Probing the Function of the Tyr-Cys Cross-Link in Metalloenzymes by the Genetic Incorporation of 3-Methylthiotyrosine
Efficient multiple‐electron redox reactions are performed by galactoase oxidase, cysteine dioxygenase, sulfite reductase, and cytochrome c nitrite reductase. A post‐translationally modified tyrosine–cysteine cross‐link (Tyr‐Cys) in their active sites is essential for their functions.
Gespeichert in:
| Veröffentlicht in: | Angewandte Chemie International Edition 2013-01, Vol.52 (4), p.1203-1207 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1207 |
|---|---|
| container_issue | 4 |
| container_start_page | 1203 |
| container_title | Angewandte Chemie International Edition |
| container_volume | 52 |
| creator | Zhou, Qing Hu, Meirong Zhang, Wei Jiang, Li Perrett, Sarah Zhou, Juanzuo Wang, Jiangyun |
| description | Efficient multiple‐electron redox reactions are performed by galactoase oxidase, cysteine dioxygenase, sulfite reductase, and cytochrome c nitrite reductase. A post‐translationally modified tyrosine–cysteine cross‐link (Tyr‐Cys) in their active sites is essential for their functions. |
| doi_str_mv | 10.1002/anie.201207229 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1701042065</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2865490881</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5439-16b77ebabc61d6e193ca54834d77bb380d827f36e3f3be4a717c8d75098ce6e83</originalsourceid><addsrcrecordid>eNqFkc9v0zAYhiMEYmNw5YgiceGS4l-xneMUtq5QCochJC6W43yl3lK72Ikg--tx1q1CXHqyLT3vo8_fm2WvMZphhMh77SzMCMIECUKqJ9kpLgkuqBD0abozSgshS3ySvYjxJvFSIv48OyEUV4KW8jQbvgbfWPcz7zeQXw7O9Na73K_v39djKOox5nXwMRZL625z6_LP0Ouu8-Duxi3EvBnv2Tk46K3JF874sPNBP4pokQKbses31vdjMlkHL7Nna91FePVwnmXfLi-u66ti-WW-qM-XhSkZrQrMGyGg0Y3huOWAK2p0ySRlrRBNQyVqJRFryoGuaQNMCyyMbEWJKmmAg6Rn2bu9dxf8rwFir7Y2Gug67cAPUWGBMGIE8fI4yirCKROCHUdJ2q1gnE7Wt_-hN34ILv05UbxiXFA6jTnbU2ZadIC12gW71WFUGKmpZjXVrA41p8CbB-3QbKE94I-9JqDaA79tB-MRnTpfLS7-lRf7rI09_DlkdbhVaVxRqu-ruao_Ef5RflipH_Qvc0LCZg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1269467338</pqid></control><display><type>article</type><title>Probing the Function of the Tyr-Cys Cross-Link in Metalloenzymes by the Genetic Incorporation of 3-Methylthiotyrosine</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><creator>Zhou, Qing ; Hu, Meirong ; Zhang, Wei ; Jiang, Li ; Perrett, Sarah ; Zhou, Juanzuo ; Wang, Jiangyun</creator><creatorcontrib>Zhou, Qing ; Hu, Meirong ; Zhang, Wei ; Jiang, Li ; Perrett, Sarah ; Zhou, Juanzuo ; Wang, Jiangyun</creatorcontrib><description>Efficient multiple‐electron redox reactions are performed by galactoase oxidase, cysteine dioxygenase, sulfite reductase, and cytochrome c nitrite reductase. A post‐translationally modified tyrosine–cysteine cross‐link (Tyr‐Cys) in their active sites is essential for their functions.</description><edition>International ed. in English</edition><identifier>ISSN: 1433-7851</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/anie.201207229</identifier><identifier>PMID: 23197358</identifier><identifier>CODEN: ACIEAY</identifier><language>eng</language><publisher>Weinheim: WILEY-VCH Verlag</publisher><subject>Animals ; Catalytic Domain ; Crosslinking ; Cysteine ; Cysteine - chemistry ; Cysteine - metabolism ; Cysteine Dioxygenase - metabolism ; Cytochromes a1 - chemistry ; Cytochromes a1 - metabolism ; Cytochromes c1 - chemistry ; Cytochromes c1 - metabolism ; Galactose Oxidase - metabolism ; Genetics ; heme proteins ; metalloenzymes ; Mutagenesis, Site-Directed ; Myoglobin - genetics ; Myoglobin - metabolism ; Nitrate Reductases - chemistry ; Nitrate Reductases - metabolism ; Nitrites ; non-natural amino acids ; Oxidase ; Oxidation-Reduction ; Redox reactions ; Reductases ; Sulfite Reductase (Ferredoxin) - metabolism ; Sulfites ; sustainable chemistry ; tyr-cys cofactor ; Tyrosine - analogs & derivatives ; Tyrosine - metabolism ; Whales</subject><ispartof>Angewandte Chemie International Edition, 2013-01, Vol.52 (4), p.1203-1207</ispartof><rights>Copyright © 2013 