELjrW5w9NGBb_O69BqqSjZgO5_HMWHhOGVxQC__oSsbTAd3gaJkmjIWbwSvt5R21nsHRb52ZS1dn1OSb6LOM7GY_UY9C_DFTrJTNZg9-pdt8gNDyHoM</recordid><startdate>20190417</startdate><enddate>20190417</enddate><creator>Benson, K R</creator><creator>Gorecki, J</creator><creator>Nikiforov, A</creator><creator>Tsui, W</creator><creator>Kasi, R M</creator><creator>Kumar, C V</creator><general>Royal Society of Chemistry</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>7QO</scope><scope>7T7</scope><scope>7TM</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0001-9986-6696</orcidid><orcidid>https://orcid.org/0000-0003-3872-1463</orcidid></search><sort><creationdate>20190417</creationdate><title>Cytochrome c-poly(acrylic acid) conjugates with improved peroxidase turnover number</title><author>Benson, K R ; Gorecki, J ; Nikiforov, A ; Tsui, W ; Kasi, R M ; Kumar, C V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c315t-cf1b73b74a57950d4e7cfe4e42d97d7dfcfebf7d687cf8cb1ea00ca3694915053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Acidification</topic><topic>Acrylic acid</topic><topic>Acrylic Resins - chemistry</topic><topic>Acrylic Resins - metabolism</topic><topic>Acrylics</topic><topic>Carbodiimide</topic><topic>Catalysis</topic><topic>Conjugates</topic><topic>Coupling (molecular)</topic><topic>Cytochrome</topic><topic>Cytochrome c</topic><topic>Cytochromes</topic><topic>Cytochromes c - chemistry</topic><topic>Cytochromes c - metabolism</topic><topic>Deactivation</topic><topic>Enzymatic activity</topic><topic>Ethyldimethylaminopropyl Carbodiimide - chemistry</topic><topic>Heme</topic><topic>Hydrogen peroxide</topic><topic>Hydrogen Peroxide - chemistry</topic><topic>Hydrogen-Ion Concentration</topic><topic>Inactivation</topic><topic>Kinetics</topic><topic>Molecular Structure</topic><topic>Molecular weight</topic><topic>Peroxidase</topic><topic>Peroxidases - metabolism</topic><topic>pH effects</topic><topic>Reaction kinetics</topic><topic>Spectroscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Benson, K R</creatorcontrib><creatorcontrib>Gorecki, J</creatorcontrib><creatorcontrib>Nikiforov, A</creatorcontrib><creatorcontrib>Tsui, W</creatorcontrib><creatorcontrib>Kasi, R M</creatorcontrib><creatorcontrib>Kumar, C V</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Organic & biomolecular chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Benson, K R</au><au>Gorecki, J</au><au>Nikiforov, A</au><au>Tsui, W</au><au>Kasi, R M</au><au>Kumar, C V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cytochrome c-poly(acrylic acid) conjugates with improved peroxidase turnover number</atitle><jtitle>Organic & biomolecular chemistry</jtitle><addtitle>Org Biomol Chem</addtitle><date>2019-04-17</date><risdate>2019</risdate><volume>17</volume><issue>16</issue><spage>4043</spage><epage>4048</epage><pages>4043-4048</pages><issn>1477-0520</issn><eissn>1477-0539</eissn><abstract>Cytochrome c-poly(acrylic acid) (cyt c-PAA) conjugates with 34-fold enchancement in peroxidase turnover number (kcat) are reported. Cyt c-PAA conjugates were prepared by carbodiimide coupling. PAA with molecular weight (Mw) ranging from 1.8k to 250k g mol-1 were employed, and the effect of PAA Mw on peroxiodase kinetics was assessed. The kcat value increased with increased Mw of PAA, ranging from 0.077(±0.002) s-1 in the absence of PAA to 2.66(±0.08) s-1 for the conjugate of cyt c with 250k PAA. Enzymatic activity studies over pH 6-8 indicated improved activity for cyt c-PAA conjugates at neutral or slightly alkaline pH. Examination of the cyt c heme spectroscopy in the presence of H2O2 revealed that formation of compound III, a reactive intermediate that leads to enzyme inactivation, was supressed in cyt c-PAA conjugates. Thus, we suggest the kcat enhancement can be attributed to acidification of the pH microenvironment and inhibition of the formation of a reactive intermediate that deactivates cyt c during the catalytic cycle.</abstract><cop>England</cop><pub>Royal Society of Chemistry</pub><pmid>30950479</pmid><doi>10.1039/c9ob00541b</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0001-9986-6696</orcidid><orcidid>https://orcid.org/0000-0003-3872-1463</orcidid></addata></record> |
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| subjects | Acidification Acrylic acid Acrylic Resins - chemistry Acrylic Resins - metabolism Acrylics Carbodiimide Catalysis Conjugates Coupling (molecular) Cytochrome Cytochrome c Cytochromes Cytochromes c - chemistry Cytochromes c - metabolism Deactivation Enzymatic activity Ethyldimethylaminopropyl Carbodiimide - chemistry Heme Hydrogen peroxide Hydrogen Peroxide - chemistry Hydrogen-Ion Concentration Inactivation Kinetics Molecular Structure Molecular weight Peroxidase Peroxidases - metabolism pH effects Reaction kinetics Spectroscopy |
| title | Cytochrome c-poly(acrylic acid) conjugates with improved peroxidase turnover number |
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