Comparison of Intra- vs Intermolecular Long-Range Electron Transfer in Crystals of Ruthenium-Modified Azurin
Selective metal-ion incorporation and ligand substitution are employed to control whether electrons tunnel over intra- or intermolecular separations in crystals of P. aeruginosa azurin modified with Ru−polypyridine complexes. Cu1+-to-Ru3+ electron transfer (ET) across a specific protein−protein inte...
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| Veröffentlicht in: | The journal of physical chemistry. B 2006-10, Vol.110 (41), p.20073-20076 |
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| container_end_page | 20076 |
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| container_issue | 41 |
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| container_title | The journal of physical chemistry. B |
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| creator | Grǎdinaru, Cristian Crane, Brian R |
| description | Selective metal-ion incorporation and ligand substitution are employed to control whether electrons tunnel over intra- or intermolecular separations in crystals of P. aeruginosa azurin modified with Ru−polypyridine complexes. Cu1+-to-Ru3+ electron transfer (ET) across a specific protein−protein interface in the crystal lattice has a time constant 5−10 times longer than ET between the same donor and acceptor within a single protein (τET = 5 vs 0.5−1.0 μs). Slower intermolecular ET agrees well with a longer distance between redox centers across the inter-protein (18.9 Å) compared to the intra-protein separation (17.0 Å) and indicates that the closest donor/acceptor pair dominates crystal ET. Lowering the crystal pH accelerates inter-protein ET (τET = 1.0 μs) but not intra-protein ET. Faster inter-protein ET likely results from a pH-induced peptide bond flip that perturbs hydrogen bonding in the path between Ru and Cu centers on adjacent molecules. |
| doi_str_mv | 10.1021/jp0644309 |
| format | Article |
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Cu1+-to-Ru3+ electron transfer (ET) across a specific protein−protein interface in the crystal lattice has a time constant 5−10 times longer than ET between the same donor and acceptor within a single protein (τET = 5 vs 0.5−1.0 μs). Slower intermolecular ET agrees well with a longer distance between redox centers across the inter-protein (18.9 Å) compared to the intra-protein separation (17.0 Å) and indicates that the closest donor/acceptor pair dominates crystal ET. Lowering the crystal pH accelerates inter-protein ET (τET = 1.0 μs) but not intra-protein ET. 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Faster inter-protein ET likely results from a pH-induced peptide bond flip that perturbs hydrogen bonding in the path between Ru and Cu centers on adjacent molecules.</description><subject>Azurin - chemistry</subject><subject>Chemistry, Physical - methods</subject><subject>Copper - chemistry</subject><subject>Crystallization</subject><subject>Electrons</subject><subject>Hydrogen-Ion Concentration</subject><subject>Ligands</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Molecular Conformation</subject><subject>Photochemistry</subject><subject>Proteins - chemistry</subject><subject>Pseudomonas aeruginosa - metabolism</subject><subject>Ruthenium - chemistry</subject><subject>Spectrophotometry</subject><issn>1520-6106</issn><issn>1520-5207</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkU1PwzAMhiMEYmNw4A-gXkDiUEj6kbbHqRpsUoFpjHOUpcnIaJORtIjx68nUalw4RLbsR6_tNwBcIniHYIDuN1uIoyiE2REYojiAvnvJcZ9jBPEAnFm7gTCIgxSfggFKYBihJBqCKtf1lhpptfK08GaqMdT3vuw-46bWFWdtRY1XaLX2F1StuTdxtcY4fmmosoIbTyovNzvb0MruRRZt886VbGv_SZdSSF5645_WSHUOToRj-EUfR-DtYbLMp37x8jjLx4VP3VKNX2JUshVlieCh2zPMIKIQZ0EpXIEJd5s7dSVSIUQaB7gsY85iRBHL4ggnURCOwE2nuzX6s-W2IbW0jFcVVVy3luA0i-Isgw687UBmtLWGC7I1sqZmRxAke2vJwVrHXvWi7arm5R_Ze-kAvwOkbfj3oU_NB8FJmMRkOX8l7kumafY8J4XjrzueMks2ujXKefLP4F_-Lo9T</recordid><startdate>20061019</startdate><enddate>20061019</enddate><creator>Grǎdinaru, Cristian</creator><creator>Crane, Brian R</creator><general>American Chemical Society</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>20061019</creationdate><title>Comparison of Intra- vs Intermolecular Long-Range Electron Transfer in Crystals of Ruthenium-Modified Azurin</title><author>Grǎdinaru, Cristian ; Crane, Brian R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a417t-d61dcbac7fe30343901a0692dffe3cf207309bf8fff8526dd5ec51a1c95467423</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Azurin - chemistry</topic><topic>Chemistry, Physical - methods</topic><topic>Copper - chemistry</topic><topic>Crystallization</topic><topic>Electrons</topic><topic>Hydrogen-Ion Concentration</topic><topic>Ligands</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Molecular Conformation</topic><topic>Photochemistry</topic><topic>Proteins - chemistry</topic><topic>Pseudomonas aeruginosa - metabolism</topic><topic>Ruthenium - chemistry</topic><topic>Spectrophotometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Grǎdinaru, Cristian</creatorcontrib><creatorcontrib>Crane, Brian R</creatorcontrib><collection>Istex</collection><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><jtitle>The journal of physical chemistry. 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Cu1+-to-Ru3+ electron transfer (ET) across a specific protein−protein interface in the crystal lattice has a time constant 5−10 times longer than ET between the same donor and acceptor within a single protein (τET = 5 vs 0.5−1.0 μs). Slower intermolecular ET agrees well with a longer distance between redox centers across the inter-protein (18.9 Å) compared to the intra-protein separation (17.0 Å) and indicates that the closest donor/acceptor pair dominates crystal ET. Lowering the crystal pH accelerates inter-protein ET (τET = 1.0 μs) but not intra-protein ET. Faster inter-protein ET likely results from a pH-induced peptide bond flip that perturbs hydrogen bonding in the path between Ru and Cu centers on adjacent molecules.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>17034174</pmid><doi>10.1021/jp0644309</doi><tpages>4</tpages></addata></record> |
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| source | ACS Publications; MEDLINE |
| subjects | Azurin - chemistry Chemistry, Physical - methods Copper - chemistry Crystallization Electrons Hydrogen-Ion Concentration Ligands Models, Chemical Models, Molecular Molecular Conformation Photochemistry Proteins - chemistry Pseudomonas aeruginosa - metabolism Ruthenium - chemistry Spectrophotometry |
| title | Comparison of Intra- vs Intermolecular Long-Range Electron Transfer in Crystals of Ruthenium-Modified Azurin |
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