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Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer
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Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer
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Journal Article
Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer
1997
Overview
High resolution x-ray diffraction data from crystals of the Rhodobacter sphaeroides photosynthetic reaction center (RC) have been collected at cryogenic temperature in the dark and under illumination, and the structures were refined at 2.2 and 2.6 angstrom resolution, respectively. In the charge-separated D(+)QACB(-) state (where D is the primary electron donor (a bacteriochlorophyll dimer), and QA and QB are the primary and secondary quinone acceptors, respectively), QB(-) is located approximately 5 angstroms from the QB position in the charge-neutral (DQAQB) state, and has undergone a 180 degree propeller twist around the isoprene chain. A model based on the difference between the two structures is proposed to explain the observed kinetics of electron transfer from QA-QB to QAQB(-) and the relative binding affinities of the different ubiquinone species in the QB pocket. In addition, several water channels (putative proton pathways) leading from the QB pocket to the surface of the RC were delineated, one of which leads directly to the membrane surface
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science
Subject
Analytical, structural and metabolic biochemistry
/ BACTERIA
/ Biological and medical sciences
/ Crystals
/ Darkness
/ Freezing
/ Fundamental and applied biological sciences. Psychology
/ Kinetics
/ Light
/ Light-Harvesting Protein Complexes
/ Non metallic chromoproteins, photoproteins
/ Photosynthetic Reaction Center Complex Proteins
/ Photosynthetic Reaction Center Complex Proteins - chemistry
/ Photosynthetic Reaction Center Complex Proteins - metabolism
/ Proteins
/ Protons
