Abstract
The bacterial photosynthetic reaction center (RC) has been genetically altered such that two of the eleven transmembrane α-helices, primarily involved in pigment binding, have been either exchanged or duplicated. These large scale structural motif rearrangements result in protein folding and/or electron transfer defects that can be compensated by single point mutations. Absorption spectra and linear dichroism spectra of these modified pigment-proteins have been obtained directly from membranes lacking all other chromophores (e.g. light harvesting antennae). Duplication of the L-subunit D helix results in the loss of the photoactive bacteriopheophytin without significant perturbation of the other prosthetic groups. Photosynthetically competent revertants of the M-subunit D helix duplication have been isolated and their RCs are possible candidates for bidirectional electron transfer. Pseudo wild-type RCs symmetrized by genetic manipulation place important structural constraints on models for charge-separation that invoke essential amino acid asymmetries between the L and M subunits.
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Robles, S.J., Breton, J., Youvan, D.C. (1990). Transmembrane Helix Exchanges Between Quasi-Symmetric Subunits of the Photosynthetic Reaction Center. In: Michel-Beyerle, ME. (eds) Reaction Centers of Photosynthetic Bacteria. Springer Series in Biophysics, vol 6. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-61297-8_28
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DOI: https://doi.org/10.1007/978-3-642-61297-8_28
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