Selective chemical shift assignment of B800 and B850 bacteriochlorophylls in uniformly [13C,15N]-labeled light-harvesting complexes by solid-state NMR spectroscopy at ultra-high magnetic field.
Related Articles Selective chemical shift assignment of B800 and B850 bacteriochlorophylls in uniformly [13C,15N]-labeled light-harvesting complexes by solid-state NMR spectroscopy at ultra-high magnetic field.
J Am Chem Soc. 2005 Mar 9;127(9):3213-9
Authors: van Gammeren AJ, Buda F, Hulsbergen FB, Kiihne S, Hollander JG, Egorova-Zachernyuk TA, Fraser NJ, Cogdell RJ, de Groot HJ
The electronic ground states of the bacteriochlorophyll a type B800 and type B850 in the light-harvesting 2 complex of Rhodopseudomonas acidophila strain 10050 have been characterized by magic angle spinning (MAS) dipolar (13)C-(13)C correlation NMR spectroscopy. Uniformly [(13)C,(15)N] enriched light-harvesting 2 (LH2) complexes were prepared biosynthetically, while [(13)C,(15)N]-B800 LH2 complexes were obtained after reconstitution of apoprotein with uniformly [(13)C,(15)N]-enriched bacteriochlorophyll cofactors. Extensive sets of isotropic (13)C NMR chemical shifts were obtained for each bacteriochlorin ring species in the LH2 protein. (13)C isotropic shifts in the protein have been compared to the corresponding shifts of monomeric BChl a dissolved in acetone-d(6). Density functional
theory calculations were performed to estimate ring current effects induced by adjacent cofactors. By correction for the ring current shifts, the (13)C shift effects due to the interactions with the protein matrix were resolved. The chemical shift changes provide a clear evidence for a global electronic effect on the B800 and B850 macrocycles, which is attributed to the dielectrics of the protein environment, in contrast with local effects due to interaction with specific amino acid residues. Considerable shifts of -6.2 < Deltasigma < +5.8 ppm are detected for (13)C nuclei in both the B800 and the B850 bacteriochlorin rings. Because the shift effects for the B800 and B850 are similar, the polarization of the electronic ground states induced by the protein environment is comparable for both cofactors and corresponds with a red shift of approximately 30 nm relative to the monomeric BChl dissolved in acetone-d(6). The electronic coupling between the B850 cofactors due to macrocycle overlap is the predominant mechanism behind the additional red shift in the B850.
PMID: 15740162 [PubMed - indexed for MEDLINE]
Source:
PubMed