1997
DOI: 10.1126/science.276.5313.812
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Light-Induced Structural Changes in Photosynthetic Reaction Center: Implications for Mechanism of Electron-Proton Transfer

Abstract: 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 … Show more

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Cited by 788 publications
(1,094 citation statements)
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“…Furthermore, our results show that a significant protein response is required to stabilize (Q A Q B −• ). Although our results do not imply that the movement of quinone from the distal to proximal sites is ratelimiting, they do support the idea that the movement to the proximal site is a necessary prerequisite for its stabilization (27). EPR signal monitored before, during and following illumination of dark frozen samples for the native RC (left panels) and the Quintuple B-branch RCs (right panels).…”
Section: Conformational Gatecontrasting
confidence: 65%
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“…Furthermore, our results show that a significant protein response is required to stabilize (Q A Q B −• ). Although our results do not imply that the movement of quinone from the distal to proximal sites is ratelimiting, they do support the idea that the movement to the proximal site is a necessary prerequisite for its stabilization (27). EPR signal monitored before, during and following illumination of dark frozen samples for the native RC (left panels) and the Quintuple B-branch RCs (right panels).…”
Section: Conformational Gatecontrasting
confidence: 65%
“…where k C is the rate constant of the rate-limiting conformational gate (9) the necessity for Q B to move into the proximal position for stabilization (27). Furthermore, our results show that a significant protein response is required to stabilize (Q A Q B −• ).…”
Section: Conformational Gatementioning
confidence: 73%
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“…In purple anoxygenic bacteria, reaction centers (RCs) embedded in the membrane perform the primary photochemistry (Blankenship et al 1995). The RC from Rhodobacter sphaeroides consists of three protein subunits and several cofactors (see e.g., Allen et al 1987;Yeates et al 1988;Ermler et al 1994;Stowell et al 1997;Camara-Artigas et al 2002). The core L and M subunits surround the cofactors that are divided into two distinct branches related by an approximate two-fold symmetry axis that runs from the center of P to the non-heme iron (Fig.…”
Section: Introductionmentioning
confidence: 99%