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Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions.

Yeates TO, Komiya H, Chirino A, Rees DC, Allen JP, Feher G
Proc Natl Acad Sci U S A 85 7993-7 (1988)
Cited: 82 times
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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-26 and the wild-type strain 2.4.1 have been determined by x-ray diffraction to resolutions of 2.8 A and 3.0 A with R values of 24% and 26%, respectively. The bacteriochlorophyll dimer (D), bacteriochlorophyll monomers (B), and bacteriopheophytin monomers (phi) form two branches, A and B, that are approximately related by a twofold symmetry axis. The cofactors are located in hydrophobic environments formed by the L and M subunits. Differences in the cofactor-protein interactions between the A and B cofactors, as well as between the corresponding cofactors of Rb, sphaeroides and Rhodopseudomonas viridis [Michel, H., Epp, O. & Deisenhofer, J. (1986) EMBO J. 3, 2445-2451], are delineated. The roles of several structural features in the preferential electron transfer along the A branch are discussed. Two bound detergent molecules of beta-octyl glucoside have been located near BA and BB. The environment of the carotenoid, C, that is present in RCs from Rb. sphaeroides 2.4.1 consists largely of aromatic residues of the M subunit. A role of BB in the triplet energy transfer from D to C and the reason for the preferential ease of removal of BB from the RC is proposed.

Reviews - 4rcr mentioned but not cited (1)

  1. Recent innovations in membrane-protein structural biology. Allen JP. F1000Res 8 (2019)

Articles - 4rcr mentioned but not cited (4)

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Reviews citing this publication (7)

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Articles citing this publication (70)

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Related citations provided by authors (9)

  1. Structure and Function of Bacterial Photosynthetic Reaction Centres. Feher G, Allen JP, Okamura MY, Rees DC Nature 339 111- (1989)
  2. The bacterial photosynthetic reaction center as a model for membrane proteins.. Rees DC, Komiya H, Yeates TO, Allen JP, Feher G Annu Rev Biochem 58 607-33 (1989)
  3. Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: symmetry relations and sequence comparisons between different species.. Komiya H, Yeates TO, Rees DC, Allen JP, Feher G Proc Natl Acad Sci U S A 85 9012-6 (1988)
  4. Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions.. Allen JP, Feher G, Yeates TO, Komiya H, Rees DC Proc Natl Acad Sci U S A 85 8487-91 (1988)
  5. Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits.. Allen JP, Feher G, Yeates TO, Komiya H, Rees DC Proc Natl Acad Sci U S A 84 6162-6 (1987)
  6. Structure of the reaction center from Rhodobacter sphaeroides R-26: the cofactors.. Allen JP, Feher G, Yeates TO, Komiya H, Rees DC Proc Natl Acad Sci U S A 84 5730-4 (1987)
  7. Structure of the reaction center from Rhodobacter sphaeroides R-26: membrane-protein interactions.. Yeates TO, Komiya H, Rees DC, Allen JP, Feher G Proc Natl Acad Sci U S A 84 6438-42 (1987)
  8. Structural homology of reaction centers from Rhodopseudomonas sphaeroides and Rhodopseudomonas viridis as determined by x-ray diffraction.. Allen JP, Feher G, Yeates TO, Rees DC, Deisenhofer J, Michel H, Huber R Proc Natl Acad Sci U S A 83 8589-93 (1986)
  9. Crystallization of reaction center from Rhodopseudomonas sphaeroides: preliminary characterization.. Allen JP, Feher G Proc Natl Acad Sci U S A 81 4795-9 (1984)

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