Structural properties of cyanobacterial hemoglobins: the unusual heme-protein cross-link of Synechocystis sp. PCC 6803 Hb and Synechococcus sp. PCC 7002 Hb
The truncated hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002 ligate the heme iron with two axial histidines (HisF8 and HisE10). In addition, these two proteins are able to form a heme-protein cross-link between a vinyl substituent and a histidine at position 16 of the H h...
Gespeichert in:
| Veröffentlicht in: | Micron (Oxford, England : 1993) England : 1993), 2004, Vol.35 (1), p.71-72 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 72 |
|---|---|
| container_issue | 1 |
| container_start_page | 71 |
| container_title | Micron (Oxford, England : 1993) |
| container_volume | 35 |
| creator | Lecomte, Juliette T.J Vuletich, David A Vu, B.Christie Kuriakose, Syna A Scott, Nancy L Falzone, Christopher J |
| description | The truncated hemoglobins from
Synechocystis sp. PCC 6803 and
Synechococcus sp. PCC 7002 ligate the heme iron with two axial histidines (HisF8 and HisE10). In addition, these two proteins are able to form a heme-protein cross-link between a vinyl substituent and a histidine at position 16 of the H helix. The product is a protein with improved resistance to thermal and acid denaturation. |
| doi_str_mv | 10.1016/j.micron.2003.10.020 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71767512</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0968432803001525</els_id><sourcerecordid>71767512</sourcerecordid><originalsourceid>FETCH-LOGICAL-c358t-b6a05e2d0ef20513278f38198e0e176b98e67a56ab9056a2ee4d22820bb5b6883</originalsourceid><addsrcrecordid>eNp9kcGO0zAQhi0EYsvCGyDkE7eEsdM4DgckVAGLtBJIC2fLdibUJbGL7azUZ-FlcUnF3rjYo5lvfvvXT8hLBjUDJt4c6tnZGHzNAZrSqoHDI7JhspPVlvfsMdlAL0rdcHlFnqV0AAC2FfCUXLEWGsH7dkN-3-W42LxEPdFjDEeM2WGiYaT2pH0w2maMrgz3OIcfUzDOp7c075EufknLOsCqrGZ0npYPpVRNzv88S9ydPNp9sKeUXaLpWNOvux0VEhp6Y6j2wz8iWLs8EB0AL8Rz8mTUU8IXl_uafP_44dvuprr98unz7v1tZZtW5soIDS3yAXDk0LKGd3JsJOslArJOmFKITrdCmx7KyRG3A-eSgzGtEVI21-T1qltc_FowZTW7ZHGatMewJNUVla5lvIDbFfxrM-KojtHNOp4UA3UORR3UGoo6h3LullDK2quL_mJmHB6WLikU4N0KYHF57zCqZB16i4OLaLMagvv_C38ASuCfrw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71767512</pqid></control><display><type>article</type><title>Structural properties of cyanobacterial hemoglobins: the unusual heme-protein cross-link of Synechocystis sp. PCC 6803 Hb and Synechococcus sp. PCC 7002 Hb</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Lecomte, Juliette T.J ; Vuletich, David A ; Vu, B.Christie ; Kuriakose, Syna A ; Scott, Nancy L ; Falzone, Christopher J</creator><creatorcontrib>Lecomte, Juliette T.J ; Vuletich, David A ; Vu, B.Christie ; Kuriakose, Syna A ; Scott, Nancy L ; Falzone, Christopher J</creatorcontrib><description>The truncated hemoglobins from
Synechocystis sp. PCC 6803 and
Synechococcus sp. PCC 7002 ligate the heme iron with two axial histidines (HisF8 and HisE10). In addition, these two proteins are able to form a heme-protein cross-link between a vinyl substituent and a histidine at position 16 of the H helix. The product is a protein with improved resistance to thermal and acid denaturation.