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Fine Tuning of Chlorophyll Spectra by Protein-Induced Ring Deformation. 2016

Dominika Bednarczyk, and Orly Dym, and Vadivel Prabahar, and Yoav Peleg, and Douglas H Pike, and Dror Noy
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel.

The ability to tune the light-absorption properties of chlorophylls by their protein environment is the key to the robustness and high efficiency of photosynthetic light-harvesting proteins. Unfortunately, the intricacy of the natural complexes makes it very difficult to identify and isolate specific protein-pigment interactions that underlie the spectral-tuning mechanisms. Herein we identify and demonstrate the tuning mechanism of chlorophyll spectra in type II water-soluble chlorophyll binding proteins from Brassicaceae (WSCPs). By comparing the molecular structures of two natural WSCPs we correlate a shift in the chlorophyll red absorption band with deformation of its tetrapyrrole macrocycle that is induced by changing the position of a nearby tryptophan residue. We show by a set of reciprocal point mutations that this change accounts for up to 2/3 of the observed spectral shift between the two natural variants.

UI MeSH Term Description Entries
D008027 Light That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range. Light, Visible,Photoradiation,Radiation, Visible,Visible Radiation,Photoradiations,Radiations, Visible,Visible Light,Visible Radiations
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D002734 Chlorophyll Porphyrin derivatives containing magnesium that act to convert light energy in photosynthetic organisms. Phyllobilins,Chlorophyll 740
D015394 Molecular Structure The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds. Structure, Molecular,Molecular Structures,Structures, Molecular
D017354 Point Mutation A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair. Mutation, Point,Mutations, Point,Point Mutations
D061146 Chlorophyll Binding Proteins A large family of proteins that have been traditionally classified as the light-harvesting proteins of the photosynthetic reaction complex. Chlorophyll binding proteins are also found in non-photosynthetic settings where they may play a photoprotective role in response to light stress. Chlorophyll Protein Complexes,Chlorophyll a Binding Proteins,Chlorophyll a-Proteins,Chlorophyll a-b Binding Proteins,Chlorophyll a-c Binding Proteins,Chlorophyll ab-Proteins,Chlorophyll ac-Proteins,Fucoxanthin Chlorophyll Binding Proteins,Fucoxanthin Chlorophyll Proteins,Fucoxanthin Chlorophyll a-c Binding Proteins,Chlorophyll Proteins, Fucoxanthin,Chlorophyll a Proteins,Chlorophyll a b Binding Proteins,Chlorophyll a c Binding Proteins,Chlorophyll ab Proteins,Chlorophyll ac Proteins,Fucoxanthin Chlorophyll a c Binding Proteins,Proteins, Fucoxanthin Chlorophyll
D019607 Brassicaceae A plant family of the order Capparales, subclass Dilleniidae, class Magnoliopsida. They are mostly herbaceous plants with peppery-flavored leaves, due to gluconapin (GLUCOSINOLATES) and its hydrolysis product butenylisotrhiocyanate. The family includes many plants of economic importance that have been extensively altered and domesticated by humans. Flowers have 4 petals. Podlike fruits contain a number of seeds. Cress is a general term used for many in the Brassicacea family. Rockcress is usually ARABIS; Bittercress is usually CARDAMINE; Yellowcress is usually RORIPPA; Pennycress is usually THLASPI; Watercress refers to NASTURTIUM; or RORIPPA or TROPAEOLUM; Gardencress refers to LEPIDIUM; Indiancress refers to TROPAEOLUM. Cress,Cruciferae,Moricandia,Cresses,Moricandias

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