Horseradish‐Peroxidase‐Catalyzed Tyrosine Click Reaction
The efficiency of protein chemical modification on tyrosine residues with N‐methylluminol derivatives was drastically improved by using horseradish peroxidase (HRP). In the previous method, based on the use of hemin and H2O2, oxidative side reactions such as cysteine oxidation were problematic for f...
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| Veröffentlicht in: | Chembiochem : a European journal of chemical biology 2017-03, Vol.18 (5), p.475-478 |
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| creator | Sato, Shinichi Nakamura, Kosuke Nakamura, Hiroyuki |
| description | The efficiency of protein chemical modification on tyrosine residues with N‐methylluminol derivatives was drastically improved by using horseradish peroxidase (HRP). In the previous method, based on the use of hemin and H2O2, oxidative side reactions such as cysteine oxidation were problematic for functionalization of proteins selectively on tyrosine residues. Oxidative activation of N‐methylluminol derivatives with a minimum amount of H2O2 prevented the occurrence of oxidative side reactions under HRP‐catalyzed conditions. As probes for HRP‐catalyzed protein modification, N‐methylluminol derivatives showed much higher efficiency than tyramide without inducing oligomerization of probe molecules. Tyrosine modification also proceeded in the presence of β‐nicotinamide adenine dinucleotide (NADH, H2O2‐free conditions).
Specific labeling of tyrosine in proteins: Horseradish‐peroxidase‐catalyzed (HRP‐catalyzed) tyrosine modification was achieved with the aid of N‐methylluminol derivatives. Tyrosine residues in peptides and proteins were modified efficiently in the presence of H2O2 or β‐nicotinamide adenine dinucleotide. |
| doi_str_mv | 10.1002/cbic.201600649 |
| format | Article |
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Specific labeling of tyrosine in proteins: Horseradish‐peroxidase‐catalyzed (HRP‐catalyzed) tyrosine modification was achieved with the aid of N‐methylluminol derivatives. Tyrosine residues in peptides and proteins were modified efficiently in the presence of H2O2 or β‐nicotinamide adenine dinucleotide.</description><identifier>ISSN: 1439-4227</identifier><identifier>EISSN: 1439-7633</identifier><identifier>DOI: 10.1002/cbic.201600649</identifier><identifier>PMID: 28009088</identifier><language>eng</language><publisher>Germany: Wiley Subscription Services, Inc</publisher><subject>Binding Sites ; Catalysis ; Click Chemistry ; Heme - chemistry ; heme proteins ; horseradish peroxidase ; Horseradish Peroxidase - chemistry ; Horseradish Peroxidase - metabolism ; Hydrogen Peroxide - chemistry ; Models, Molecular ; Molecular Structure ; protein labeling ; protein modifications ; Tyrosine - chemistry ; tyrosine modification</subject><ispartof>Chembiochem : a European journal of chemical biology, 2017-03, Vol.18 (5), p.475-478</ispartof><rights>2017 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.</rights><rights>2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5539-f7006dec9acc3f1be47fabba08617b750cf880ac554843e9906fa5449232d8213</citedby><cites>FETCH-LOGICAL-c5539-f7006dec9acc3f1be47fabba08617b750cf880ac554843e9906fa5449232d8213</cites><orcidid>0000-0002-4511-2984 ; 0000-0002-8563-1658</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fcbic.201600649$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fcbic.201600649$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28009088$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sato, Shinichi</creatorcontrib><creatorcontrib>Nakamura, Kosuke</creatorcontrib><creatorcontrib>Nakamura, Hiroyuki</creatorcontrib><title>Horseradish‐Peroxidase‐Catalyzed Tyrosine Click Reaction</title><title>Chembiochem : a European journal of chemical biology</title><addtitle>Chembiochem</addtitle><description>The efficiency of protein chemical modification on tyrosine residues with N‐methylluminol derivatives was drastically improved by using horseradish peroxidase (HRP). In the previous method, based on the use of hemin and H2O2, oxidative side reactions such as cysteine oxidation were problematic for functionalization of proteins selectively on tyrosine residues. Oxidative activation of N‐methylluminol derivatives with a minimum amount of H2O2 prevented the occurrence of oxidative side reactions under HRP‐catalyzed conditions. As probes for HRP‐catalyzed protein modification, N‐methylluminol derivatives showed much higher efficiency than tyramide without inducing oligomerization of probe molecules. Tyrosine modification also proceeded in the presence of β‐nicotinamide adenine dinucleotide (NADH, H2O2‐free conditions).
