Comparison of Calculated and Experimentally Resolved Rate Constants for Excitation Energy Transfer in C-Phycocyanin. 1. Monomers
Rate constants for excitation energy transfer in light-harvesting protein, C-phycocyanin (PC), in the monomeric aggregation state, isolated from the cyanobacterium cynechococcus sp. PCC 7002, are calculated, using Foerster theory and compared with the results of time-resolved fluorescence measuremen...
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| Veröffentlicht in: | Journal of Physical Chemistry 1995-05, Vol.99 (20), p.8412-8419 |
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| container_title | Journal of Physical Chemistry |
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| creator | Debreczeny, Martin P Sauer, Kenneth Zhou, Jianhui Bryant, Donald A |
| description | Rate constants for excitation energy transfer in light-harvesting protein, C-phycocyanin (PC), in the monomeric aggregation state, isolated from the cyanobacterium cynechococcus sp. PCC 7002, are calculated, using Foerster theory and compared with the results of time-resolved fluorescence measurements. The assignments of the energy-transfer rate constants in PC monomers are confirmed here by time-resolved fluorescence anisotropy measurements of the PC monomers isolated from both the wild-type and a mutant strain (cpcB/C155S) whose PC is missing the {beta}{sub 155} chromophore. It is concluded that the Foerster model of resonant energy transfer in the weak coupling limit successfully describes the dominant energy-transfer processes in this protein in the monomeric state. 31 refs., 3 figs., 4 tabs. |
| doi_str_mv | 10.1021/j100020a080 |
| format | Article |
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Monomers</title><source>ACS Publications</source><creator>Debreczeny, Martin P ; Sauer, Kenneth ; Zhou, Jianhui ; Bryant, Donald A</creator><creatorcontrib>Debreczeny, Martin P ; Sauer, Kenneth ; Zhou, Jianhui ; Bryant, Donald A</creatorcontrib><description>Rate constants for excitation energy transfer in light-harvesting protein, C-phycocyanin (PC), in the monomeric aggregation state, isolated from the cyanobacterium cynechococcus sp. PCC 7002, are calculated, using Foerster theory and compared with the results of time-resolved fluorescence measurements. The assignments of the energy-transfer rate constants in PC monomers are confirmed here by time-resolved fluorescence anisotropy measurements of the PC monomers isolated from both the wild-type and a mutant strain (cpcB/C155S) whose PC is missing the {beta}{sub 155} chromophore. It is concluded that the Foerster model of resonant energy transfer in the weak coupling limit successfully describes the dominant energy-transfer processes in this protein in the monomeric state. 31 refs., 3 figs., 4 tabs.</description><identifier>ISSN: 0022-3654</identifier><identifier>EISSN: 1541-5740</identifier><identifier>DOI: 10.1021/j100020a080</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>40 CHEMISTRY ; BIOLOGY AND MEDICINE, BASIC STUDIES ; COMPILED DATA ; ENERGY TRANSFER ; EXCITATION ; FLUORESCENCE ; MONOMERS ; PHOTOSYNTHESIS ; PROTEINS ; TIME RESOLUTION</subject><ispartof>Journal of Physical Chemistry, 1995-05, Vol.99 (20), p.8412-8419</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a392t-56f9ce261163a80b082fe8e6176ad0930419497afd87be160affa13a528ae9173</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/j100020a080$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/j100020a080$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,885,2764,27075,27923,27924,56737,56787</link.rule.ids><backlink>$$Uhttps://www.osti.gov/biblio/62306$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Debreczeny, Martin P</creatorcontrib><creatorcontrib>Sauer, Kenneth</creatorcontrib><creatorcontrib>Zhou, Jianhui</creatorcontrib><creatorcontrib>Bryant, Donald A</creatorcontrib><title>Comparison of Calculated and Experimentally Resolved Rate Constants for Excitation Energy Transfer in C-Phycocyanin. 