Quantitative assessment of chlorophyll types in cryo-EM maps of photosystem I acclimated to far-red light.

Autor:	Gisriel CJ; Department of Chemistry, Yale University, New Haven, CT 06520, USA., Huang HL; Department of Chemistry, Yale University, New Haven, CT 06520, USA., Reiss KM; Department of Chemistry, Yale University, New Haven, CT 06520, USA., Flesher DA; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA., Batista VS; Department of Chemistry, Yale University, New Haven, CT 06520, USA., Bryant DA; Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA., Brudvig GW; Department of Chemistry, Yale University, New Haven, CT 06520, USA.; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA., Wang J; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
Jazyk:	angličtina
Zdroj:	BBA advances [BBA Adv] 2021 Jun 26; Vol. 1, pp. 100019. Date of Electronic Publication: 2021 Jun 26 (Print Publication: 2021).
DOI:	10.1016/j.bbadva.2021.100019
Abstrakt:	Chlorophyll cofactors are vital for the metabolism of photosynthetic organisms. Cryo-electron microscopy (cryo-EM) has been used to elucidate molecular structures of pigment-protein complexes, but the minor structural differences between multiple types of chlorophylls make them difficult to distinguish in cryo-EM maps. This is exemplified by inconsistencies in the assignments of chlorophyll f molecules in structures of photosystem I acclimated to far-red light (FRL-PSI). A quantitative assessment of chlorophyll substituents in cryo-EM maps was used to identify chlorophyll f -binding sites in structures of FRL-PSI from two cyanobacteria. The two cryo-EM maps provide direct evidence for chlorophyll f -binding at two and three binding sites, respectively, and three more sites in each structure exhibit strong indirect evidence for chlorophyll f -binding. Common themes in chlorophyll f -binding are described that clarify the current understanding of the molecular basis for FRL photoacclimation in photosystems. Competing Interests: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper. (©2021TheAuthor(s).PublishedbyElsevierB.V.)
Databáze:	MEDLINE
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