Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions.
The three-dimensional structure of the reaction center (RC) from Rhodobacter sphaeroides has been determined by x-ray diffraction to a resolution of 2.8 A with an R value of 24%. The interactions of the protein with the primary quinone, QA, secondary quinone, QB, and the nonheme iron are described and compared to those of RCs from Rhodopseudomonas viridis. Structural differences between the QA and QB environments that contribute to the function of the quinones (the electron transfer from QA- to QB and the charge recombination of QA-, QB- with the primary donor) are delineated. The protein residues that may be involved in the protonation of QB are identified. A pathway for the doubly reduced QB to dissociate from the RC is proposed. The interactions between QB and the residues that have been changed in herbicide-resistant mutants are described. The environment of the nonheme iron is compared to the environments of metal ions in other proteins.
Allen
J P
JP
University of California, San Diego, La Jolla 92093.
Feher
G
G
Yeates
T O
TO
Komiya
H
H
Rees
D C
DC
D001426:Bacterial Proteins / Q000378:metabolism*; D007501:Iron / Q000378:metabolism*; D046911:Macromolecular Substances; D008958:Models, Molecular; D045322:Photosynthetic Reaction Center Complex Proteins; D011487:Protein Conformation; D011809:Quinones / Q000378:metabolism*; D012242:Rhodobacter sphaeroides / Q000378:metabolism*; D014961:X-Ray Diffraction
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D045322:Photosynthetic Reaction Center Complex Proteins; D011809:Quinones; D007501:Iron