Catalytic and Biocatalytic Iron Porphyrin Carbene Formation: Effects of Binding Mode, Carbene Substituent, Porphyrin Substituent, and Protein Axial Ligand
Iron porphyrin carbenes (IPCs) are important intermediates in various chemical reactions catalyzed by iron porphyrins and engineered heme proteins, as well as in the metabolism of various xenobiotics by cytochrome P450. However, there are no prior theoretical reports to help understand their formati...
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| Veröffentlicht in: | Journal of the American Chemical Society 2015-06, Vol.137 (24), p.7560-7563 |
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| creator | Khade, Rahul L Zhang, Yong |
| description | Iron porphyrin carbenes (IPCs) are important intermediates in various chemical reactions catalyzed by iron porphyrins and engineered heme proteins, as well as in the metabolism of various xenobiotics by cytochrome P450. However, there are no prior theoretical reports to help understand their formation mechanisms and identify key information governing the binding mode, formation feasibility, and stability/reactivity. A systematic quantum chemical study was performed to investigate the effects of carbene substituent, porphyrin substituent, and axial ligand on IPC formation pathways. Results not only are consistent with available experimental data but also provide a number of unprecedented insights into electronic, steric, and H-bonding effects of various structural factors on IPC formation mechanisms. These results shall facilitate research on IPC and related systems for sustainable chemical catalysis and biocatalysis. |
| doi_str_mv | 10.1021/jacs.5b03437 |
| format | Article |
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However, there are no prior theoretical reports to help understand their formation mechanisms and identify key information governing the binding mode, formation feasibility, and stability/reactivity. A systematic quantum chemical study was performed to investigate the effects of carbene substituent, porphyrin substituent, and axial ligand on IPC formation pathways. Results not only are consistent with available experimental data but also provide a number of unprecedented insights into electronic, steric, and H-bonding effects of various structural factors on IPC formation mechanisms. These results shall facilitate research on IPC and related systems for sustainable chemical catalysis and biocatalysis.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/jacs.5b03437</identifier><identifier>PMID: 26067900</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Binding ; Biocatalysis ; Carbenes ; Catalysis ; Communication ; Cytochrome P-450 Enzyme System - metabolism ; Formations ; Hemeproteins - metabolism ; Interprocessor communication ; Iron ; Iron Compounds - chemistry ; Iron Compounds - metabolism ; Ligands ; Metalloporphyrins - chemistry ; Metalloporphyrins - metabolism ; Methane - analogs & derivatives ; Methane - chemistry ; Methane - metabolism ; Models, Molecular ; Porphyrins ; Proteins ; Thermodynamics</subject><ispartof>Journal of the American Chemical Society, 2015-06, Vol.137 (24), p.7560-7563</ispartof><rights>Copyright © 2015 American Chemical Society</rights><rights>Copyright © 2015 American Chemical Society 2015 American Chemical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a516t-1bf2bc804c0b06bb7c3b49e327d70a7bd108d560df69b56e77b6b12bc24b03a03</citedby><cites>FETCH-LOGICAL-a516t-1bf2bc804c0b06bb7c3b49e327d70a7bd108d560df69b56e77b6b12bc24b03a03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jacs.5b03437$$EPDF$$P50$$Gacs$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jacs.5b03437$$EHTML$$P50$$Gacs$$Hfree_for_read</linktohtml><link.rule.ids>230,315,781,785,886,2766,27081,27929,27930,56743,56793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26067900$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Khade, Rahul L</creatorcontrib><creatorcontrib>Zhang, Yong</creatorcontrib><title>Catalytic and Biocatalytic Iron Porphyrin Carbene Formation: Effects of Binding Mode, Carbene Substituent, Porphyrin Substituent, and Protein Axial Ligand</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>Iron porphyrin carbenes (IPCs) are important intermediates in various chemical reactions catalyzed by iron porphyrins and engineered heme proteins, as well as in the metabolism of various xenobiotics by cytochrome P450. However, there are no prior theoretical reports to help understand their formation mechanisms and identify key information governing the binding mode, formation feasibility, and stability/reactivity. A systematic quantum chemical study was performed to investigate the effects of carbene substituent, porphyrin substituent, and axial ligand on IPC formation pathways. Results not only are consistent with available experimental data but also provide a number of unprecedented insights into electronic, steric, and H-bonding effects of various structural factors on IPC formation mechanisms. These results shall facilitate research on IPC and related systems for sustainable chemical catalysis and biocatalysis.