Chlorophyll a/b binding-specificity in water-soluble chlorophyll protein.

Autor: Palm DM; Institute of Molecular Physiology, Johannes Gutenberg-University, Mainz, Germany., Agostini A; Institute of Molecular Physiology, Johannes Gutenberg-University, Mainz, Germany., Averesch V; Institute of Molecular Physiology, Johannes Gutenberg-University, Mainz, Germany., Girr P; Institute of Molecular Physiology, Johannes Gutenberg-University, Mainz, Germany., Werwie M; Institute of Molecular Physiology, Johannes Gutenberg-University, Mainz, Germany., Takahashi S; Faculty of Life Sciences, Toyo University, Itakura, Gunma, Japan., Satoh H; Department of Biomolecular Science, Faculty of Science, Toho University, Funabashi, Chiba, Japan., Jaenicke E; Institute of Molecular Physiology, Johannes Gutenberg-University, Mainz, Germany. ejaenick@uni-mainz.de., Paulsen H; Institute of Molecular Physiology, Johannes Gutenberg-University, Mainz, Germany. paulsen@uni-mainz.de.
Jazyk: angličtina
Zdroj: Nature plants [Nat Plants] 2018 Nov; Vol. 4 (11), pp. 920-929. Date of Electronic Publication: 2018 Oct 08.
DOI: 10.1038/s41477-018-0273-z
Abstrakt: We altered the chlorophyll (Chl) binding sites in various versions of water-soluble chlorophyll protein (WSCP) by amino acid exchanges to alter their preferences for either Chl a or Chl b. WSCP is ideally suited for this mutational analysis since it forms a tetrameric complex with only four identical Chl binding sites. A loop of 4-6 amino acids is responsible for Chl a versus Chl b selectivity. We show that a single amino acid exchange within this loop changes the relative Chl a/b affinities by a factor of 40. We obtained crystal structures of this WSCP variant binding either Chl a or Chl b. The Chl binding sites in these structures were compared with those in the major light-harvesting complex (LHCII) of the photosynthetic apparatus in plants to search for similar structural features involved in Chl a/b binding specificity.
Databáze: MEDLINE
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