1. Light and Energy. 2. Organization and Structure of Photosynthetic Systems. 3. History and Development of Photosynthesis. 4. Photosynthetic Pigments-Structure and Spectroscopy. 5. Antenna Complexes and Energy Transfer Processes. 6. Reaction Center Complexes. 7. Electron Transfer Pathways and Components. 8. Chemiosmotic Coupling and ATP Synthesis. 9. Carbon Metabolism. 10. Genetics, Assembly and Regulation of Photosynthetic. Systems. 11. Origin and Evolution of Photosynthesis. Appendix 1. Light, Energy and Kinetics

Molecular mechanisms of photosynthesis

How lipids affect the activities of integral membrane proteins

Ultrafast dynamics of carotenoid excited States-from solution to natural and artificial systems.

Femtosecond visible and infrared analogues of multiple-pulse nuclear magnetic resonance techniques provide novel snapshot probes into the structure and electronic and vibrational dynamics of complex molecular assemblies such as photosynthetic antennae, proteins, and hydrogen-bonded liquids. A classical-oscillator description of these spectroscopies in terms of interacting quasiparticles (rather than transitions among global eigenstates) is developed and sets the stage for designing new pulse sequences and inverting the multidimensional signals to yield molecular structures. Considerable computational advantages and a clear physical insight into the origin of the response and the relevant coherence sizes are provided by a real-space analysis of the underlying coherence-transfer pathways in Liouville space.

Multidimensional femtosecond correlation spectroscopies of electronic and vibrational excitations.

Publisher Summary This chapter discusses the translation, rotation, and screw-rotation (TLS) parameterization of anisotropic displacement parameters (ADPs). In general, each atom can deviate anisotropically from its mean position, and six parameters are necessary to describe the mean square displacements fully. These parameters are referred to as the “ADPs,” are usually denoted U, and can be visualized as “thermal ellipsoids.” The addition of an extra six parameters per atom in macromolecular refinement is usually not justified by the data, except when atomic resolution data are available (

Macromolecular TLS refinement in REFMAC at moderate resolutions.

The crystal structure at 4.8 angstrom resolution of the reaction center–light harvesting 1 (RC–LH1) core complex from Rhodopseudomonas palustris shows the reaction center surrounded by an oval LH1 complex that consists of 15 pairs of transmembrane helical α- and β-apoproteins and their coordinated bacteriochlorophylls. Complete closure of the RC by the LH1 is prevented by a single transmembrane helix, out of register with the array of inner LH1 α-apoproteins. This break, located next to the binding site in the reaction center for the secondary electron acceptor ubiquinone (UQB), may provide a portal through which UQB can transfer electrons to cytochrome b/c1.

https://science.sciencemag.org/content/sci/302/5652/1969.full.pdf

Crystal structure of the RC-LH1 core complex from Rhodopseudomonas palustris.

The structure and thermal motion of the B800-850 LH2 complex from Rps.acidophila at 2.0A resolution and 100K: new structural features and functionally relevant motions.

Single assemblies of the intact light-harvesting complex LH2 from Rhodopseudomonas acidophila were bound to mica surfaces at 300 K and examined by observing their fluorescence after polarized light excitation The complexes are generally not cylindrically symmetric They act like elliptic absorbers, indicating that the high symmetry found in crystals of LH2 is not present when the molecules are immobilized on mica The ellipticity and the principal axes of the ellipses fluctuate on the time scale of seconds, indicating that there is a mobile structural deformation The B850 ring of cofactors shows significantly less asymmetry than B800 The photobleaching strongly depends on the presence of oxygen

https://www.pnas.org/content/pnas/96/20/11271.full.pdf

The dynamics of structural deformations of immobilized single light-harvesting complexes

The essential function of carotenoids in photosynthesis is to act as photoprotective agents, preventing chlorophylls and bacteriochlorophylls from sensitizing harmful photodestructive reactions in the presence of oxygen. Based upon recent structural studies on reaction centres and antenna complexes from purple photosynthetic bacteria, the detailed organization of the carotenoids is described. Then with specific reference to bacterial antenna complexes the details of the photoprotective role, triplet triplet energy transfer, are presented.

/pdf/how-carotenoids-protect-bacterial-photosynthesis-tobkenmy4a.pdf

How carotenoids protect bacterial photosynthesis

The past several years have seen dramatic progress in our understanding of the reactions taking place in the early events of photosynthesis. This has been in large part due to research involving purple photosynthetic bacteria ([16][1], [28][2], [34][3], [35][4],[46][5], [56][6]). These anaerobic

Tina D. Howard

Papers

Crystal structure of the RC-LH1 core complex from Rhodopseudomonas palustris.

The structure and thermal motion of the B800-850 LH2 complex from Rps.acidophila at 2.0A resolution and 100K: new structural features and functionally relevant motions.

The dynamics of structural deformations of immobilized single light-harvesting complexes

How carotenoids protect bacterial photosynthesis

How Photosynthetic Bacteria Harvest Solar Energy