</description><identifier>ISSN: 0968-4328</identifier><identifier>EISSN: 1878-4291</identifier><identifier>DOI: 10.1016/j.micron.2003.10.020</identifier><identifier>PMID: 15036295</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Bacterial Proteins - chemistry ; Covalent attachment ; Cyanobacteria - chemistry ; Cyanoglobin ; Hemichrome ; Hemoglobins - chemistry ; Nuclear magnetic resonance ; Paramagnetic complex ; Truncated hemoglobin ; Truncated Hemoglobins</subject><ispartof>Micron (Oxford, England : 1993), 2004, Vol.35 (1), p.71-72</ispartof><rights>2003 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c358t-b6a05e2d0ef20513278f38198e0e176b98e67a56ab9056a2ee4d22820bb5b6883</citedby><cites>FETCH-LOGICAL-c358t-b6a05e2d0ef20513278f38198e0e176b98e67a56ab9056a2ee4d22820bb5b6883</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0968432803001525$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,4010,27902,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15036295$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lecomte, Juliette T.J</creatorcontrib><creatorcontrib>Vuletich, David A</creatorcontrib><creatorcontrib>Vu, B.Christie</creatorcontrib><creatorcontrib>Kuriakose, Syna A</creatorcontrib><creatorcontrib>Scott, Nancy L</creatorcontrib><creatorcontrib>Falzone, Christopher J</creatorcontrib><title>Structural properties of cyanobacterial hemoglobins: the unusual heme-protein cross-link of Synechocystis sp. PCC 6803 Hb and Synechococcus sp. PCC 7002 Hb</title><title>Micron (Oxford, England : 1993)</title><addtitle>Micron</addtitle><description>The truncated hemoglobins from
Synechocystis sp. PCC 6803 and
Synechococcus sp. PCC 7002 ligate the heme iron with two axial histidines (HisF8 and HisE10). In addition, these two proteins are able to form a heme-protein cross-link between a vinyl substituent and a histidine at position 16 of the H helix. The product is a protein with improved resistance to thermal and acid denaturation.</description><subject>Bacterial Proteins - chemistry</subject><subject>Covalent attachment</subject><subject>Cyanobacteria - chemistry</subject><subject>Cyanoglobin</subject><subject>Hemichrome</subject><subject>Hemoglobins - chemistry</subject><subject>Nuclear magnetic resonance</subject><subject>Paramagnetic complex</subject><subject>Truncated hemoglobin</subject><subject>Truncated Hemoglobins</subject><issn>0968-4328</issn><issn>1878-4291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcGO0zAQhi0EYsvCGyDkE7eEsdM4DgckVAGLtBJIC2fLdibUJbGL7azUZ-FlcUnF3rjYo5lvfvvXT8hLBjUDJt4c6tnZGHzNAZrSqoHDI7JhspPVlvfsMdlAL0rdcHlFnqV0AAC2FfCUXLEWGsH7dkN-3-W42LxEPdFjDEeM2WGiYaT2pH0w2maMrgz3OIcfUzDOp7c075EufknLOsCqrGZ0npYPpVRNzv88S9ydPNp9sKeUXaLpWNOvux0VEhp6Y6j2wz8iWLs8EB0AL8Rz8mTUU8IXl_uafP_44dvuprr98unz7v1tZZtW5soIDS3yAXDk0LKGd3JsJOslArJOmFKITrdCmx7KyRG3A-eSgzGtEVI21-T1qltc_FowZTW7ZHGatMewJNUVla5lvIDbFfxrM-KojtHNOp4UA3UORR3UGoo6h3LullDK2quL_mJmHB6WLikU4N0KYHF57zCqZB16i4OLaLMagvv_C38ASuCfrw</recordid><startdate>2004</startdate><enddate>2004</enddate><creator>Lecomte, Juliette T.J</creator><creator>Vuletich, David A</creator><creator>Vu, B.Christie</creator><creator>Kuriakose, Syna A</creator><creator>Scott, Nancy L</creator><creator>Falzone, Christopher J</creator><general>Elsevier Ltd</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>2004</creationdate><title>Structural properties of cyanobacterial hemoglobins: the unusual heme-protein cross-link of Synechocystis sp. PCC 6803 Hb and Synechococcus sp. PCC 7002 Hb</title><author>Lecomte, Juliette T.J ; Vuletich, David A ; Vu, B.Christie ; Kuriakose, Syna A ; Scott, Nancy L ; Falzone, Christopher