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| ==Structure of Re(CO)3(4,7-dimethyl-phen)(Thr126His)(Lys122Trp)(His83Glu)(Trp48Phe)(Tyr72Phe)(Tyr108Phe)AzCu(II), a Rhenium modified Azurin mutant== | | ==Structure of Re(CO)3(4,7-dimethyl-phen)(Thr126His)(Lys122Trp)(His83Glu)(Trp48Phe)(Tyr72Phe)(Tyr108Phe)AzCu(II), a Rhenium modified Azurin mutant== |
- | <StructureSection load='4k9j' size='340' side='right' caption='[[4k9j]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='4k9j' size='340' side='right'caption='[[4k9j]], [[Resolution|resolution]] 1.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4k9j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K9J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K9J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4k9j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K9J FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=REQ:(1,10+PHENANTHROLINE)-(TRI-CARBON+MONOXIDE)+RHENIUM+(I)'>REQ</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4azu|4azu]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">azu, PA4922 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4k9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k9j OCA], [https://pdbe.org/4k9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k9j RCSB], [https://www.ebi.ac.uk/pdbsum/4k9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k9j ProSAT]</span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k9j OCA], [http://pdbe.org/4k9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k9j RCSB], [http://www.ebi.ac.uk/pdbsum/4k9j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k9j ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE]] Transfers electrons from cytochrome c551 to cytochrome oxidase. | + | [https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase. |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| ==See Also== | | ==See Also== |
- | *[[Azurin|Azurin]] | + | *[[Azurin 3D structures|Azurin 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Pseae]] | + | [[Category: Large Structures]] |
- | [[Category: Blanco-Rodriguez, A M]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
- | [[Category: Clark, I P]] | + | [[Category: Blanco-Rodriguez AM]] |
- | [[Category: Gray, H B]] | + | [[Category: Clark IP]] |
- | [[Category: Jr, A Vlcek]] | + | [[Category: Gray HB]] |
- | [[Category: Kaiser, J T]] | + | [[Category: Kaiser JT]] |
- | [[Category: Nikolovski, P]] | + | [[Category: Nikolovski P]] |
- | [[Category: Sokolova, L]] | + | [[Category: Sokolova L]] |
- | [[Category: Takematsu, K]] | + | [[Category: Takematsu K]] |
- | [[Category: Towrie, M]] | + | [[Category: Towrie M]] |
- | [[Category: Williamson, H R]] | + | [[Category: Vlcek Jr A]] |
- | [[Category: Winkler, J R]] | + | [[Category: Williamson HR]] |
- | [[Category: Electron transport]] | + | [[Category: Winkler JR]] |
- | [[Category: Rhenium]]
| + | |
| Structural highlights
Function
AZUR_PSEAE Transfers electrons from cytochrome c551 to cytochrome oxidase.
Publication Abstract from PubMed
Re126W122CuI Pseudomonas aeruginosa azurin incorporates three redox sites, ReI(CO)3(4,7-dimethyl-1,10-phenanthroline) covalently bound at H126, the W122 indole side chain, and CuI, which are well separated in the protein fold: Re-W122(indole) = 13.1 A; dmp-W122(indole) = 10.0 A, Re-Cu = 25.6 A. In view of the long intramolecular Re-Cu distance, it is surprising that CuI is oxidized in less than 50 ns after near-UV excitation of the Re chromophore. Back electron transfer (BET) regenerating CuI and ground-state ReI takes much longer (220 ns and 6 us). We show that these ET reactions occur in protein dimers, (Re126W122CuI)2, which are in equilibrium with unreactive monomers. In support of this interpretation, ET yields and kinetics are concentration-dependent and solution mass spectrometry (LILBID-MS) confirms the presence of a broad oligomer distribution with prevalent monomers and dimers; in the crystal structure, two Re126W122CuII molecules are oriented in such a way that the redox cofactors Re(dmp) and W122-indole belonging to different monomers are located at a protein-protein interface (//), where the intermolecular ET-relevant distances (Re-W122(indole) = 6.9 A, dmp-W122(indole) = 3.5 A, and Re-Cu = 14.0 A) are much shorter than intramolecular ones. We propose that forward ET is accelerated by intermolecular electron hopping through a surface tryptophan: *Re//<-W122<-CuI; our kinetics analysis indicates that an equilibrium (K = 0.8-0.9) between *Re and charge-separated Re(dmp*-)(W122*+), which is established in a few ns, stores part of the excitation energy. The second ET step, intramolecular CuI oxidation, CuI->W122*+, occurs in 30 ns. The system is well coupled for forward ET but not for ReI(dmp*-)->CuII BET. Our work on interfacial electron hopping in (Re126W122CuI)2 sheds new light on redox-unit placements required for functional long-range charge separation in protein complexes.
Tryptophan-accelerated electron flow across a protein-protein interface.,Takematsu K, Williamson H, Blanco-Rodriguez AM, Sokolova L, Nikolovski P, Kaiser JT, Towrie M, Clark IP, Vlcek A, Winkler JR, Gray HB J Am Chem Soc. 2013 Sep 13. PMID:24032375[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Takematsu K, Williamson H, Blanco-Rodriguez AM, Sokolova L, Nikolovski P, Kaiser JT, Towrie M, Clark IP, Vlcek A, Winkler JR, Gray HB. Tryptophan-accelerated electron flow across a protein-protein interface. J Am Chem Soc. 2013 Sep 13. PMID:24032375 doi:10.1021/ja406830d
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