Solid state NMR studies of photoinduced polarization in photosynthetic reaction centers: mechanism and simulations.
We simulate Photo-Chemically Induced Dynamic Nuclear Polarization in the 15N-solid-state NMR of 15N-labeled photosynthetic reaction centers using a Radical Pair Mechanism (RPM). According to the experimental data, the directly polarized nuclei include all eight nitrogens in the ground state of the bacteriochlorophyll special pair (P), and N-II in the bacteriopheophytin acceptor (H) [M.G. Zysmilich, A.E. McDermott, J. Am. Chem. Soc., 116 (1994) 8362-8363.] [M.G. Zysmilich, A. McDermott, J. Am. Chem. Soc., 118 (1996) 5867-5873.] [M.G. Zysmilich, A. McDermott, Proc. Natl. Acad. Sci. U.S.A., 93 (1996) 6857-6860.]; other signals are polarized in nonspecifically labeled samples, but the polarization apparently results from magnetization exchange with neighboring polarized nitrogens, and these are not treated in this work. Two quantitative models for the polarization associated with the RPM are presented and are used to test the validity of the proposal that this mechanism is cooperative in the reaction centers. The kinetic models can treat the steady state polarizations as well as the approach to steady state, and in principle could be expanded to include anisotropic effects, or pulse-probe experiments. Several features of the detailed simulations of the steady-state amplitudes and the kinetics of the approach to steady-state are compared with our data, including the signs and approximate absolute magnitudes of the polarization on the nitrogen nuclei in P and H(L), and the changes in the relative amplitudes with the change in the lifetime of the molecular triplet, photoaccumulation time, nuclear relaxation rate and illumination intensity. The simulations demonstrate that the polarization intensities are in qualitative agreement with those predicted for the RPM, including the curious observation of strong polariza-tion on the pheophytin acceptor for certain experimental conditions. However, this agreement requires efficient relaxation of the nitrogens on H(L) by 3P, due to a fortuitous low nanosecond value for the spin-lattice relaxation for the electrons in the molecular triplet of the donor, T1e of 3P. Whether this fortuitous match is valid is unproven.
McDermott
A
A
Department of Chemistry, Columbia University, New York, NY 10027, USA.
Zysmilich
M G
MG
Polenova
T
T
D016880:Anisotropy; D001429:Bacteriochlorophylls / Q000737:chemistry / Q000528:radiation effects; D004579:Electron Transport; D007700:Kinetics; D045342:Light-Harvesting Protein Complexes; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008956:Models, Chemical; D009584:Nitrogen / Q000737:chemistry; D010674:Pheophytins / Q000737:chemistry / Q000528:radiation effects; D010777:Photochemistry; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry* / Q000528:radiation effects*
D001429:Bacteriochlorophylls; D045342:Light-Harvesting Protein Complexes; D010674:Pheophytins; D045322:Photosynthetic Reaction Center Complex Proteins; C006678:bacteriopheophytin; D009584:Nitrogen