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><rights>Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5439-16b77ebabc61d6e193ca54834d77bb380d827f36e3f3be4a717c8d75098ce6e83</citedby><cites>FETCH-LOGICAL-c5439-16b77ebabc61d6e193ca54834d77bb380d827f36e3f3be4a717c8d75098ce6e83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fanie.201207229$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fanie.201207229$$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/23197358$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhou, Qing</creatorcontrib><creatorcontrib>Hu, Meirong</creatorcontrib><creatorcontrib>Zhang, Wei</creatorcontrib><creatorcontrib>Jiang, Li</creatorcontrib><creatorcontrib>Perrett, Sarah</creatorcontrib><creatorcontrib>Zhou, Juanzuo</creatorcontrib><creatorcontrib>Wang, Jiangyun</creatorcontrib><title>Probing the Function of the Tyr-Cys Cross-Link in Metalloenzymes by the Genetic Incorporation of 3-Methylthiotyrosine</title><title>Angewandte Chemie International Edition</title><addtitle>Angew. Chem. Int. Ed</addtitle><description>Efficient multiple‐electron redox reactions are performed by galactoase oxidase, cysteine dioxygenase, sulfite reductase, and cytochrome c nitrite reductase. A post‐translationally modified tyrosine–cysteine cross‐link (Tyr‐Cys) in their active sites is essential for their functions.</description><subject>Animals</subject><subject>Catalytic Domain</subject><subject>Crosslinking</subject><subject>Cysteine</subject><subject>Cysteine - chemistry</subject><subject>Cysteine - metabolism</subject><subject>Cysteine Dioxygenase - metabolism</subject><subject>Cytochromes a1 - chemistry</subject><subject>Cytochromes a1 - metabolism</subject><subject>Cytochromes c1 - chemistry</subject><subject>Cytochromes c1 - metabolism</subject><subject>Galactose Oxidase - metabolism</subject><subject>Genetics</subject><subject>heme proteins</subject><subject>metalloenzymes</subject><subject>Mutagenesis, Site-Directed</subject><subject>Myoglobin - genetics</subject><subject>Myoglobin - metabolism</subject><subject>Nitrate Reductases - chemistry</subject><subject>Nitrate Reductases - metabolism</subject><subject>Nitrites</subject><subject>non-natural amino acids</subject><subject>Oxidase</subject><subject>Oxidation-Reduction</subject><subject>Redox reactions</subject><subject>Reductases</subject><subject>Sulfite Reductase (Ferredoxin) - metabolism</subject><subject>Sulfites</subject><subject>sustainable chemistry</subject><subject>tyr-cys cofactor</subject><subject>Tyrosine - analogs & derivatives</subject><subject>Tyrosine - metabolism</subject><subject>Whales</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9v0zAYhiMEYmNw5YgiceGS4l-xneMUtq5QCochJC6W43yl3lK72Ikg--tx1q1CXHqyLT3vo8_fm2WvMZphhMh77SzMCMIECUKqJ9kpLgkuqBD0abozSgshS3ySvYjxJvFSIv48OyEUV4KW8jQbvgbfWPcz7zeQXw7O9Na73K_v39djKOox5nXwMRZL625z6_LP0Ouu8-Duxi3EvBnv2Tk46K3JF874sPNBP4pokQKbses31vdjMlkHL7Nna91FePVwnmXfLi-u66ti-WW-qM-XhSkZrQrMGyGg0Y3huOWAK2p0ySRlrRBNQyVqJRFryoGuaQNMCyyMbEWJKmmAg6Rn2bu9dxf8rwFir7Y2Gug67cAPUWGBMGIE8fI4yirCKROCHUdJ2q1gnE7Wt_-hN34ILv05UbxiXFA6jTnbU2ZadIC12gW71WFUGKmpZjXVrA41p8CbB-3QbKE94I-9JqDaA79tB-MRnTpfLS7-lRf7rI09_DlkdbhVaVxRqu-ruao_Ef5RflipH_Qvc0LCZg</recordid><startdate>20130121</startdate><enddate>20130121</enddate><creator>Zhou, Qing</creator><creator>Hu, Meirong</creator><creator>Zhang, Wei</creator><creator>Jiang, Li</creator><creator>Perrett, Sarah</creator><creator>Zhou, Juanzuo</creator><creator>Wang, Jiangyun</creator><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><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>7TM</scope><scope>K9.</scope><scope>7X8</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7SR</scope><scope>8BQ</scope><scope>JG9</scope></search><sort><creationdate>20130121</creationdate><title>Probing the Function of the Tyr-Cys Cross-Link in Metalloenzymes by the Genetic Incorporation of 3-Methylthiotyrosine</title><author>Zhou, Qing ; Hu, Meirong ; Zhang, Wei ; Jiang, Li ; Perrett, Sarah ; Zhou, Juanzuo ; Wang, Jiangyun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5439-16b77ebabc61d6e193ca54834d77bb380d827f36e3f3be4a717c8d75098ce6e83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Animals</topic><topic>Catalytic Domain</topic><topic>Crosslinking</topic><topic>Cysteine</topic><topic>Cysteine - chemistry</topic><topic>Cysteine - metabolism</topic><topic>Cysteine Dioxygenase - metabolism</topic><topic>Cytochromes a1 - chemistry</topic><topic>Cytochromes a1 - metabolism</topic><topic>Cytochromes