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AND PERSPECTIVE In purple photosynthetic bacteria light energy is transformed into chemical energy by the action of a light-driven proton pump coupled to electron 0066-4154/92/0701-0861$02.00 transfer. A central role in this process is played by the bacterial reaction center (RC), a membrane protein that absorbs photons, performs the initial rapid electron transfer reactions and is the site for the initial proton uptake reactions of the proton pump (reviewed in references 1-4). The key reactions that occur in the RC involve the two-electron reduction and concomitant binding of two protons from the cytoplasm side of the membrane by a bound quinone, QB , on the RC (Figure 1). The doubly reduced quinone subsequently dissociates from the RC and is reoxidized by the cytochrome ble\ complex, releasing protons on the periplasmic side of the membrane. The net result of these reactions is the vectorial transport of protons across the membrane, driven by electron transfer, as proposed by Mitchell (5). This proton transport produces a pH gradient that drives ATP synthesis (reviewed in reference 6). The transmembrane proton-pumping function of the RC has been known since the initial observation by Baltscheffsky & von Stedingk (8) of proton uptake by chromatophores from
Annual Review of Biochemistry – Annual Reviews
Published: Jul 1, 1992
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