Putative Hydrogen Bond to Tyrosine M208 in Photosynthetic Reaction Centers from Rhodobacter capsulatus Significantly Slows Primary Charge Separation
Slow, ∼50 ps, P* → P+HA – electron transfer is observed in Rhodobacter capsulatus reaction centers (RCs) bearing the native Tyr residue at M208 and the single amino acid change of isoleucine at M204 to glutamic acid. The P* decay kinetics are unusually homogeneous (single exponential) at room temper...
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| Veröffentlicht in: | The journal of physical chemistry. B 2014-06, Vol.118 (24), p.6721-6732 |
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| container_title | The journal of physical chemistry. B |
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| creator | Saggu, Miguel Carter, Brett Zhou, Xiaoxue Faries, Kaitlyn Cegelski, Lynette Holten, Dewey Boxer, Steven G Kirmaier, Christine |
| description | Slow, ∼50 ps, P* → P+HA – electron transfer is observed in Rhodobacter capsulatus reaction centers (RCs) bearing the native Tyr residue at M208 and the single amino acid change of isoleucine at M204 to glutamic acid. The P* decay kinetics are unusually homogeneous (single exponential) at room temperature. Comparative solid-state NMR of [4′-13C]Tyr labeled wild-type and M204E RCs show that the chemical shift of Tyr M208 is significantly altered in the M204E mutant and in a manner consistent with formation of a hydrogen bond to the Tyr M208 hydroxyl group. Models based on RC crystal structure coordinates indicate that if such a hydrogen bond is formed between the Glu at M204 and the M208 Tyr hydroxyl group, the −OH would be oriented in a fashion expected (based on the calculations by Alden et al., J. Phys. Chem. 1996, 100, 16761–16770) to destabilize P+BA – in free energy. Alteration of the environment of Tyr M208 and BA by Glu M204 via this putative hydrogen bond has a powerful influence on primary charge separation. |
| doi_str_mv | 10.1021/jp503422c |
| format | Article |
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The P* decay kinetics are unusually homogeneous (single exponential) at room temperature. Comparative solid-state NMR of [4′-13C]Tyr labeled wild-type and M204E RCs show that the chemical shift of Tyr M208 is significantly altered in the M204E mutant and in a manner consistent with formation of a hydrogen bond to the Tyr M208 hydroxyl group. Models based on RC crystal structure coordinates indicate that if such a hydrogen bond is formed between the Glu at M204 and the M208 Tyr hydroxyl group, the −OH would be oriented in a fashion expected (based on the calculations by Alden et al., J. Phys. Chem. 1996, 100, 16761–16770) to destabilize P+BA – in free energy. Alteration of the environment of Tyr M208 and BA by Glu M204 via this putative hydrogen bond has a powerful influence on primary charge separation.</description><identifier>ISSN: 1520-6106</identifier><identifier>ISSN: 1520-5207</identifier><identifier>EISSN: 1520-5207</identifier><identifier>DOI: 10.1021/jp503422c</identifier><identifier>PMID: 24902471</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>ambient temperature ; Amino Acid Substitution ; Amino acids ; Carbon Isotopes - chemistry ; Charge ; crystal structure ; Electron transfer ; Gibbs free energy ; glutamic acid ; Hydrogen Bonding ; Hydrogen bonds ; Hydroxyl groups ; isoleucine ; Kinetics ; Mathematical models ; mutants ; nuclear magnetic resonance spectroscopy ; Nuclear Magnetic Resonance, Biomolecular ; Photosynthetic Reaction Center Complex Proteins - chemistry ; Photosynthetic Reaction Center Complex Proteins - metabolism ; photosynthetic reaction centers ; Rhodobacter capsulatus ; Rhodobacter capsulatus - metabolism ; Separation ; Temperature ; Tyrosine ; Tyrosine - chemistry</subject><ispartof>The journal of physical chemistry. 