Biochim

Biophys Acta 1767:610–615. doi:10.​1016/​j.​bbabio.​2006.​12.​012 CrossRefPubMed Roy E, Rohmer T, Gast P et al (2008) Characterization of the primary electron pair in reaction centers of Heliobacillus mobilis by 13C photo-CIDNP MAS NMR. Biochemistry 47:4629–4635. doi:10.​1021/​bi800030g CrossRefPubMed Schrödinger E (1944) What is life?. Cambridge University Press, Cambridge Schulten EAM, Matysik J, Alia A et al (2002) C-13 MAS NMR and photo-CIDNP reveal a pronounced asymmetry in the electronic ground state of the special pair of Rhodobacter selleck chemicals llc sphaeroides reaction centers. Biochemistry 41:8708–8717. doi:10.​1021/​bi025608u CrossRefPubMed Tributsch H (2006) CCI-779 mw Kinetically determined solar cells. C R Chim 9:584–596 Tributsch H, Pohlmann L (1998) Electron transfer and new frontiers. Science 279:1891–1895CrossRefPubMed Ward HR, Lawler RG (1967) Nuclear magnetic resonance emission and enhanced absorption in rapid organometallic reactions. J Am Chem Soc 89:5518–5519CrossRef Werner H-J, Schulten K, Weller A (1978) Electron transfer and spin exchange contributing to the magnetic field dependence of the primary photochemical reaction of bacterial photosynthesis. Biochim Biophys Acta 502:255–268CrossRefPubMed Zysmilich MG, McDermott A (1994) Photochemically induced dynamic nuclear-polarization in the solid-state N-15 spectra of reaction centers from

photosynthetic bacteria Rhodobacter sphaeroides R-26. J Am Chem Soc 116:8362–8363CrossRef Zysmilich MG, McDermott A (1996a) Natural abundance solid-state carbon NMR studies learn more of photosynthetic reaction centers with photoinduced polarization. Proc Natl Acad Sci USA 93:6857–6860CrossRefPubMed Zysmilich MG, McDermott A (1996b) Farnesyltransferase Photochemically induced nuclear spin polarization in bacterial photosynthetic reaction centers: Assignments

of the N-15 ssNMR spectra. J Am Chem Soc 118:5867–5873CrossRef”
“Introduction Solid-state magic angle spinning (MAS) NMR provides a versatile method for the determination of structure for ordered systems without translation symmetry, such as proteins, macromolecular complexes, aggregates, or membrane systems. With the continued difficulty in crystallizing membrane proteins, solid-state NMR spectroscopy is becoming an important method in the analysis of this important class of proteins. For MAS NMR, protein crystallization is not necessary. The homogeneous environment in the protein sample and a local order are sufficient. In addition, use of stable isotopes in combination with MAS NMR offers prospects for the study of larger and more complex biomolecules, such as large membrane-bound photosynthetic complexes, in their undisturbed native form. In photosynthetic research, a variety of structural details have been obtained using MAS NMR (de Groot 2008). For instance, structural and functional details from light-harvesting pigments (Boender et al. 1995; van Rossum et al.