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  • 1
    Electronic Resource
    Electronic Resource
    Crystallographic studies of mutant reaction centres from Rhodobacter sphaeroides (1998)
    Springer
    Photosynthesis research 55 (1998), S. 133-140 
    Details
    ISSN: 1573-5079
    Keywords: atomic structure ; membrane protein ; purple bacteria ; site-directed mutagenesis ; X-ray crystallography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract X-ray structures have been determined for five mutant reaction centres from Rhodobacter sphaeroides, at resolutions varying between 3.4 Å and 2.3 Å. The aim was to examine the effects of mutagenesis of polar residues in the binding pocket of the reaction centre carotenoid. The number of water molecules identified in each structure depended on the resolution and completeness of the data. In a 2.3 Å structure for a WM115F/FM197R mutant reaction centre, two water molecules partially filled the cavity that was created when the tryptophan residue was replaced by a less bulky phenylalanine. Structures obtained for four reaction centres with mutations of polar residues in the carotenoid binding pocket failed to show any significant change in the structure of the reaction centre carotenoid. Low resolution data for a YM210W mutant reaction centre showed that the overall structure of this complex is well conserved. This finding is discussed in light of the intriguing spectroscopic properties of the YM210W mutant reaction centre, and an alternative pathway for transmembrane electron transfer identified in this mutant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006095520441
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  • 2
    Electronic Resource
    Electronic Resource
    The purple bacterial photosynthetic unit (1996)
    Springer
    Photosynthesis research 48 (1996), S. 55-63 
    Details
    ISSN: 1573-5079
    Keywords: bacteriochlorophyll ; energy transfer ; light-harvesting complexes ; membrane proteins ; photosynthetic bacteria ; reaction centres
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Now is a very exciting time for researchers in the area of the primary reactions of purple bacterial photosynthesis. Detailed structural information is now available for not only the reaction center (Lancaster et al. 1995, in: Blankenship RE et al. (eds) Anoxygenic Photosynthetic Bacteria, pp 503–526), but also LH2 from Rhodopseudomonas acidophila (McDermott et al. 1995, Nature 374: 517–521) and LH1 from Rhodospirillum rubrum (Karrasch et al. 1995. EMBO J 14: 631–638). These structures can now be integrated to produce models of the complete photosynthetic unit (PSU) (Papiz et al., 1996, Trends Plant Sci, in press), which opens the door to a much more detailed understanding of the energy transfer events occurring within the PSU.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00040996
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Effects of mutagenesis on the detailed structure of spheroidenone in the Rhodobacter sphaeroides reaction centre examined by resonance Raman spectroscopy (1999)
    Springer
    Photosynthesis research 59 (1999), S. 223-230 
    Details
    ISSN: 1573-5079
    Keywords: mutagenesis ; pigment-protein ; spheroidenone ; structure ; Raman spectroscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The effect of mutagenesis on the detailed conformation of the carotenoid cofactor of the bacterial reaction centre has been examined using resonance Raman spectroscopy. Four single site mutations were made, removing polar residues that line the binding pocket for spheroidenone in the reaction centre from Rhodobacter sphaeroides. All of the mutations caused changes in the relative intensity of bands in the ν2 frequency region of the carotenoid resonance Raman spectrum, suggesting a change in the geometry of the central 15,15′-cis bond of the spheroidenone. In addition, increased splitting of the ν1 vibrational modes in two of the mutant RCs indicated a reduction of the effective conjugation length of the spheroidenone, possibly due to an increased distortion from a planar geometry along the C=C backbone of the spheroidenone. These changes in the detailed conformation of the reaction centre carotenoid do not affect the optical properties o f the cofactor, and are beyond the limits of detection of X-ray crystallography as currently applied to the bacterial reaction centre.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006168118363
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    Paper (German National Licenses)
    Fulltext
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