Setting an Upper Limit on the Myoglobin Iron(IV)Hydroxide pK a: Insight into Axial Ligand Tuning in Heme Protein Catalysis
To provide insight into the iron(IV)hydroxide pK a of histidine ligated heme proteins, we have probed the active site of myoglobin compound II over the pH range of 3.9–9.5, using EXAFS, Mössbauer, and resonance Raman spectroscopies. We find no indication of ferryl protonation over this pH range,...
Gespeichert in:
| Veröffentlicht in: | Journal of the American Chemical Society 2014-06, Vol.136 (25), p.9124-9131 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 9131 |
|---|---|
| container_issue | 25 |
| container_start_page | 9124 |
| container_title | Journal of the American Chemical Society |
| container_volume | 136 |
| creator | Yosca, Timothy H Behan, Rachel K Krest, Courtney M Onderko, Elizabeth L Langston, Matthew C Green, Michael T |
| description | To provide insight into the iron(IV)hydroxide pK a of histidine ligated heme proteins, we have probed the active site of myoglobin compound II over the pH range of 3.9–9.5, using EXAFS, Mössbauer, and resonance Raman spectroscopies. We find no indication of ferryl protonation over this pH range, allowing us to set an upper limit of 2.7 on the iron(IV)hydroxide pK a in myoglobin. Together with the recent determination of an iron(IV)hydroxide pK a ∼ 12 in the thiolate-ligated heme enzyme cytochrome P450, this result provides insight into Nature’s ability to tune catalytic function through its choice of axial ligand. |
| doi_str_mv | 10.1021/ja503588n |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_1540704435</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1540704435</sourcerecordid><originalsourceid>FETCH-LOGICAL-a171t-788fbaf2f9613fa312f5274525ce3d71b0dd27bd76273c055569a3ff4eb1c59b3</originalsourceid><addsrcrecordid>eNo9kV1LwzAYhYMobk4v_AOSG2FeVPPRNK13Y6grThTcvC1pm3YZbVKbFFZ_vR2bXr0ceM7h8B4ArjG6x4jgh61giLIw1CdgjBlBHsMkOAVjhBDxeBjQEbiwdjtIn4T4HIyIH3KGcTQGP5_SOaVLKDRcN41s4VLVykGjodtI-NabsjKp0jBujZ7GX3eLPm_NTuUSNq9QPMJYW1VuHFTaGTjbKVENCaXQOVx1eh88eBeylvCjNU4OYi6cqHqr7CU4K0Rl5dXxTsD6-Wk1X3jL95d4Plt6AnPshv5hkYqCFFGAaSEoJgUj3GeEZZLmHKcozwlPcx4QTjPEGAsiQYvClynOWJTSCZgecpvWfHfSuqRWNpNVJbQ0nU0w8xFHvk_ZgN4c0S6tZZ40rapF2yd__xqA2wMgMptsTdfqoXmCUbLfIfnfgf4CvYR3EA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1540704435</pqid></control><display><type>article</type><title>Setting an Upper Limit on the Myoglobin Iron(IV)Hydroxide pK a: Insight into Axial Ligand Tuning in Heme Protein Catalysis</title><source>MEDLINE</source><source>American Chemical Society Journals</source><creator>Yosca, Timothy H ; Behan, Rachel K ; Krest, Courtney M ; Onderko, Elizabeth L ; Langston, Matthew C ; Green, Michael T</creator><creatorcontrib>Yosca, Timothy H ; Behan, Rachel K ; Krest, Courtney M ; Onderko, Elizabeth L ; Langston, Matthew C ; Green, Michael T</creatorcontrib><description>To provide insight into the iron(IV)hydroxide pK a of histidine ligated heme proteins, we have probed the active site of myoglobin compound II over the pH range of 3.9–9.5, using EXAFS, Mössbauer, and resonance Raman spectroscopies. We find no indication of ferryl protonation over this pH range, allowing us to set an upper limit of 2.7 on the iron(IV)hydroxide pK a in myoglobin. Together with the recent determination of an iron(IV)hydroxide pK a ∼ 12 in the thiolate-ligated heme enzyme cytochrome P450, this result provides insight into Nature’s ability to tune catalytic function through its choice of axial ligand.