Abstract
Light-induced electron transport in bacterial photosynthetic reaction centers leads to the creation of a charge-separated state stable for milliseconds to seconds. The structures provided by X-ray crystallography (Michel et aL, 1986; Allen et al., 1988; Deisenhofer & Michel, 1989; El-Kabbani et al, 1991) constitute a unique guideline to address questions on how the function may be related to the arrangement of the cofactors and of specific amino acid residues in their vicinity. The sequence of electron transfer reactions, the identity of the reaction partners, and the reaction mechanisms have been characterized from static and time-resolved absorbance measurements (for a review, see Parson & Ke, 1982). Transfer of the first electron to the primary (QA) and secondary (QB) quinone electron acceptors has received considerable attention, since it is associated with intraprotein protolytic reactions (for a recent review, see Okamura & Feher, 1992), which have a potential role in electrostatic charge stabilization.
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