Polarized Absorption Spectra of Green Fluorescent Protein Single Crystals:  Transition Dipole Moment Directions†

Biochemistry ◽  
2003 ◽  
Vol 42 (1) ◽  
pp. 177-183 ◽  
Author(s):  
Federico I. Rosell ◽  
Steven G. Boxer
Biopolymers ◽  
2007 ◽  
Vol 85 (3) ◽  
pp. 253-263 ◽  
Author(s):  
Soumya S. Patnaik ◽  
Steven Trohalaki ◽  
Rajesh R. Naik ◽  
Morley O. Stone ◽  
Ruth Pachter

2012 ◽  
Vol 59 (1) ◽  
Author(s):  
Tomoko Horibe ◽  
Katsunori Nakagawa ◽  
Toshiyuki Kusumoto ◽  
Ritsuko Fujii ◽  
Richard J Cogdell ◽  
...  

Reconstituted LH1 complexes were prepared using the LH1 subunit-type complexes, isolated from the purple photosynthetic bacterium Rhodospirillum (Rs.) rubrum, and purified all-trans spirilloxanthin. Stark absorption spectra of spirilloxanthin bound to both the native and reconstituted LH1 complexes were compared in different polarization angles (χ) against the external electric field. From the polarization angle dependence of the Stark absorption spectra, two angles were determined in reference to the direction of transition dipole moment (m) of spirilloxanthin: one is the change in polarizability upon photoexcitation (Δα), θ(Δα) and the other is the change in static dipole moment upon photoexcitation (Δμ), θ(Δμ). Despite the symmetric molecular structure of all-trans spirilloxanthin, its Stark absorption spectra show pronounced values of Δμ. This large Δμ values essentially caused by the effect of induced dipole moment through Δα both in the cases for native and reconstituted LH1 complexes. However, slightly different values of θ(Δα) and θ(Δμ) observed for the native LH1 complex suggest that spirilloxanthin is asymmetrically distorted when bound to the native LH1 complex and gives rise to intrinsic Δμ value.


2018 ◽  
Author(s):  
Angus J. Bain ◽  
Nicholas Robinson ◽  
Thomas Masters ◽  
Thomas Blacker ◽  
Richard J. Marsh ◽  
...  

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