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1 edition of Structure of the reaction center from "Rhodobacter sphaeroides" R-26 found in the catalog.

Structure of the reaction center from "Rhodobacter sphaeroides" R-26

Structure of the reaction center from "Rhodobacter sphaeroides" R-26

the protein subunits

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Published by National Academy of Sciences of the United States of America in Washington, D.C .
Written in English


Edition Notes

Photocopy of: Proceedings of the National Academy of Sciences of the United States of America, vol. 84, September, (1987), pp.6162-6166.

Other titlesProceedings of the National Academy of Sciences of the United States of America.
StatementJ. P. Allen ... [et al.].
ContributionsAllen, J. P., National Academy of Sciences (U.S.)
ID Numbers
Open LibraryOL17122582M

Photosynthesis Research, ISSN , 6/, Volume , Issue 3, pp. - Structure and Function of the Photosynthetic Reaction Center of Rhodobacter sphaeroides, er and J.R. Norris. Refinement of the Structure of a Water-Soluble Antenna Complex from Green Photosynthetic Bacteria by Incorporation of the Chemically Determined Amino Acid Sequence, D.E. Tranrud and B.W. Matthews.

Photosynthetic reaction centers from purple bacteria exhibit an approximate twofold symmetry axis, which relates both the cofactors and the L and M subunits. For the reaction center from Rhodobacter sphaeroides, deviations from this twofold symmetry axis have been quantitated by superposing, by a degrees rotation, the cofactors of the B branch onto the A branch and . The electronic structure of the primary donor cation radical in Rhodobacter sphaeroides R ENDOR and TRIPLE resonance studies in single crystals of reaction centers. Biochimica et Biophysica Acta (BBA) - Bioenergetics , (1),

The Crystal Structure of the Photosynthetic Reaction Center from Rhodopseudomonas viridis --Structure of the Reaction Center from Rhodobacter sphaeroides R and --Symmetry Breaking Structures Involved in the Docking of Cytochrome c and Primary Electron Transfer in Reaction Centers of Rhodobacter sphaeroides --Crystallographic Studies of. Structure of the Reaction Center from Rhodobacter Sphaeroides R Protein-Cofactor (Quinones and Fe2+) Interactions Allen, J.P., Feher, G., Yeates, T.O., Komiya, H., Rees, D.C. () Proc Natl Acad Sci U S A ; Structure of the Reaction Center from Rhodobacter Sphaeroides R The Protein Subunits.


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Structure of the reaction center from "Rhodobacter sphaeroides" R-26 Download PDF EPUB FB2

Electron density map at 3 A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J Mol Biol. Dec 5; (2)– Allen JP, Feher G, Yeates TO, Komiya H, Rees DC. Structure of the reaction center from Rhodobacter sphaeroides R the by: The three-dimensional structure of the cofactors of the reaction center of Rhodobacter sphaeroides R has been determined by x-ray diffraction and refined at a resolution of A with an R value of 26%.

The main features of the structure are similar Cited by: The three-dimensional structure of the protein subunits of the reaction center (RC) of Rhodobacter sphaeroides has been determined by x-ray diffraction at a resolution of A with an R factor of 26%.

The L and M subunits each contain five transmembrane helices and several helices that do not span the by: Abstract. The three-dimensional structures of the cofactors and protein subunits of the reaction center (RC) from the carotenoidless mutant strain of Rhodobacter sphaeroides R and the wild-type strain have been determined by x-ray diffraction to resolutions of A and A with R values of 24% and 26%, by: Abstract.

Detailed theories of electron transfer in reaction centers (RCs) require knowledge of their three dimensional structure. We have determined the structure of RCs from Rb. sphaeroides by x-ray diffraction of single crystals. Diffraction data of RCs from both the carotenoidless mutant, R, and the wild type strain, were analyzed at resolutions of Cited by: The three-dimensional structure of the protein subunits of the reaction center (RC) of Rhodobacter sphaeroides has been determined by x-ray diffraction at a resolution of A with an R factor of 26%.

The L and M subunits each contain five transmembrane helices and several helices that do not span the membrane. The L and M subunits are related to each other by a 2. The three-dimensional structure of the cofactors of the reaction center of Rhodobacter sphaeroides R has been determined by x-ray diffraction and refined at a resolution of A with an R value of 26%.

The structure of the reaction center (RC) from Rhodobacter sphaeroides strain R has been refined to an R value of 21% at Å resolution. Progress in the determination of modified RCs is described. In particular, the structure of RCs with only 1 quinone and with bound herbicide are reported.

