Long-range reactive dynamics in myoglobin
We report the complete vibrational spectrum of the probe nucleus 57Fe at the oxygen-binding site of the protein myoglobin. The Fe-pyrrole nitrogen stretching modes of the heme group, identified here, probe asymmetric interactions with the protein environment. Collective oscillations of the polypepti...
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| Veröffentlicht in: | Physical review letters 2001-05, Vol.86 (21), p.4966-4969 |
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| container_end_page | 4969 |
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| container_issue | 21 |
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| container_title | Physical review letters |
| container_volume | 86 |
| creator | Sage, J T Durbin, S M Sturhahn, W Wharton, D C Champion, P M Hession, P Sutter, J Alp, E E |
| description | We report the complete vibrational spectrum of the probe nucleus 57Fe at the oxygen-binding site of the protein myoglobin. The Fe-pyrrole nitrogen stretching modes of the heme group, identified here, probe asymmetric interactions with the protein environment. Collective oscillations of the polypeptide, rather than localized heme vibrations, dominate the low frequency region. We conclude that the heme "doming" mode is significantly delocalized, so that distant sites respond to oxygen binding on vibrational time scales. This has ramifications for understanding long-range interactions in biomolecules, such as those that mediate cooperativity in allosteric proteins. |
| doi_str_mv | 10.1103/PhysRevLett.86.4966 |
| format | Article |
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This has ramifications for understanding long-range interactions in biomolecules, such as those that mediate cooperativity in allosteric proteins.</description><identifier>ISSN: 0031-9007</identifier><identifier>EISSN: 1079-7114</identifier><identifier>DOI: 10.1103/PhysRevLett.86.4966</identifier><identifier>PMID: 11384393</identifier><language>eng</language><publisher>United States: American Physical Society (APS)</publisher><subject>advanced photon source ; Animals ; BASIC BIOLOGICAL SCIENCES ; Binding Sites ; GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE ; HEME ; Horses ; INTERACTION RANGE ; Iron Isotopes - chemistry ; MYOGLOBIN ; Myoglobin - chemistry ; Myoglobin - metabolism ; NITROGEN ; OSCILLATIONS ; OXYGEN ; PROTEINS ; Spectrum Analysis ; Thermodynamics</subject><ispartof>Physical review letters, 2001-05, Vol.86 (21), p.4966-4969</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c329t-10b91bb61539f8094b6cdd3bb3620d2a10734e2e73c7a2503fb07349f9401f1e3</citedby><cites>FETCH-LOGICAL-c329t-10b91bb61539f8094b6cdd3bb3620d2a10734e2e73c7a2503fb07349f9401f1e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,2876,2877,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11384393$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/15003700$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Sage, J T</creatorcontrib><creatorcontrib>Durbin, S M</creatorcontrib><creatorcontrib>Sturhahn, W</creatorcontrib><creatorcontrib>Wharton, D C</creatorcontrib><creatorcontrib>Champion, P M</creatorcontrib><creatorcontrib>Hession, P</creatorcontrib><creatorcontrib>Sutter, J</creatorcontrib><creatorcontrib>Alp, E E</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><creatorcontrib>Northeastern Univ</creatorcontrib><creatorcontrib>Purdue Univ</creatorcontrib><title>Long-range reactive dynamics in myoglobin</title><title>Physical review letters</title><addtitle>Phys Rev Lett</addtitle><description>We report the complete vibrational spectrum of the probe nucleus 57Fe at the oxygen-binding site of the protein myoglobin. The Fe-pyrrole nitrogen stretching modes of the heme group, identified here, probe asymmetric interactions with the protein environment. Collective oscillations of the polypeptide, rather than localized heme vibrations, dominate the low frequency region. We conclude that the heme "doming" mode is significantly delocalized, so that distant sites respond to oxygen binding on vibrational time scales. This has ramifications for understanding long-range interactions in biomolecules, such as those that mediate cooperativity in allosteric proteins.