Long-Range Reactive Dynamics in Myoglobin
We report the complete vibrational spectrum of the probe nucleus {sup 57}Fe 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 pol...
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| Veröffentlicht in: | Physical review letters 2001-05, Vol.86 (21) |
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| container_title | Physical review letters |
| container_volume | 86 |
| creator | Sage, J. Timothy Durbin, Stephen M. Sturhahn, Wolfgang Wharton, David C. Champion, Paul M. Hession, Philip Sutter, John Alp, E. Ercan |
| description | We report the complete vibrational spectrum of the probe nucleus {sup 57}Fe 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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Timothy ; Durbin, Stephen M. ; Sturhahn, Wolfgang ; Wharton, David C. ; Champion, Paul M. ; Hession, Philip ; Sutter, John ; Alp, E. Ercan</creatorcontrib><description>We report the complete vibrational spectrum of the probe nucleus {sup 57}Fe 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><identifier>ISSN: 0031-9007</identifier><identifier>EISSN: 1079-7114</identifier><identifier>DOI: 10.1103/PhysRevLett.86.4966</identifier><language>eng</language><publisher>United States: The American Physical Society</publisher><subject>BASIC BIOLOGICAL SCIENCES ; HEME ; INTERACTION RANGE ; MYOGLOBIN ; NITROGEN ; OSCILLATIONS ; OXYGEN ; PROBES ; PROTEINS</subject><ispartof>Physical review letters, 2001-05, Vol.86 (21)</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.osti.gov/biblio/40205854$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Sage, J. Timothy</creatorcontrib><creatorcontrib>Durbin, Stephen M.</creatorcontrib><creatorcontrib>Sturhahn, Wolfgang</creatorcontrib><creatorcontrib>Wharton, David C.</creatorcontrib><creatorcontrib>Champion, Paul M.</creatorcontrib><creatorcontrib>Hession, Philip</creatorcontrib><creatorcontrib>Sutter, John</creatorcontrib><creatorcontrib>Alp, E. Ercan</creatorcontrib><title>Long-Range Reactive Dynamics in Myoglobin</title><title>Physical review letters</title><description>We report the complete vibrational spectrum of the probe nucleus {sup 57}Fe 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>BASIC BIOLOGICAL SCIENCES</subject><subject>HEME</subject><subject>INTERACTION RANGE</subject><subject>MYOGLOBIN</subject><subject>NITROGEN</subject><subject>OSCILLATIONS</subject><subject>OXYGEN</subject><subject>PROBES</subject><subject>PROTEINS</subject><issn>0031-9007</issn><issn>1079-7114</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><recordid>eNqNyrsKwjAUANCLKFgfX-AScHJovbdN03b2gUMFKe4lhthGajIkCP17Fz_A6SwHYEOYEGG2v_Wjb_Sn1iEkpUh4JcQEIsKiigsiPoUIMaO4QizmsPD-hYiUijKCXe1sFzfSdpo1WqpgPpodRyvfRnlmLLuOrhvcw9gVzJ5y8Hr9cwnb8-l-uMTOB9N6ZYJWvXLWahVajinmZc6z_9YXGVo5Vg</recordid><startdate>20010521</startdate><enddate>20010521</enddate><creator>Sage, J. 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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>The American Physical Society</pub><doi>10.1103/PhysRevLett.86.4966</doi></addata></record> |
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| ispartof | Physical review letters, 2001-05, Vol.86 (21) |
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| source | American Physical Society Journals |
| subjects | BASIC BIOLOGICAL SCIENCES HEME INTERACTION RANGE MYOGLOBIN NITROGEN OSCILLATIONS OXYGEN PROBES PROTEINS |
| title | Long-Range Reactive Dynamics in Myoglobin |
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