羟氨苄青霉素引起大疱性类天疱疮样疹

T.J. DiMagno and JR. Volume 2: P.L. Duttonn, C.C. Moser, J.M. Keske, K. Warncke, and R.S. Farid, Electron-Transfer Mechanisms in Reaction Centers: Engineering Guidelines. A. Warshel and W.W. Parson, Simulations of Electron Transfer in Bacterial Reaction Centres. C. Kirmaier and D. Holten, Electron Transfer and Charge Recombination Reactions in Wild-type and Mutant Bacterial Reaction Centres. W. Zinth and W. Kaiser, Time Resolved Spectroscopy of the Primary Electron Transfer in Reaction Centers of Rb. sphaeroides and Rps. viridis. V.A. Shuvalov, Tune and Frequency Domain Study of Different Electron Transfer Processes in Bacterial Reaction Centres.Morris, Electron Transfer in Photosynthetic Bacteria. G.J. Small and R. Jankowiak Spectral Hole Bunting: A Window on Excited State Electronic Structure, Heterogeneity, Electron-Phonon Coupling and Transport Dynamics of Photosynthetic Units. S.G. Boxer, Photosynthetic Reaction Centre Spectroscopy and Electron Transfer Dynamics in Applied Electric Fields. H.A. Frank Carotenoids in Photosynthetic Bacterial Reaction Centers: Structure, Spectroscopy, and Photochemistry. W. Maentele, Infrared Vibrational Spectroscopy of the Photosynthetic Reaction Center. M.C. Thurnauer and S. Snyder, Electron Spin Polarization in Photosynthetic Reaction Centres. A.J. Hoff, Magnetic Resonance of Bacterial Photosynthetic Reaction Centres. H. Levanon and M.K. Bowman, Tune-domain EPR Spectroscopy of Energy and Electron Transfer. D. Gust and T.A. Moore, Multi-step Electron and Energy Transfer in Artificial Photosynthesis. M.R. Wasielewski, Modelling Primary Electron Transfer in Photosynthesis using Supra-molecular Structures. J. Fajer and K.M. Barkigia, Models of Photosynthetic Chromophores, Molecular Structures of Chlorins, and Bacteriochlorins. J. Deisenhofer and H. Michel, The Three-Dimensional Structure of the Reaction Centre from Rhodopseudomonas viridis.

The Photosynthetic Reaction Center

The profanation of the singly reduced quinones Q::\ and QJj and the doubly reduced quinone Q~is discussed. Q::\ and QJj are not protonated directly in contrast to Q~which forms Q8 H2 • Experimental evidence is presented showing that Q8 H2 leaves the reaction center (RC). It is shown that this process is compatible with the three-dimensional structure of the RC. A model for the profanation involving a chain of protonatable residues connecting Q8 with the aqueous interface was tested by replacing Glu-2I2 of the L subunit with the non-protonatable residue Gin. The rate of profanation, deduced from a cytochrome turnover assay, was greatly reduced in the mutant, implicating Glu-2I2 as a proton donor. Repl<Icing Glu-2 I 2 with the protonatable residue Asp did not significantly affect the profanation rate. From the pH dependence of the electron transfer from Q::\ to Q8 the pK of Glu-2 I 2 was determined to be 9.5.

Current Research in Photosynthesis

The enzymes responsible for chlorophyll biosynthesis in plants, algae and cyanobacteria are identified and described, with emphasis on their protein composition and structure, required cofactors, physical and catalytic properties, protein-protein interactions and allosteric modulation of activity. Properties and features of the pathway that enable it to operate in a coordinated way while using unstable and light-sensitive intermediates in potentially hostile biochemical environments are discussed. The evolutionary relationships and possible origins of the chlorophyll biosynthetic enzymes are also discussed.

Enzymes of chlorophyll biosynthesis

Energy transfer and trapping in photosystem I.

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2893%2981442-3

Derivation of the formyl-group oxygen of chlorophyll b from molecular oxygen in greening leaves of a higher plant (Zea mays)

Bacteriochlorophylls modified at position C-3: long-range intramolecular interaction with position C-132

he methanolic extract of the cyanobacterium (blue-green alga) Spirulina geitleri has been treated with methanolic acid to convert all chlorophyllous pigments to their methylpheophorbides. Fractionation of the latter from methylpheophorbide a by thin layer chromatography and high pressure liquid chromatography yielded methylpheophorbide-RCI. Its structure has been determined as 132S-hydroxy-20-chloro-methylpheophorbide a by 1H-nuclear magnetic resonance, absorption and circular dichroism spectroscopy, mass spectrometry and by partial synthesis from chlorophyll a. The pigment is isolated from Spirulina geitleri irrespective of the use or omission of chlorinated substances during the isolation procedure.

https://epub.ub.uni-muenchen.de/2175/1/105.pdf

W. Schäfer

Papers

Derivation of the formyl-group oxygen of chlorophyll b from molecular oxygen in greening leaves of a higher plant (Zea mays)

Bacteriochlorophylls modified at position C-3: long-range intramolecular interaction with position C-132

Structure of methylpheophorbide-rci*

Bacteriochlorophylls modified at position C-3

Bacterial reaction centers with modified chromophores