1. Monomers</title><title>Journal of Physical Chemistry</title><addtitle>J. Phys. Chem</addtitle><description>Rate constants for excitation energy transfer in light-harvesting protein, C-phycocyanin (PC), in the monomeric aggregation state, isolated from the cyanobacterium cynechococcus sp. PCC 7002, are calculated, using Foerster theory and compared with the results of time-resolved fluorescence measurements. The assignments of the energy-transfer rate constants in PC monomers are confirmed here by time-resolved fluorescence anisotropy measurements of the PC monomers isolated from both the wild-type and a mutant strain (cpcB/C155S) whose PC is missing the {beta}{sub 155} chromophore. It is concluded that the Foerster model of resonant energy transfer in the weak coupling limit successfully describes the dominant energy-transfer processes in this protein in the monomeric state. 31 refs., 3 figs., 4 tabs.</description><subject>40 CHEMISTRY</subject><subject>BIOLOGY AND MEDICINE, BASIC STUDIES</subject><subject>COMPILED DATA</subject><subject>ENERGY TRANSFER</subject><subject>EXCITATION</subject><subject>FLUORESCENCE</subject><subject>MONOMERS</subject><subject>PHOTOSYNTHESIS</subject><subject>PROTEINS</subject><subject>TIME RESOLUTION</subject><issn>0022-3654</issn><issn>1541-5740</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNpt0E1v2zAMBmBh6IClXU_7A7rtUDgTLVu2j4ORfgxdG6TpWWAVanXmSIGkFvWtP30aMgw99CSAeviCJGNfQMxBlPBtC0KIUqBoxQc2g7qCom4qccRmuVwWUtXVJ3Yc4zYzkBJm7LX3uz2GIXrHveU9juZpxEQbjm7DFy97CsOOXMJxnPiKoh-f898qC957FxO6FLn1IVMzJExDzlk4Cr8mvg7ooqXAB8f7Yvk4GW8mdIObc5jzn975HYX4mX20OEY6_feesPvzxbq_LK5vL67679cFyq5MRa1sZ6hUAEpiKx5EW1pqSUGjcCM6KSroqq5Bu2mbBwIl0FoEiXXZInXQyBPGD7k-pkHHPCyZR-OdI5O0KqVQmZwdiAk-xkBW7_PyGCYNQv-9r35z36yLgx5iopf_FMNvrRrZ1Hq9vMtdVd2r_kb_yP7rwaOJeuufgsvrvpv8B6SCiMk</recordid><startdate>199505</startdate><enddate>199505</enddate><creator>Debreczeny, Martin P</creator><creator>Sauer, Kenneth</creator><creator>Zhou, Jianhui</creator><creator>Bryant, Donald A</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>OTOTI</scope></search><sort><creationdate>199505</creationdate><title>Comparison of Calculated and Experimentally Resolved Rate Constants for Excitation Energy Transfer in C-Phycocyanin. 1. 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Monomers</atitle><jtitle>Journal of Physical Chemistry</jtitle><addtitle>J. Phys. Chem</addtitle><date>1995-05</date><risdate>1995</risdate><volume>99</volume><issue>20</issue><spage>8412</spage><epage>8419</epage><pages>8412-8419</pages><issn>0022-3654</issn><eissn>1541-5740</eissn><abstract>Rate constants for excitation energy transfer in light-harvesting protein, C-phycocyanin (PC), in the monomeric aggregation state, isolated from the cyanobacterium cynechococcus sp. PCC 7002, are calculated, using Foerster theory and compared with the results of time-resolved fluorescence measurements. The assignments of the energy-transfer rate constants in PC monomers are confirmed here by time-resolved fluorescence anisotropy measurements of the PC monomers isolated from both the wild-type and a mutant strain (cpcB/C155S) whose PC is missing the {beta}{sub 155} chromophore. It is concluded that the Foerster model of resonant energy transfer in the weak coupling limit successfully describes the dominant energy-transfer processes in this protein in the monomeric state. 31 refs., 3 figs., 4 tabs.</abstract><cop>United States</cop><pub>American Chemical Society</pub><doi>10.1021/j100020a080</doi><tpages>8</tpages></addata></record> |
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| subjects | 40 CHEMISTRY BIOLOGY AND MEDICINE, BASIC STUDIES COMPILED DATA ENERGY TRANSFER EXCITATION FLUORESCENCE MONOMERS PHOTOSYNTHESIS PROTEINS TIME RESOLUTION |
| title | Comparison of Calculated and Experimentally Resolved Rate Constants for Excitation Energy Transfer in C-Phycocyanin. 1. Monomers |
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