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B</title><addtitle>J. Phys. Chem. B</addtitle><description>Slow, ∼50 ps, P* → P+HA – electron transfer is observed in Rhodobacter capsulatus reaction centers (RCs) bearing the native Tyr residue at M208 and the single amino acid change of isoleucine at M204 to glutamic acid. The P* decay kinetics are unusually homogeneous (single exponential) at room temperature. Comparative solid-state NMR of [4′-13C]Tyr labeled wild-type and M204E RCs show that the chemical shift of Tyr M208 is significantly altered in the M204E mutant and in a manner consistent with formation of a hydrogen bond to the Tyr M208 hydroxyl group. Models based on RC crystal structure coordinates indicate that if such a hydrogen bond is formed between the Glu at M204 and the M208 Tyr hydroxyl group, the −OH would be oriented in a fashion expected (based on the calculations by Alden et al., J. Phys. Chem. 1996, 100, 16761–16770) to destabilize P+BA – in free energy. Alteration of the environment of Tyr M208 and BA by Glu M204 via this putative hydrogen bond has a powerful influence on primary charge separation.</description><subject>ambient temperature</subject><subject>Amino Acid Substitution</subject><subject>Amino acids</subject><subject>Carbon Isotopes - chemistry</subject><subject>Charge</subject><subject>crystal structure</subject><subject>Electron transfer</subject><subject>Gibbs free energy</subject><subject>glutamic acid</subject><subject>Hydrogen Bonding</subject><subject>Hydrogen bonds</subject><subject>Hydroxyl groups</subject><subject>isoleucine</subject><subject>Kinetics</subject><subject>Mathematical models</subject><subject>mutants</subject><subject>nuclear magnetic resonance spectroscopy</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Photosynthetic Reaction Center Complex Proteins - chemistry</subject><subject>Photosynthetic Reaction Center Complex Proteins - metabolism</subject><subject>photosynthetic reaction centers</subject><subject>Rhodobacter capsulatus</subject><subject>Rhodobacter capsulatus - metabolism</subject><subject>Separation</subject><subject>Temperature</subject><subject>Tyrosine</subject><subject>Tyrosine - chemistry</subject><issn>1520-6106</issn><issn>1520-5207</issn><issn>1520-5207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>N~.</sourceid><sourceid>EIF</sourceid><recordid>eNqFkt-K1DAUxoso7h-98AUkN4J7MXqSpml7I-igrrDisLNelzQ9mWboJDVJV_oePrAZZhwUhL0ICZwfX853zpdlLyi8ocDo2-1YQM4ZU4-yc1owWKRTPj6-BQVxll2EsAVgBavE0-yM8RoYL-l59ms1RRnNPZLrufNug5Z8cLYj0ZG72btgLJKvDCpiLFn1Lrow29hjNIrcolTROEuWaCP6QLR3O3Lbu861qYKeKDmGaZBxCmRtNtZoo6SNw0zWg_sZyMqbnfQzWfbSb5CscZRe7hWfZU-0HAI-P96X2fdPH--W14ubb5-_LN_fLGQBPC7qSmsFHS2FVh0XUEqpOedFXrZYcqZqqFrOBQdI46GQ19iixrxq25xpUVf5ZfbuoDtO7Q47lXx4OTTjoa_GSdP8W7GmbzbuvuEguKh5Enh9FPDux4QhNjsTFA6DtOim0DDY_11Wdf4gmlwwKNLC4GG0KKhgVOR71asDqtKugkd9ap5Cs89Gc8pGYl_-7fZE_glDAl4dAKlCs3WTt2n4_xH6DaQ2wpM</recordid><startdate>20140619</startdate><enddate>20140619</enddate><creator>Saggu, Miguel</creator><creator>Carter, Brett</creator><creator>Zhou, Xiaoxue</creator><creator>Faries, Kaitlyn</creator><creator>Cegelski, Lynette</creator><creator>Holten, Dewey</creator><creator>Boxer, Steven G</creator><creator>Kirmaier, Christine</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>7QL</scope><scope>C1K</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20140619</creationdate><title>Putative Hydrogen Bond to Tyrosine M208 in Photosynthetic Reaction Centers from Rhodobacter capsulatus Significantly Slows Primary Charge Separation</title><author>Saggu, Miguel ; Carter, Brett ; Zhou, Xiaoxue ; Faries, Kaitlyn ; Cegelski, Lynette ; Holten, Dewey ; Boxer, Steven G ; Kirmaier, Christine</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a504t-98ffc0d176fcd4607aaf444537be742c908b4464005031039ebefe38bb32f6983</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>ambient temperature</topic><topic>Amino Acid Substitution</topic><topic>Amino acids</topic><topic>Carbon Isotopes - chemistry</topic><topic>Charge</topic><topic>crystal structure</topic><topic>Electron transfer</topic><topic>Gibbs free