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| | <StructureSection load='5lri' size='340' side='right'caption='[[5lri]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='5lri' size='340' side='right'caption='[[5lri]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lri]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LRI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LRI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lri]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides_2.4.1 Cereibacter sphaeroides 2.4.1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LRI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LRI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=DD9:NONANE'>DD9</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=SPN:SPEROIDENONE'>SPN</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</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]] 2.4Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lri OCA], [http://pdbe.org/5lri PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lri RCSB], [http://www.ebi.ac.uk/pdbsum/5lri PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lri ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=DD9:NONANE'>DD9</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=SPN:SPEROIDENONE'>SPN</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></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=5lri FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lri OCA], [https://pdbe.org/5lri PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lri RCSB], [https://www.ebi.ac.uk/pdbsum/5lri PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lri ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RCEL_RHOS4 RCEL_RHOS4]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis (By similarity). [[http://www.uniprot.org/uniprot/RCEH_RHOS4 RCEH_RHOS4]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[http://www.uniprot.org/uniprot/RCEM_RHOS4 RCEM_RHOS4]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. | + | [https://www.uniprot.org/uniprot/RCEL_CERS4 RCEL_CERS4] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Cereibacter sphaeroides 2 4.1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fyfe, P K]] | + | [[Category: Fyfe PK]] |
| - | [[Category: Jones, M R]] | + | [[Category: Jones MR]] |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Photosynthesis]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| Structural highlights
5lri is a 3 chain structure with sequence from Cereibacter sphaeroides 2.4.1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.4Å |
| Ligands: | , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
RCEL_CERS4 The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
Publication Abstract from PubMed
Upon photoexcitation, the reaction center (RC) pigment-proteins that facilitate natural photosynthesis achieve a metastable separation of electrical charge among the embedded cofactors. Because of the high quantum efficiency of this process, there is a growing interest in their incorporation into biohybrid materials for solar energy conversion, bioelectronics and biosensing. Multiple bioelectrochemical studies have shown that reaction centers from various photosynthetic organisms can be interfaced with diverse electrode materials for the generation of photocurrents, but many mechanistic aspects of native protein functionality in a non-native environment is unknown. In vivo, RC's catalyse ubiquinone-10 reduction, protonation and exchange with other lipid phase ubiquinone-10s via protein-controlled spatial orientation and protein rearrangement. In contrast, the mechanism of ubiquinone-0 reduction, used to facilitate fast RC turnover in an aqueous photoelectrochemical cell (PEC), may not proceed via the same pathway as the native cofactor. In this report we show truncation of the native isoprene tail results in larger RC turnover rates in a PEC despite the removal of the tail's purported role of ubiquinone headgroup orientation and binding. Through the use of reaction centers with single or double mutations, we also show the extent to which two-electron/two-proton ubiquinone chemistry that operates in vivo also underpins the ubiquinone-0 reduction by surface-adsorbed RCs in a PEC. This reveals that only the ubiquinone headgroup is critical to the fast turnover of the RC in a PEC and provides insight into design principles for the development of new biophotovoltaic cells and biosensors.
On the mechanism of ubiquinone mediated photocurrent generation by a reaction center based photocathode.,Friebe VM, Swainsbury DJ, Fyfe PK, van der Heijden W, Jones MR, Frese RN Biochim Biophys Acta. 2016 Dec;1857(12):1925-1934. doi:, 10.1016/j.bbabio.2016.09.011. Epub 2016 Sep 28. PMID:27687473[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Friebe VM, Swainsbury DJ, Fyfe PK, van der Heijden W, Jones MR, Frese RN. On the mechanism of ubiquinone mediated photocurrent generation by a reaction center based photocathode. Biochim Biophys Acta. 2016 Dec;1857(12):1925-1934. doi:, 10.1016/j.bbabio.2016.09.011. Epub 2016 Sep 28. PMID:27687473 doi:http://dx.doi.org/10.1016/j.bbabio.2016.09.011
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