Unusual Heme−Histidine Bond in the Active Site of a Chaperone
The heme chaperone CcmE is essential for the delivery of heme to c-type cytochromes. It forms an unusual transient, yet covalent, bond between an essential histidine, H130, and heme. We report on the discovery of the chemical structure of this bond solved by NMR, where the heme vinyl is cross-linked...
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| Veröffentlicht in: | Journal of the American Chemical Society 2005-03, Vol.127 (11), p.3716-3717 |
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| container_end_page | 3717 |
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| container_issue | 11 |
| container_start_page | 3716 |
| container_title | Journal of the American Chemical Society |
| container_volume | 127 |
| creator | Lee, Donghan Pervushin, Konstantin Bischof, Daniela Braun, Martin Thöny-Meyer, Linda |
| description | The heme chaperone CcmE is essential for the delivery of heme to c-type cytochromes. It forms an unusual transient, yet covalent, bond between an essential histidine, H130, and heme. We report on the discovery of the chemical structure of this bond solved by NMR, where the heme vinyl is cross-linked at the β carbon to the Nδ1 of H130. As this type of heme linkage has not been described previously in any cytochrome or hemoprotein, it represents a novel type of heme−histidine complex. |
| doi_str_mv | 10.1021/ja044658e |
| format | Article |
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It forms an unusual transient, yet covalent, bond between an essential histidine, H130, and heme. We report on the discovery of the chemical structure of this bond solved by NMR, where the heme vinyl is cross-linked at the β carbon to the Nδ1 of H130. As this type of heme linkage has not been described previously in any cytochrome or hemoprotein, it represents a novel type of heme−histidine complex.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja044658e</identifier><identifier>PMID: 15771504</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Amino Acid Sequence ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Binding Sites ; Biological and medical sciences ; Fundamental and applied biological sciences. 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Am. Chem. Soc</addtitle><description>The heme chaperone CcmE is essential for the delivery of heme to c-type cytochromes. It forms an unusual transient, yet covalent, bond between an essential histidine, H130, and heme. We report on the discovery of the chemical structure of this bond solved by NMR, where the heme vinyl is cross-linked at the β carbon to the Nδ1 of H130. As this type of heme linkage has not been described previously in any cytochrome or hemoprotein, it represents a novel type of heme−histidine complex.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Heme - chemistry</subject><subject>Heme - metabolism</subject><subject>Hemeproteins - chemistry</subject><subject>Hemeproteins - metabolism</subject><subject>Histidine - chemistry</subject><subject>Histidine - metabolism</subject><subject>Interactions. Associations</subject><subject>Intermolecular phenomena</subject><subject>Molecular biophysics</subject><subject>Molecular Chaperones - chemistry</subject><subject>Molecular Chaperones - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpt0M1qGzEUBWBRGmon7SIvELRpIItJpdHoZ1YlGZI6xdCCbehOyNIdLHc840gzIX2DrPOIeZIo2MSbrsRFH4fDQeiUkktKcvptbUhRCK7gAxpTnpOM01x8RGNCSJ5JJdgIHce4TmeRK_oJjSiXknJSjNH3RTvEwTR4Aht4eXqe-Nh751vA113rsG9xvwJ8ZXv_AHjme8BdjQ2uVmYLoWvhMzqqTRPhy_49QYvbm3k1yaa_ftxVV9PMMEX7bGkJLxitnSpz5aC0NbEllMrWjDkuqYPUeFnIMhemcAWTDLiw0nGeg3KuZCfofJe7Dd39ALHXGx8tNI1poRuiFpJTpQhP8GIHbehiDFDrbfAbE_5pSvTbWvp9rWTP9qHDcgPuIPfzJPB1D0y0pqmDaa2PBycE47QUyWU7l9aDx_d_E_6mYkxyPf8903-qn2xazSd6esg1Nup1N4Q2bfefgq9PhYvm</recordid><startdate>20050323</startdate><enddate>20050323</enddate><creator>Lee, Donghan</creator><creator>Pervushin, Konstantin</creator><creator>Bischof, Daniela</creator><creator>Braun, Martin</creator><creator>Thöny-Meyer, Linda</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>IQODW</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>7X8</scope></search><sort><creationdate>20050323</creationdate><title>Unusual Heme−Histidine Bond in the Active Site of a Chaperone</title><author>Lee, Donghan ; Pervushin, Konstantin ; Bischof, Daniela ; Braun, Martin ; Thöny-Meyer, Linda</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a381t-bc05431fd8928de9cf0c9e98cf33d571de126b47926a4d4373e56c7d552e8dd93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Heme - chemistry</topic><topic>Heme - metabolism</topic><topic>Hemeproteins - chemistry</topic><topic>Hemeproteins - metabolism</topic><topic>Histidine - chemistry</topic><topic>Histidine - metabolism</topic><topic>Interactions. Associations</topic><topic>Intermolecular phenomena</topic><topic>Molecular biophysics</topic><topic>Molecular Chaperones - chemistry</topic><topic>Molecular Chaperones - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Donghan</creatorcontrib><creatorcontrib>Pervushin, Konstantin</creatorcontrib><creatorcontrib>Bischof, Daniela</creatorcontrib><creatorcontrib>Braun, Martin</creatorcontrib><creatorcontrib>Thöny-Meyer, Linda</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><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>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Donghan</au><au>Pervushin, Konstantin</au><au>Bischof, Daniela</au><au>Braun, Martin</au><au>Thöny-Meyer, Linda</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Unusual Heme−Histidine Bond in the Active Site of a Chaperone</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2005-03-23</date><risdate>2005</risdate><volume>127</volume><issue>11</issue><spage>3716</spage><epage>3717</epage><pages>3716-3717</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>The heme chaperone CcmE is essential for the delivery of heme to c-type cytochromes. It forms an unusual transient, yet covalent, bond between an essential histidine, H130, and heme. We report on the discovery of the chemical structure of this bond solved by NMR, where the heme vinyl is cross-linked at the β carbon to the Nδ1 of H130. As this type of heme linkage has not been described previously in any cytochrome or hemoprotein, it represents a novel type of heme−histidine complex.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>15771504</pmid><doi>10.1021/ja044658e</doi><tpages>2</tpages></addata></record> |
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| identifier | ISSN: 0002-7863 |
| ispartof | Journal of the American Chemical Society, 2005-03, Vol.127 (11), p.3716-3717 |
| issn | 0002-7863 1520-5126 |
| language | eng |
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| source | MEDLINE; ACS Publications |
| subjects | Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Biological and medical sciences Fundamental and applied biological sciences. Psychology Heme - chemistry Heme - metabolism Hemeproteins - chemistry Hemeproteins - metabolism Histidine - chemistry Histidine - metabolism Interactions. Associations Intermolecular phenomena Molecular biophysics Molecular Chaperones - chemistry Molecular Chaperones - metabolism Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization |
| title | Unusual Heme−Histidine Bond in the Active Site of a Chaperone |
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