Bidirectional electron transfer in photosystem I: Replacement of the symmetry-breaking tryptophan close to the PsaB-bound phylloquinone (A1B) with a glycine residue alters the redox properties of A1B and blocks forward electron transfer at cryogenic temperatures
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference37 articles.
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2. Four-dimensional microED of conformational dynamics in protein microcrystals on the femto-to-microsecond timescales;Journal of Structural Biology;2023-03
3. Photosystems I and II;The Chlamydomonas Sourcebook;2023
4. Room temperature XFEL crystallography reveals asymmetry in the vicinity of the two phylloquinones in photosystem I;Scientific Reports;2021-11-08
5. Conserved residue PsaB-Trp673 is essential for high-efficiency electron transfer between the phylloquinones and the iron-sulfur clusters in Photosystem I;Photosynthesis Research;2021-05-15
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