Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. 1997

M H Stowell, and T M McPhillips, and D C Rees, and S M Soltis, and E Abresch, and G Feher
Division of Chemistry and Chemical Engineering, 147-75CH, California Institute of Technology, Pasadena, CA 91125, USA.

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+QAQB- 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 degrees 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.

UI MeSH Term Description Entries
D008027 Light That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range. Light, Visible,Photoradiation,Radiation, Visible,Visible Radiation,Photoradiations,Radiations, Visible,Visible Light,Visible Radiations
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011522 Protons Stable elementary particles having the smallest known positive charge, found in the nuclei of all elements. The proton mass is less than that of a neutron. A proton is the nucleus of the light hydrogen atom, i.e., the hydrogen ion. Hydrogen Ions,Hydrogen Ion,Ion, Hydrogen,Ions, Hydrogen,Proton
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D003460 Crystallization The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Crystalline Polymorphs,Polymorphism, Crystallization,Crystal Growth,Polymorphic Crystals,Crystal, Polymorphic,Crystalline Polymorph,Crystallization Polymorphism,Crystallization Polymorphisms,Crystals, Polymorphic,Growth, Crystal,Polymorph, Crystalline,Polymorphic Crystal,Polymorphisms, Crystallization,Polymorphs, Crystalline
D003624 Darkness The absence of light. Darknesses
D004579 Electron Transport The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270) Respiratory Chain,Chain, Respiratory,Chains, Respiratory,Respiratory Chains,Transport, Electron
D005615 Freezing Liquids transforming into solids by the removal of heat. Melting
D006860 Hydrogen Bonding A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds. Hydrogen Bonds,Bond, Hydrogen,Hydrogen Bond

Related Publications

M H Stowell, and T M McPhillips, and D C Rees, and S M Soltis, and E Abresch, and G Feher
October 1986, Physical review. A, General physics,
M H Stowell, and T M McPhillips, and D C Rees, and S M Soltis, and E Abresch, and G Feher
December 2004, Journal of the American Chemical Society,
M H Stowell, and T M McPhillips, and D C Rees, and S M Soltis, and E Abresch, and G Feher
April 2010, Science (New York, N.Y.),
M H Stowell, and T M McPhillips, and D C Rees, and S M Soltis, and E Abresch, and G Feher
January 1976, Brookhaven symposia in biology,
M H Stowell, and T M McPhillips, and D C Rees, and S M Soltis, and E Abresch, and G Feher
April 2004, Proceedings of the National Academy of Sciences of the United States of America,
M H Stowell, and T M McPhillips, and D C Rees, and S M Soltis, and E Abresch, and G Feher
August 1998, Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy,
M H Stowell, and T M McPhillips, and D C Rees, and S M Soltis, and E Abresch, and G Feher
July 2019, The journal of physical chemistry. B,
M H Stowell, and T M McPhillips, and D C Rees, and S M Soltis, and E Abresch, and G Feher
November 1984, Biochemistry,
M H Stowell, and T M McPhillips, and D C Rees, and S M Soltis, and E Abresch, and G Feher
June 1996, Biophysical journal,
Copied contents to your clipboard!