2GMR
Photosynthetic reaction center mutant from Rhodobacter sphaeroides with Asp L210 replaced with Asn
2GMR の概要
| エントリーDOI | 10.2210/pdb2gmr/pdb |
| 分子名称 | Photosynthetic Reaction center protein L chain, Photosynthetic Reaction center protein M chain, Photosynthetic reaction center protein H chain, ... (10 entities in total) |
| 機能のキーワード | photosynthetic reaction center, integral membrane protein, electron transport, proton transfer, l210dn, mutant, photosynthesis |
| 由来する生物種 | Rhodobacter sphaeroides 詳細 |
| 細胞内の位置 | Cellular chromatophore membrane ; Multi-pass membrane protein : Q3J1A5 P0C0Y9 Cellular chromatophore membrane; Single-pass membrane protein: P0C0Y7 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 102529.85 |
| 構造登録者 | Stachnik, J.M.,Hermes, S.,Gerwert, K.,Hofmann, E. (登録日: 2006-04-07, 公開日: 2006-11-21, 最終更新日: 2023-08-30) |
| 主引用文献 | Hermes, S.,Stachnik, J.M.,Onidas, D.,Remy, A.,Hofmann, E.,Gerwert, K. Proton uptake in the reaction center mutant L210DN from Rhodobacter sphaeroides via protonated water molecules. Biochemistry, 45:13741-13749, 2006 Cited by PubMed Abstract: The reaction center (RC) of Rhodobacter sphaeroides uses light energy to reduce and protonate a quinone molecule, QB (the secondary quinone electron acceptor), to form quinol, QBH2. Asp210 in the L-subunit has been shown to be a catalytic residue in this process. Mutation of Asp210 to Asn leads to a deceleration of reoxidation of QA- in the QA-QB --> QAQB- transition. Here we determined the structure of the Asp210 to Asn mutant to 2.5 A and show that there are no major structural differences as compared to the wild-type protein. We found QB in the distal position and a chain of water molecules between Asn210 and QB. Using time-resolved Fourier transform infrared (trFTIR) spectroscopy, we characterized the molecular reaction mechanism of this mutant. We found that QB- formation precedes QA- oxidation even more pronounced than in the wild-type reaction center. Continuum absorbance changes indicate deprotonation of a protonated water cluster, most likely of the water chain between Asn210 and QB. A detailed analysis of wild-type structures revealed a highly conserved water chain between Asp210 or Glu210 and QB in Rb. sphaeroides and Rhodopseudomonas viridis, respectively. PubMed: 17105193DOI: 10.1021/bi060742q 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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