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja503588n</identifier><identifier>PMID: 24875119</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Catalysis ; Catalytic Domain ; Histidine - chemistry ; Hydrogen-Ion Concentration ; Hydroxides - chemistry ; Iron - chemistry ; Ligands ; Molecular Structure ; Myoglobin - chemistry ; Spectroscopy, Mossbauer ; Spectrum Analysis, Raman ; X-Ray Absorption Spectroscopy</subject><ispartof>Journal of the American Chemical Society, 2014-06, Vol.136 (25), p.9124-9131</ispartof><rights>Copyright © 2014 American Chemical Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/ja503588n$$EPDF$$P50$$Gacs$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/ja503588n$$EHTML$$P50$$Gacs$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24875119$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yosca, Timothy H</creatorcontrib><creatorcontrib>Behan, Rachel K</creatorcontrib><creatorcontrib>Krest, Courtney M</creatorcontrib><creatorcontrib>Onderko, Elizabeth L</creatorcontrib><creatorcontrib>Langston, Matthew C</creatorcontrib><creatorcontrib>Green, Michael T</creatorcontrib><title>Setting an Upper Limit on the Myoglobin Iron(IV)Hydroxide pK a: Insight into Axial Ligand Tuning in Heme Protein Catalysis</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>To provide insight into the iron(IV)hydroxide pK a of histidine ligated heme proteins, we have probed the active site of myoglobin compound II over the pH range of 3.9–9.5, using EXAFS, Mössbauer, and resonance Raman spectroscopies. We find no indication of ferryl protonation over this pH range, allowing us to set an upper limit of 2.7 on the iron(IV)hydroxide pK a in myoglobin. Together with the recent determination of an iron(IV)hydroxide pK a ∼ 12 in the thiolate-ligated heme enzyme cytochrome P450, this result provides insight into Nature’s ability to tune catalytic function through its choice of axial ligand.</description><subject>Catalysis</subject><subject>Catalytic Domain</subject><subject>Histidine - chemistry</subject><subject>Hydrogen-Ion Concentration</subject><subject>Hydroxides - chemistry</subject><subject>Iron - chemistry</subject><subject>Ligands</subject><subject>Molecular Structure</subject><subject>Myoglobin - chemistry</subject><subject>Spectroscopy, Mossbauer</subject><subject>Spectrum Analysis, Raman</subject><subject>X-Ray Absorption Spectroscopy</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>N~.</sourceid><sourceid>EIF</sourceid><recordid>eNo9kV1LwzAYhYMobk4v_AOSG2FeVPPRNK13Y6grThTcvC1pm3YZbVKbFFZ_vR2bXr0ceM7h8B4ArjG6x4jgh61giLIw1CdgjBlBHsMkOAVjhBDxeBjQEbiwdjtIn4T4HIyIH3KGcTQGP5_SOaVLKDRcN41s4VLVykGjodtI-NabsjKp0jBujZ7GX3eLPm_NTuUSNq9QPMJYW1VuHFTaGTjbKVENCaXQOVx1eh88eBeylvCjNU4OYi6cqHqr7CU4K0Rl5dXxTsD6-Wk1X3jL95d4Plt6AnPshv5hkYqCFFGAaSEoJgUj3GeEZZLmHKcozwlPcx4QTjPEGAsiQYvClynOWJTSCZgecpvWfHfSuqRWNpNVJbQ0nU0w8xFHvk_ZgN4c0S6tZZ40rapF2yd__xqA2wMgMptsTdfqoXmCUbLfIfnfgf4CvYR3EA</recordid><startdate>20140625</startdate><enddate>20140625</enddate><creator>Yosca, Timothy H</creator><creator>Behan, Rachel K</creator><creator>Krest, Courtney M</creator><creator>Onderko, Elizabeth L</creator><creator>Langston, Matthew C</creator><creator>Green, Michael T</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>7X8</scope></search><sort><creationdate>20140625</creationdate><title>Setting an Upper Limit on the Myoglobin Iron(IV)Hydroxide pK a: Insight into Axial Ligand Tuning in Heme Protein Catalysis</title><author>Yosca, Timothy H ; Behan, Rachel K ; Krest, Courtney M ; Onderko, Elizabeth L ; Langston, Matthew C ; Green, Michael