Search results for "Light harvesting complex II"
showing 3 items of 3 documents
Crystallization of Light-Harvesting Complex II From Vicia Faba (Fabaceae)
1998
The most abundant chlorophyll binding complex in plants is the intrinsic light-harvesting complex II (LHC II), comprising about half of the total chlorophyll in thylakoid membranes. The structure of LHC II has been determined by electron crystallography, providing a three-dimensional map at 3.4 A (1). Nevertheless, high-resolution structure based on x-ray crystallography is still missing because of the lack of highly ordered 3-D crystals. While delipidation of membrane proteins suitable for high-quality 3-D crystals seems to be a prerequisite, in case of LHC H delipidation leads to a loss of the ability to crystallize. So far, standard purification methods like chromatography have been proo…
Site-specific incorporation of perylene into an N-terminally modified light-harvesting complex II.
2010
Employing the utility of the native chemical ligation, site-specific attachment of an ultrastable perylene dye to a derivative of the major light-harvesting complex (LHCII) was demonstrated. Biochemical analysis of the conjugate indicated that the structure and function of LHCII remain largely unaffected by the N-terminal modification.
Assemblies of semiconductor quantum dots and light-harvesting-complex II
2010
Abstract A novel hybrid system composed of fluorescent core/shell semiconductor quantum dots and the light harvesting complex II (LHCIIb), a membrane protein of higher plants, has been assembled. Experiments with different mutants show that hybrid formation can be mediated by a C-terminal His 6 tag attached to the protein as well as by positive charges of the first N-terminal amino acids of LHCIIb. Quenching of the quantum dot fluorescence upon binding of LHCIIb was partially attributed to energy transfer from the quantum dots to LHCIIb.