J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c358t-b6a05e2d0ef20513278f38198e0e176b98e67a56ab9056a2ee4d22820bb5b6883</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Bacterial Proteins - chemistry</topic><topic>Covalent attachment</topic><topic>Cyanobacteria - chemistry</topic><topic>Cyanoglobin</topic><topic>Hemichrome</topic><topic>Hemoglobins - chemistry</topic><topic>Nuclear magnetic resonance</topic><topic>Paramagnetic complex</topic><topic>Truncated hemoglobin</topic><topic>Truncated Hemoglobins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lecomte, Juliette T.J</creatorcontrib><creatorcontrib>Vuletich, David A</creatorcontrib><creatorcontrib>Vu, B.Christie</creatorcontrib><creatorcontrib>Kuriakose, Syna A</creatorcontrib><creatorcontrib>Scott, Nancy L</creatorcontrib><creatorcontrib>Falzone, Christopher J</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>Micron (Oxford, England : 1993)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lecomte, Juliette T.J</au><au>Vuletich, David A</au><au>Vu, B.Christie</au><au>Kuriakose, Syna A</au><au>Scott, Nancy L</au><au>Falzone, Christopher J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural properties of cyanobacterial hemoglobins: the unusual heme-protein cross-link of Synechocystis sp. PCC 6803 Hb and Synechococcus sp. PCC 7002 Hb</atitle><jtitle>Micron (Oxford, England : 1993)</jtitle><addtitle>Micron</addtitle><date>2004</date><risdate>2004</risdate><volume>35</volume><issue>1</issue><spage>71</spage><epage>72</epage><pages>71-72</pages><issn>0968-4328</issn><eissn>1878-4291</eissn><abstract>The truncated hemoglobins from
Synechocystis sp. PCC 6803 and
Synechococcus sp. PCC 7002 ligate the heme iron with two axial histidines (HisF8 and HisE10). In addition, these two proteins are able to form a heme-protein cross-link between a vinyl substituent and a histidine at position 16 of the H helix. The product is a protein with improved resistance to thermal and acid denaturation.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>15036295</pmid><doi>10.1016/j.micron.2003.10.020</doi><tpages>2</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0968-4328 |
| ispartof | Micron (Oxford, England : 1993), 2004, Vol.35 (1), p.71-72 |
| issn | 0968-4328 1878-4291 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71767512 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Bacterial Proteins - chemistry Covalent attachment Cyanobacteria - chemistry Cyanoglobin Hemichrome Hemoglobins - chemistry Nuclear magnetic resonance Paramagnetic complex Truncated hemoglobin Truncated Hemoglobins |
| title | Structural properties of cyanobacterial hemoglobins: the unusual heme-protein cross-link of Synechocystis sp. PCC 6803 Hb and Synechococcus sp. PCC 7002 Hb |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T04%3A28%3A00IST&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=Structural%20properties%20of%20cyanobacterial%20hemoglobins:%20the%20unusual%20heme-protein%20cross-link%20of%20Synechocystis%20sp.%20PCC%206803%20Hb%20and%20Synechococcus%20sp.%20PCC%207002%20Hb&rft.jtitle=Micron%20(Oxford,%20England%20:%201993)&rft.au=Lecomte,%20Juliette%20T.J&rft.date=2004&rft.volume=35&rft.issue=1&rft.spage=71&rft.epage=72&rft.pages=71-72&rft.issn=0968-4328&rft.eissn=1878-4291&rft_id=info:doi/10.1016/j.micron.2003.10.020&rft_dat=%3Cproquest_cross%3E71767512%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=71767512&rft_id=info:pmid/15036295&rft_els_id=S0968432803001525&rfr_iscdi=true |