energy</topic><topic>glutamic acid</topic><topic>Hydrogen Bonding</topic><topic>Hydrogen bonds</topic><topic>Hydroxyl groups</topic><topic>isoleucine</topic><topic>Kinetics</topic><topic>Mathematical models</topic><topic>mutants</topic><topic>nuclear magnetic resonance spectroscopy</topic><topic>Nuclear Magnetic Resonance, Biomolecular</topic><topic>Photosynthetic Reaction Center Complex Proteins - chemistry</topic><topic>Photosynthetic Reaction Center Complex Proteins - metabolism</topic><topic>photosynthetic reaction centers</topic><topic>Rhodobacter capsulatus</topic><topic>Rhodobacter capsulatus - metabolism</topic><topic>Separation</topic><topic>Temperature</topic><topic>Tyrosine</topic><topic>Tyrosine - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Saggu, Miguel</creatorcontrib><creatorcontrib>Carter, Brett</creatorcontrib><creatorcontrib>Zhou, Xiaoxue</creatorcontrib><creatorcontrib>Faries, Kaitlyn</creatorcontrib><creatorcontrib>Cegelski, Lynette</creatorcontrib><creatorcontrib>Holten, Dewey</creatorcontrib><creatorcontrib>Boxer, Steven G</creatorcontrib><creatorcontrib>Kirmaier, Christine</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The journal of physical chemistry. B</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Saggu, Miguel</au><au>Carter, Brett</au><au>Zhou, Xiaoxue</au><au>Faries, Kaitlyn</au><au>Cegelski, Lynette</au><au>Holten, Dewey</au><au>Boxer, Steven G</au><au>Kirmaier, Christine</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Putative Hydrogen Bond to Tyrosine M208 in Photosynthetic Reaction Centers from Rhodobacter capsulatus Significantly Slows Primary Charge Separation</atitle><jtitle>The journal of physical chemistry. B</jtitle><addtitle>J. Phys. Chem. B</addtitle><date>2014-06-19</date><risdate>2014</risdate><volume>118</volume><issue>24</issue><spage>6721</spage><epage>6732</epage><pages>6721-6732</pages><issn>1520-6106</issn><issn>1520-5207</issn><eissn>1520-5207</eissn><abstract>Slow, ∼50 ps, P* → P+HA – electron transfer is observed in Rhodobacter capsulatus reaction centers (RCs) bearing the native Tyr residue at M208 and the single amino acid change of isoleucine at M204 to glutamic acid. The P* decay kinetics are unusually homogeneous (single exponential) at room temperature. Comparative solid-state NMR of [4′-13C]Tyr labeled wild-type and M204E RCs show that the chemical shift of Tyr M208 is significantly altered in the M204E mutant and in a manner consistent with formation of a hydrogen bond to the Tyr M208 hydroxyl group. Models based on RC crystal structure coordinates indicate that if such a hydrogen bond is formed between the Glu at M204 and the M208 Tyr hydroxyl group, the −OH would be oriented in a fashion expected (based on the calculations by Alden et al., J. Phys. Chem. 1996, 100, 16761–16770) to destabilize P+BA – in free energy. Alteration of the environment of Tyr M208 and BA by Glu M204 via this putative hydrogen bond has a powerful influence on primary charge separation.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>24902471</pmid><doi>10.1021/jp503422c</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; ACS Publications |
| subjects | ambient temperature Amino Acid Substitution Amino acids Carbon Isotopes - chemistry Charge crystal structure Electron transfer Gibbs free energy glutamic acid Hydrogen Bonding Hydrogen bonds Hydroxyl groups isoleucine Kinetics Mathematical models mutants nuclear magnetic resonance spectroscopy Nuclear Magnetic Resonance, Biomolecular Photosynthetic Reaction Center Complex Proteins - chemistry Photosynthetic Reaction Center Complex Proteins - metabolism photosynthetic reaction centers Rhodobacter capsulatus Rhodobacter capsulatus - metabolism Separation Temperature Tyrosine Tyrosine - chemistry |
| title | Putative Hydrogen Bond to Tyrosine M208 in Photosynthetic Reaction Centers from Rhodobacter capsulatus Significantly Slows Primary Charge Separation |
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