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


Book details:

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

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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. J. Lous, R. A. Isaacson, G. Feher, D. Gaul, C. 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.