</description><subject>Binding</subject><subject>Biocatalysis</subject><subject>Carbenes</subject><subject>Catalysis</subject><subject>Communication</subject><subject>Cytochrome P-450 Enzyme System - metabolism</subject><subject>Formations</subject><subject>Hemeproteins - metabolism</subject><subject>Interprocessor communication</subject><subject>Iron</subject><subject>Iron Compounds - chemistry</subject><subject>Iron Compounds - metabolism</subject><subject>Ligands</subject><subject>Metalloporphyrins - chemistry</subject><subject>Metalloporphyrins - metabolism</subject><subject>Methane - analogs & derivatives</subject><subject>Methane - chemistry</subject><subject>Methane - metabolism</subject><subject>Models, Molecular</subject><subject>Porphyrins</subject><subject>Proteins</subject><subject>Thermodynamics</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>N~.</sourceid><sourceid>EIF</sourceid><recordid>eNqFkU1vEzEQhi0Eomnhxhn5yCFbxl6vvcsBqUQtVAqiEnC2bK83dbSxg-1F5K_wa-uoIbQSEifLM8-88_Ei9IrAOQFK3q6VSeeNhprV4gmakYZC1RDKn6IZANBKtLw-QacprcuX0ZY8RyeUAxcdwAz9Xqisxl12Bivf4w8umGPgOgaPb0Lc3u6i83ihorbe4qsQNyq74N_hy2GwJicchlLpe-dX-HPo7fzIfp10yi5P1uf5A6lH4X3fmxiyLYmLX06NeOlWJfgCPRvUmOzLw3uGvl9dflt8qpZfPl4vLpaVagjPFdED1aYFZkAD11qYWrPO1lT0ApTQPYG2bzj0A-90w60QmmtSSigrR1NQn6H397rbSW9sb8pQUY1yG91GxZ0MysnHGe9u5Sr8lIy1lBFeBN4cBGL4MdmU5cYlY8dReRumJElLm4aQQv8f5R2hXc2gLuj8HjUxpBTtcJyIgNw7L_fOy4PzBX_9cIsj_Mfqv633VeswRV-O-m-tO10mugY</recordid><startdate>20150624</startdate><enddate>20150624</enddate><creator>Khade, Rahul L</creator><creator>Zhang, Yong</creator><general>American Chemical Society</general><scope>N~.</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>7SR</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>5PM</scope></search><sort><creationdate>20150624</creationdate><title>Catalytic and Biocatalytic Iron Porphyrin Carbene Formation: Effects of Binding Mode, Carbene Substituent, Porphyrin Substituent, and Protein Axial Ligand</title><author>Khade, Rahul L ; Zhang, Yong</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a516t-1bf2bc804c0b06bb7c3b49e327d70a7bd108d560df69b56e77b6b12bc24b03a03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Binding</topic><topic>Biocatalysis</topic><topic>Carbenes</topic><topic>Catalysis</topic><topic>Communication</topic><topic>Cytochrome P-450 Enzyme System - metabolism</topic><topic>Formations</topic><topic>Hemeproteins - metabolism</topic><topic>Interprocessor communication</topic><topic>Iron</topic><topic>Iron Compounds - chemistry</topic><topic>Iron Compounds - metabolism</topic><topic>Ligands</topic><topic>Metalloporphyrins - chemistry</topic><topic>Metalloporphyrins - metabolism</topic><topic>Methane - analogs & derivatives</topic><topic>Methane - chemistry</topic><topic>Methane - metabolism</topic><topic>Models, Molecular</topic><topic>Porphyrins</topic><topic>Proteins</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Khade, Rahul L</creatorcontrib><creatorcontrib>Zhang, Yong</creatorcontrib><collection>American Chemical Society (ACS) Open Access</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><collection>Engineered Materials Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Khade, Rahul L</au><au>Zhang, Yong</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Catalytic and Biocatalytic Iron Porphyrin Carbene Formation: Effects of Binding Mode, Carbene Substituent, Porphyrin Substituent, and Protein Axial Ligand</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2015-06-24</date><risdate>2015</risdate><volume>137</volume><issue>24</issue><spage>7560</spage><epage>7563</epage><pages>7560-7563</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><abstract>Iron porphyrin carbenes (IPCs) are important intermediates in various chemical reactions catalyzed by iron porphyrins and engineered heme proteins, as well as in the metabolism of various xenobiotics by cytochrome P450. However, there are no prior theoretical reports to help understand their formation mechanisms and identify key information governing the binding mode, formation feasibility, and stability/reactivity. A systematic quantum chemical study was performed to investigate the effects of carbene substituent, porphyrin substituent, and axial ligand on IPC formation pathways. 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| ispartof | Journal of the American Chemical Society, 2015-06, Vol.137 (24), p.7560-7563 |
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| source | MEDLINE; ACS Publications |
| subjects | Binding Biocatalysis Carbenes Catalysis Communication Cytochrome P-450 Enzyme System - metabolism Formations Hemeproteins - metabolism Interprocessor communication Iron Iron Compounds - chemistry Iron Compounds - metabolism Ligands Metalloporphyrins - chemistry Metalloporphyrins - metabolism Methane - analogs & derivatives Methane - chemistry Methane - metabolism Models, Molecular Porphyrins Proteins Thermodynamics |
| title | Catalytic and Biocatalytic Iron Porphyrin Carbene Formation: Effects of Binding Mode, Carbene Substituent, Porphyrin Substituent, and Protein Axial Ligand |
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