T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a171t-788fbaf2f9613fa312f5274525ce3d71b0dd27bd76273c055569a3ff4eb1c59b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Catalysis</topic><topic>Catalytic Domain</topic><topic>Histidine - chemistry</topic><topic>Hydrogen-Ion Concentration</topic><topic>Hydroxides - chemistry</topic><topic>Iron - chemistry</topic><topic>Ligands</topic><topic>Molecular Structure</topic><topic>Myoglobin - chemistry</topic><topic>Spectroscopy, Mossbauer</topic><topic>Spectrum Analysis, Raman</topic><topic>X-Ray Absorption Spectroscopy</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yosca, Timothy H</creatorcontrib><creatorcontrib>Behan, Rachel K</creatorcontrib><creatorcontrib>Krest, Courtney M</creatorcontrib><creatorcontrib>Onderko, Elizabeth L</creatorcontrib><creatorcontrib>Langston, Matthew C</creatorcontrib><creatorcontrib>Green, Michael T</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>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yosca, Timothy H</au><au>Behan, Rachel K</au><au>Krest, Courtney M</au><au>Onderko, Elizabeth L</au><au>Langston, Matthew C</au><au>Green, Michael T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Setting an Upper Limit on the Myoglobin Iron(IV)Hydroxide pK a: Insight into Axial Ligand Tuning in Heme Protein Catalysis</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2014-06-25</date><risdate>2014</risdate><volume>136</volume><issue>25</issue><spage>9124</spage><epage>9131</epage><pages>9124-9131</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><abstract>To provide insight into the iron(IV)hydroxide pK a of histidine ligated heme proteins, we have probed the active site of myoglobin compound II over the pH range of 3.9–9.5, using EXAFS, Mössbauer, and resonance Raman spectroscopies. We find no indication of ferryl protonation over this pH range, allowing us to set an upper limit of 2.7 on the iron(IV)hydroxide pK a in myoglobin. Together with the recent determination of an iron(IV)hydroxide pK a ∼ 12 in the thiolate-ligated heme enzyme cytochrome P450, this result provides insight into Nature’s ability to tune catalytic function through its choice of axial ligand.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>24875119</pmid><doi>10.1021/ja503588n</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0002-7863 |
| ispartof | Journal of the American Chemical Society, 2014-06, Vol.136 (25), p.9124-9131 |
| issn | 0002-7863 1520-5126 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1540704435 |
| source | MEDLINE; American Chemical Society Journals |
| subjects | Catalysis Catalytic Domain Histidine - chemistry Hydrogen-Ion Concentration Hydroxides - chemistry Iron - chemistry Ligands Molecular Structure Myoglobin - chemistry Spectroscopy, Mossbauer Spectrum Analysis, Raman X-Ray Absorption Spectroscopy |
| title | Setting an Upper Limit on the Myoglobin Iron(IV)Hydroxide pK a: Insight into Axial Ligand Tuning in Heme Protein Catalysis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-03T07%3A05%3A55IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Setting%20an%20Upper%20Limit%20on%20the%20Myoglobin%20Iron(IV)Hydroxide%20pK%20a:%20Insight%20into%20Axial%20Ligand%20Tuning%20in%20Heme%20Protein%20Catalysis&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.au=Yosca,%20Timothy%20H&rft.date=2014-06-25&rft.volume=136&rft.issue=25&rft.spage=9124&rft.epage=9131&rft.pages=9124-9131&rft.issn=0002-7863&rft.eissn=1520-5126&rft_id=info:doi/10.1021/ja503588n&rft_dat=%3Cproquest_pubme%3E1540704435%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1540704435&rft_id=info:pmid/24875119&rfr_iscdi=true |