1R2C

PHOTOSYNTHETIC REACTION CENTER BLASTOCHLORIS VIRIDIS (ATCC)

1R2C の概要

• エントリーDOI: 10.2210/pdb1r2c/pdb
• 分子名称: Photosynthetic reaction center cytochrome C subunit precursor, FE (II) ION, SULFATE ION, ... (13 entities in total)
• 機能のキーワード: photosynthetic reaction center, secondary quinone (qb), photosynthesis
• 由来する生物種: Blastochloris viridis; 詳細
• 細胞内の位置: Cell membrane; Lipid-anchor: P06009; Cellular chromatophore membrane; Multi-pass membrane protein (By similarity): P07173 P06010; Cellular chromatophore membrane; Single-pass membrane protein: P06008
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 143612.66

構造登録者

Baxter, R.H.,Ponomarenko, N.,Pahl, R.,Srajer, V.,Moffat, K.,Norris, J.R. (登録日: 2003-09-26, 公開日: 2004-04-27, 最終更新日: 2024-10-30)

主引用文献

Baxter, R.H.,Ponomarenko, N.,Srajer, V.,Pahl, R.,Moffat, K.,Norris, J.R.
Time-resolved crystallographic studies of light-induced structural changes in the photosynthetic reaction center.
Proc.Natl.Acad.Sci.USA, 101:5982-5987, 2004

PubMed Abstract: Light-induced structural changes in the bacterial reaction center were studied by a time-resolved crystallographic experiment. Crystals of protein from Blastochloris viridis (formerly Rhodopseudomonas viridis) were reconstituted with ubiquinone and analyzed by monochromatic and Laue diffraction, in the dark and 3 ms after illuminating the crystal with a pulsed laser (630 nm, 3 mJ/pulse, 7 ns duration). Refinement of monochromatic data shows that ubiquinone binds only in the "proximal" Q(B) binding site. No significant structural difference was observed between the light and dark datasets; in particular, no quinone motion was detected. This result may be reconciled with previous studies by postulating equilibration of the "distal" and "proximal" binding sites upon extended dark adaption, and in which movement of ubiquinone is not the conformational gate for the first electron transfer between Q(A) and Q(B).

PubMed: 15073325
DOI: 10.1073/pnas.0306840101

実験手法

X-RAY DIFFRACTION (2.86 Å)