Specific labeling of tyrosine in proteins: Horseradish‐peroxidase‐catalyzed (HRP‐catalyzed) tyrosine modification was achieved with the aid of N‐methylluminol derivatives. Tyrosine residues in peptides and proteins were modified efficiently in the presence of H2O2 or β‐nicotinamide adenine dinucleotide.</description><subject>Binding Sites</subject><subject>Catalysis</subject><subject>Click Chemistry</subject><subject>Heme - chemistry</subject><subject>heme proteins</subject><subject>horseradish peroxidase</subject><subject>Horseradish Peroxidase - chemistry</subject><subject>Horseradish Peroxidase - metabolism</subject><subject>Hydrogen Peroxide - chemistry</subject><subject>Models, Molecular</subject><subject>Molecular Structure</subject><subject>protein labeling</subject><subject>protein modifications</subject><subject>Tyrosine - chemistry</subject><subject>tyrosine modification</subject><issn>1439-4227</issn><issn>1439-7633</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc9KAzEQh4MotlavHqXgxUvr5M9uEvCii9qCoEg9L9lsFlO3uzXpouvJR_AZfRJTWit40dPMwJePyfwQOsQwxADkVGdWDwngGCBmcgt1MaNywGNKt9c9I4R30J73UwCQMcW7qENEaEGILjob1c4bp3LrHz_fP-6Mq19trrwJQ6IWqmzfTN6ftK72tjL9pLT6qX9vlF7YutpHO4UqvTlY1x56uLqcJKPBze31ODm_GegoChsUPCyXGy2V1rTAmWG8UFmmQMSYZzwCXQgBKsBMMGqkhLhQEWOSUJILgmkPnay8c1c_N8Yv0pn12pSlqkzd-BQLzgWOgMA_0IhwQSSJAnr8C53WjavCR5ZCRjEBJgI1XFE6nMA7U6RzZ2fKtSmGdBlBuowg3UQQHhyttU02M_kG_755AOQKeLGlaf_QpcnFOPmRfwGPXZKU</recordid><startdate>20170302</startdate><enddate>20170302</enddate><creator>Sato, Shinichi</creator><creator>Nakamura, Kosuke</creator><creator>Nakamura, Hiroyuki</creator><general>Wiley Subscription Services, 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>7QL</scope><scope>7QO</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-4511-2984</orcidid><orcidid>https://orcid.org/0000-0002-8563-1658</orcidid></search><sort><creationdate>20170302</creationdate><title>Horseradish‐Peroxidase‐Catalyzed Tyrosine Click Reaction</title><author>Sato, Shinichi ; Nakamura, Kosuke ; Nakamura, Hiroyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5539-f7006dec9acc3f1be47fabba08617b750cf880ac554843e9906fa5449232d8213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Binding Sites</topic><topic>Catalysis</topic><topic>Click Chemistry</topic><topic>Heme - chemistry</topic><topic>heme proteins</topic><topic>horseradish peroxidase</topic><topic>Horseradish Peroxidase - chemistry</topic><topic>Horseradish Peroxidase - metabolism</topic><topic>Hydrogen Peroxide - chemistry</topic><topic>Models, Molecular</topic><topic>Molecular Structure</topic><topic>protein labeling</topic><topic>protein modifications</topic><topic>Tyrosine - chemistry</topic><topic>tyrosine modification</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sato, Shinichi</creatorcontrib><creatorcontrib>Nakamura, Kosuke</creatorcontrib><creatorcontrib>Nakamura, Hiroyuki</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Chembiochem : a European journal of chemical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sato, Shinichi</au><au>Nakamura, Kosuke</au><au>Nakamura, Hiroyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Horseradish‐Peroxidase‐Catalyzed Tyrosine Click Reaction</atitle><jtitle>Chembiochem : a European journal of chemical biology</jtitle><addtitle>Chembiochem</addtitle><date>2017-03-02</date><risdate>2017</risdate><volume>18</volume><issue>5</issue><spage>475</spage><epage>478</epage><pages>475-478</pages><issn>1439-4227</issn><eissn>1439-7633</eissn><abstract>The efficiency of protein chemical modification on tyrosine residues with N‐methylluminol derivatives was drastically improved by using horseradish peroxidase (HRP). In the previous method, based on the use of hemin and H2O2, oxidative side reactions such as cysteine oxidation were problematic for functionalization of proteins selectively on tyrosine residues. Oxidative activation of N‐methylluminol derivatives with a minimum amount of H2O2 prevented the occurrence of oxidative side reactions under HRP‐catalyzed conditions. As probes for HRP‐catalyzed protein modification, N‐methylluminol derivatives showed much higher efficiency than tyramide without inducing oligomerization of probe molecules. Tyrosine modification also proceeded in the presence of β‐nicotinamide adenine dinucleotide (NADH, H2O2‐free conditions).
Specific labeling of tyrosine in proteins: Horseradish‐peroxidase‐catalyzed (HRP‐catalyzed) tyrosine modification was achieved with the aid of N‐methylluminol derivatives. Tyrosine residues in peptides and proteins were modified efficiently in the presence of H2O2 or β‐nicotinamide adenine dinucleotide.</abstract><cop>Germany</cop><pub>Wiley Subscription Services, Inc</pub><pmid>28009088</pmid><doi>10.1002/cbic.201600649</doi><tpages>4</tpages><orcidid>https://orcid.org/0000-0002-4511-2984</orcidid><orcidid>https://orcid.org/0000-0002-8563-1658</orcidid></addata></record> |
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| ispartof | Chembiochem : a European journal of chemical biology, 2017-03, Vol.18 (5), p.475-478 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Binding Sites Catalysis Click Chemistry Heme - chemistry heme proteins horseradish peroxidase Horseradish Peroxidase - chemistry Horseradish Peroxidase - metabolism Hydrogen Peroxide - chemistry Models, Molecular Molecular Structure protein labeling protein modifications Tyrosine - chemistry tyrosine modification |
| title | Horseradish‐Peroxidase‐Catalyzed Tyrosine Click Reaction |
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