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Inside Back Cover: Fine Tuning of Chlorophyll Spectra by Protein‐Induced Ring Deformation (Angew. Chem. Int. Ed. 24/2016)
Author(s) -
Bednarczyk Dominika,
Dym Orly,
Prabahar Vadivel,
Peleg Yoav,
Pike Douglas H.,
Noy Dror
Publication year - 2016
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201603826
Subject(s) - chlorophyll , planarity testing , chlorophyll a , ring (chemistry) , chemistry , hydrogen bond , spectral line , tryptophan , photochemistry , crystallography , molecule , organic chemistry , physics , biochemistry , amino acid , astronomy
A red bend aromatic ring deformation has long been postulated as a mechanism for tuning the absorption spectra of chlorophylls in their natural protein environment. In their Communication on page 6901 ff., D. Noy and co‐workers provide the first direct demonstration of such a mechanism in the water‐soluble chlorophyll binding protein (WSCP) from Brassicaceae. Changes in hydrogen bonding to a tryptophan residue reposition it to perturb the planarity of the chlorophyll macrocycle thereby causing significant absorption red shifts.