The Crystal Structure of the Photosynthetic Reaction Center from Rhodopseudomonas viridis.- Structure of the Reaction Center from Rhodobacter sphaeroides R and Symmetry Breaking Structures Involved in the Docking of Cytochrome c and Primary Electron Transfer in Reaction Centers of Rhodobacter sphaeroides Frank H.A., Aldema M.L.

() Correlation Between the Polarized Light Absorption and the X-Ray Structure of Single Crystals of the Reaction Center from Rhodobacter Sphaeroides R In: Breton J., Verméglio A. (eds) The Photosynthetic Bacterial Reaction Center II. Nato ASI Series (Series A: Life Sciences), vol Springer, Boston, MA.

The three-dimensional structure of the protein subunits of the reaction center (RC) of Rhodobacter sphaeroides has been determined by x-ray diffraction at a resolution of A with an R factor of 26%. EPR and ENDOR Studies of the Oxidized Donor in Reaction Centers of Rhodobacter sphaeroides Strain R and two Heterodimer Mutants in which Histidine M or L was Replaced by Leucine M.

Huber, E. Lous, R. Isaacson, G. Feher, D. Gaul, C. Schenck. Anisotropic Magnetic Field Effects of the Photosynthetic Bacterial Reaction Center of Rhodobacter sphaeroides R, Studied by Linear Dichroic Magneto-optical Difference Spectroscopy (LD-MODS) in the Temperature Range – K.

ical measurementsare confirmed bythe x-ray structure. The reaction center (RC) is an integral membrane protein-pigment complex that mediates the primary processes of photosynthesis-i.e., the light-induced electron transfers from a donor to a series ofacceptor species.

Thethree-di-mensional structure of the RC from the photosynthetic. Structure of the reaction center from Rhodobacter sphaeroides R the cofactors.

Proc Natl Acad Sci U S A. Aug; 84 (16)– [PMC free article] [Google Scholar] Allen JP, Feher G, Yeates TO, Komiya H, Rees DC. Structure of the reaction center from Rhodobacter sphaeroides R the protein subunits.

Structure of the reaction center from Rhodobacter sphaeroides R the protein subunits. Proc Natl Acad Sci U S A. Sep; 84 (17)– [PMC free article] Yeates TO, Komiya H, Rees DC, Allen JP, Feher G.

Structure of the reaction center from Rhodobacter sphaeroides R membrane-protein interactions. The photoinduced charge separation in Q B-depleted reaction centers (RCs) from Rhodobacter sphaeroides R in solid air-dried and vacuum-dried (~10 −2 Torr) films, obtained in the presence of detergent n-dodecyl-β-D-maltoside (DM), is characterized using ultrafast transient absorption is shown that drying of RC-DM complexes is accompanied by.

The three-dimensional structures of the cofactors and protein subunits of the reaction center (RC) from the carotenoidless mutant strain of Rhodobacter sphaeroides R and the wild-type strain have been determined by x-ray diffraction to resolutions of A and A with R values of 24% and 26%, respectively.

The bacteriochlorophyll dimer (D), bacteriochlorophyll. In this work we investigated the hydrogen bonds to the two carbonyl oxygens of the semiquinone Q A ⋅ − in the well-characterized reaction center from the photosynthetic bacterium Rhodobacter sphaeroides R We used electron paramagnetic resonance and electron nuclear double resonance techniques at 35 GHz at a temperature of 80 K.

The three-dimensional structures of the cofactors and protein subunits of the reaction center (RC) from the carotenoidless mutant strain of Rhodobacter sphaeroides R and the wild-type strain have been determined by x-ray diffraction to resolutions of A and A with R values of 24% and 26%, respectively.

The three-dimensional structure of the protein subunits of the reaction center (RC) of Rhodobacter sphaeroides has been determined by x-ray diffraction at a resolution of angstrom with an R factor of 26%. The L and M subunits each contain five transmembrane helices and several helices that do not span the membrane.

The L and M subunits are related to each .In this work, the photosynthetic Reaction Center (RC) of the bacterium Rhodobacter sphaeroides has been used as a model for the study of the ultrasound-induced IMP denaturation. Purified RCs were suspended in i) detergent micelles, in ii) detergent-free buffer and iii) reconstituted in liposomes, and then treated with ultrasound at 30 W and Book • Edited by: 1 - Structure and Function of the Photosynthetic Reaction Center of Rhodobacter sphaeroides.

Marianne Schiffer and James R. Norris. Pages The availability of the photosynthetic reaction center's structure at an atomic resolution of less than three angstroms has revolutionized research. This protein is the.