Structure-Function Relationships in [FeFe]-Hydrogenase Active Site Maturation
Since the discovery that, despite the active site complexity, only three gene products suffice to obtain active recombinant [FeFe]-hydrogenase, significant light has been shed on this process. Both the source of the CO and CN− ligands to iron and the assembly site of the catalytic subcluster are kno...
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| Veröffentlicht in: | The Journal of biological chemistry 2012-04, Vol.287 (17), p.13532-13540 |
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| container_title | The Journal of biological chemistry |
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| creator | Nicolet, Yvain Fontecilla-Camps, Juan C. |
| description | Since the discovery that, despite the active site complexity, only three gene products suffice to obtain active recombinant [FeFe]-hydrogenase, significant light has been shed on this process. Both the source of the CO and CN− ligands to iron and the assembly site of the catalytic subcluster are known, and an apo structure of HydF has been published recently. However, the nature of the substrate(s) for the synthesis of the bridging dithiolate ligand to the subcluster remains to be established. From both spectroscopy and model chemistry, it is predicted that an amine function in this ligand plays a central role in catalysis, acting as a base in the heterolytic cleavage of hydrogen. |
| doi_str_mv | 10.1074/jbc.R111.310797 |
| format | Article |
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Both the source of the CO and CN− ligands to iron and the assembly site of the catalytic subcluster are known, and an apo structure of HydF has been published recently. However, the nature of the substrate(s) for the synthesis of the bridging dithiolate ligand to the subcluster remains to be established. 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Both the source of the CO and CN− ligands to iron and the assembly site of the catalytic subcluster are known, and an apo structure of HydF has been published recently. However, the nature of the substrate(s) for the synthesis of the bridging dithiolate ligand to the subcluster remains to be established. From both spectroscopy and model chemistry, it is predicted that an amine function in this ligand plays a central role in catalysis, acting as a base in the heterolytic cleavage of hydrogen.</description><subject>Algorithms</subject><subject>Biochemistry - methods</subject><subject>Catalysis</subject><subject>Catalytic Domain</subject><subject>Chlamydomonas - metabolism</subject><subject>Escherichia coli Proteins - metabolism</subject><subject>Giardia - metabolism</subject><subject>Hydrogen - chemistry</subject><subject>Hydrogenase</subject><subject>Hydrogenase - chemistry</subject><subject>Iron-Sulfur Proteins - chemistry</subject><subject>Ligands</subject><subject>Metalloenzymes</subject><subject>Minireviews</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Molecular Conformation</subject><subject>Protein Structure</subject><subject>Recombinant Proteins - chemistry</subject><subject>S-Adenosylmethionine (SAM)</subject><subject>Spectrophotometry - methods</subject><subject>Structure-Activity Relationship</subject><subject>Thermotoga maritima - metabolism</subject><subject>Trans-Activators - metabolism</subject><subject>X-ray Crystallography</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kc1LAzEQxYMotn6cvckevWybz-7mIpRirdAiVAVBJGyys5qy3a3JbqH_vanVogfnkgn5vTdhHkIXBPcITnh_oU1vTgjpsXCVyQHqEpyymAnyfIi6GFMSSyrSDjrxfoFDcUmOUYdSlkouky6aPTSuNU3rIB63lWlsXUVzKLNt49_tyke2il7GMIbXeLLJXf0GVeYhGgZ0DdGDbSCaZUH_pThDR0VWejj_Pk_R0_jmcTSJp_e3d6PhNDYCyyamnKUcDB3kwgxSo2mS6JQIITHFGhJR4AIPtAatuS641GC0NiLXwEQhUynZKbre-a5avYTcQNW4rFQrZ5eZ26g6s-rvS2Xf1Vu9VoxxTDgPBlffBq7-aME3amm9gbLMKqhbrwjGkjCK-SCg_R1qXO29g2I_hmC1DUGFENQ2BLULISguf_9uz_9sPQByB0DY0dqCU95YqAzk1oFpVF7bf80_AfxRmHU</recordid><startdate>20120420</startdate><enddate>20120420</enddate><creator>Nicolet, Yvain</creator><creator>Fontecilla-Camps, Juan C.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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><scope>5PM</scope></search><sort><creationdate>20120420</creationdate><title>Structure-Function Relationships in [FeFe]-Hydrogenase Active Site Maturation</title><author>Nicolet, Yvain ; 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| subjects | Algorithms Biochemistry - methods Catalysis Catalytic Domain Chlamydomonas - metabolism Escherichia coli Proteins - metabolism Giardia - metabolism Hydrogen - chemistry Hydrogenase Hydrogenase - chemistry Iron-Sulfur Proteins - chemistry Ligands Metalloenzymes Minireviews Models, Chemical Models, Molecular Molecular Conformation Protein Structure Recombinant Proteins - chemistry S-Adenosylmethionine (SAM) Spectrophotometry - methods Structure-Activity Relationship Thermotoga maritima - metabolism Trans-Activators - metabolism X-ray Crystallography |
| title | Structure-Function Relationships in [FeFe]-Hydrogenase Active Site Maturation |
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