c1 - chemistry</topic><topic>Cytochromes c1 - metabolism</topic><topic>Galactose Oxidase - metabolism</topic><topic>Genetics</topic><topic>heme proteins</topic><topic>metalloenzymes</topic><topic>Mutagenesis, Site-Directed</topic><topic>Myoglobin - genetics</topic><topic>Myoglobin - metabolism</topic><topic>Nitrate Reductases - chemistry</topic><topic>Nitrate Reductases - metabolism</topic><topic>Nitrites</topic><topic>non-natural amino acids</topic><topic>Oxidase</topic><topic>Oxidation-Reduction</topic><topic>Redox reactions</topic><topic>Reductases</topic><topic>Sulfite Reductase (Ferredoxin) - metabolism</topic><topic>Sulfites</topic><topic>sustainable chemistry</topic><topic>tyr-cys cofactor</topic><topic>Tyrosine - analogs & derivatives</topic><topic>Tyrosine - metabolism</topic><topic>Whales</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhou, Qing</creatorcontrib><creatorcontrib>Hu, Meirong</creatorcontrib><creatorcontrib>Zhang, Wei</creatorcontrib><creatorcontrib>Jiang, Li</creatorcontrib><creatorcontrib>Perrett, Sarah</creatorcontrib><creatorcontrib>Zhou, Juanzuo</creatorcontrib><creatorcontrib>Wang, Jiangyun</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>METADEX</collection><collection>Materials Research Database</collection><jtitle>Angewandte Chemie International Edition</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Zhou, Qing</au><au>Hu, Meirong</au><au>Zhang, Wei</au><au>Jiang, Li</au><au>Perrett, Sarah</au><au>Zhou, Juanzuo</au><au>Wang, Jiangyun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Probing the Function of the Tyr-Cys Cross-Link in Metalloenzymes by the Genetic Incorporation of 3-Methylthiotyrosine</atitle><jtitle>Angewandte Chemie International Edition</jtitle><addtitle>Angew. Chem. Int. Ed</addtitle><date>2013-01-21</date><risdate>2013</risdate><volume>52</volume><issue>4</issue><spage>1203</spage><epage>1207</epage><pages>1203-1207</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><coden>ACIEAY</coden><abstract>Efficient multiple‐electron redox reactions are performed by galactoase oxidase, cysteine dioxygenase, sulfite reductase, and cytochrome c nitrite reductase. A post‐translationally modified tyrosine–cysteine cross‐link (Tyr‐Cys) in their active sites is essential for their functions.</abstract><cop>Weinheim</cop><pub>WILEY-VCH Verlag</pub><pmid>23197358</pmid><doi>10.1002/anie.201207229</doi><tpages>5</tpages><edition>International ed. in English</edition></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1433-7851 |
| ispartof | Angewandte Chemie International Edition, 2013-01, Vol.52 (4), p.1203-1207 |
| issn | 1433-7851 1521-3773 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1701042065 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Animals Catalytic Domain Crosslinking Cysteine Cysteine - chemistry Cysteine - metabolism Cysteine Dioxygenase - metabolism Cytochromes a1 - chemistry Cytochromes a1 - metabolism Cytochromes c1 - chemistry Cytochromes c1 - metabolism Galactose Oxidase - metabolism Genetics heme proteins metalloenzymes Mutagenesis, Site-Directed Myoglobin - genetics Myoglobin - metabolism Nitrate Reductases - chemistry Nitrate Reductases - metabolism Nitrites non-natural amino acids Oxidase Oxidation-Reduction Redox reactions Reductases Sulfite Reductase (Ferredoxin) - metabolism Sulfites sustainable chemistry tyr-cys cofactor Tyrosine - analogs & derivatives Tyrosine - metabolism Whales |
| title | Probing the Function of the Tyr-Cys Cross-Link in Metalloenzymes by the Genetic Incorporation of 3-Methylthiotyrosine |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-07T04%3A49%3A12IST&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=Probing%20the%20Function%20of%20the%20Tyr-Cys%20Cross-Link%20in%20Metalloenzymes%20by%20the%20Genetic%20Incorporation%20of%203-Methylthiotyrosine&rft.jtitle=Angewandte%20Chemie%20International%20Edition&rft.au=Zhou,%20Qing&rft.date=2013-01-21&rft.volume=52&rft.issue=4&rft.spage=1203&rft.epage=1207&rft.pages=1203-1207&rft.issn=1433-7851&rft.eissn=1521-3773&rft.coden=ACIEAY&rft_id=info:doi/10.1002/anie.201207229&rft_dat=%3Cproquest_cross%3E2865490881%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=1269467338&rft_id=info:pmid/23197358&rfr_iscdi=true |