</description><subject>advanced photon source</subject><subject>Animals</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Binding Sites</subject><subject>GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE</subject><subject>HEME</subject><subject>Horses</subject><subject>INTERACTION RANGE</subject><subject>Iron Isotopes - chemistry</subject><subject>MYOGLOBIN</subject><subject>Myoglobin - chemistry</subject><subject>Myoglobin - metabolism</subject><subject>NITROGEN</subject><subject>OSCILLATIONS</subject><subject>OXYGEN</subject><subject>PROTEINS</subject><subject>Spectrum Analysis</subject><subject>Thermodynamics</subject><issn>0031-9007</issn><issn>1079-7114</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpNkF9LwzAUxYMobk4_gSAFQfCh896kS5tHGf6DgiL6HJI03SJtqk026Le3YwN9uFy4nHO450fIJcIcEdjd23oI73Zb2hjnBZ9ngvMjMkXIRZojZsdkCsAwFQD5hJyF8AUASHlxSiaIrMiYYFNyW3Z-lfbKr2zSW2Wi29qkGrxqnQmJ80k7dKum086fk5NaNcFeHPaMfD4-fCyf0_L16WV5X6aGURFTBC1Qa44LJuoCRKa5qSqmNeMUKqrG_1hmqc2ZyRVdAKv17iJqkQHWaNmMXO9zuxCdDMZFa9am896aKHExdsrHmZGbveq77342NkTZumBs0yhvu02QORSioJSPQrYXmr4Lobe1_O5dq_pBIsgdR_mPoyy43HEcXVeH-I1ubfXnOYBjvxuXbxg</recordid><startdate>20010521</startdate><enddate>20010521</enddate><creator>Sage, J T</creator><creator>Durbin, S M</creator><creator>Sturhahn, W</creator><creator>Wharton, D C</creator><creator>Champion, P M</creator><creator>Hession, P</creator><creator>Sutter, J</creator><creator>Alp, E E</creator><general>American Physical Society (APS)</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><scope>OTOTI</scope></search><sort><creationdate>20010521</creationdate><title>Long-range reactive dynamics in myoglobin</title><author>Sage, J T ; Durbin, S M ; Sturhahn, W ; Wharton, D C ; Champion, P M ; Hession, P ; Sutter, J ; Alp, E E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c329t-10b91bb61539f8094b6cdd3bb3620d2a10734e2e73c7a2503fb07349f9401f1e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>advanced photon source</topic><topic>Animals</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>Binding Sites</topic><topic>GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE</topic><topic>HEME</topic><topic>Horses</topic><topic>INTERACTION RANGE</topic><topic>Iron Isotopes - chemistry</topic><topic>MYOGLOBIN</topic><topic>Myoglobin - chemistry</topic><topic>Myoglobin - metabolism</topic><topic>NITROGEN</topic><topic>OSCILLATIONS</topic><topic>OXYGEN</topic><topic>PROTEINS</topic><topic>Spectrum Analysis</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sage, J T</creatorcontrib><creatorcontrib>Durbin, S M</creatorcontrib><creatorcontrib>Sturhahn, W</creatorcontrib><creatorcontrib>Wharton, D C</creatorcontrib><creatorcontrib>Champion, P M</creatorcontrib><creatorcontrib>Hession, P</creatorcontrib><creatorcontrib>Sutter, J</creatorcontrib><creatorcontrib>Alp, E E</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><creatorcontrib>Northeastern Univ</creatorcontrib><creatorcontrib>Purdue Univ</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><collection>OSTI.GOV</collection><jtitle>Physical review letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sage, J T</au><au>Durbin, S M</au><au>Sturhahn, W</au><au>Wharton, D C</au><au>Champion, P M</au><au>Hession, P</au><au>Sutter, J</au><au>Alp, E E</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><aucorp>Northeastern Univ</aucorp><aucorp>Purdue Univ</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Long-range reactive dynamics in myoglobin</atitle><jtitle>Physical review letters</jtitle><addtitle>Phys Rev Lett</addtitle><date>2001-05-21</date><risdate>2001</risdate><volume>86</volume><issue>21</issue><spage>4966</spage><epage>4969</epage><pages>4966-4969</pages><issn>0031-9007</issn><eissn>1079-7114</eissn><abstract>We report the complete vibrational spectrum of the probe nucleus 57Fe at the oxygen-binding site of the protein myoglobin. The Fe-pyrrole nitrogen stretching modes of the heme group, identified here, probe asymmetric interactions with the protein environment. Collective oscillations of the polypeptide, rather than localized heme vibrations, dominate the low frequency region. We conclude that the heme "doming" mode is significantly delocalized, so that distant sites respond to oxygen binding on vibrational time scales. This has ramifications for understanding long-range interactions in biomolecules, such as those that mediate cooperativity in allosteric proteins.</abstract><cop>United States</cop><pub>American Physical Society (APS)</pub><pmid>11384393</pmid><doi>10.1103/PhysRevLett.86.4966</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Physical review letters, 2001-05, Vol.86 (21), p.4966-4969 |
| issn | 0031-9007 1079-7114 |
| language | eng |
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| source | MEDLINE; American Physical Society Journals |
| subjects | advanced photon source Animals BASIC BIOLOGICAL SCIENCES Binding Sites GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE HEME Horses INTERACTION RANGE Iron Isotopes - chemistry MYOGLOBIN Myoglobin - chemistry Myoglobin - metabolism NITROGEN OSCILLATIONS OXYGEN PROTEINS Spectrum Analysis Thermodynamics |
| title | Long-range reactive dynamics in myoglobin |
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