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D Tiede

Publications and source records attributed to D Tiede.

16 recordsLinked to original sources
PubMed1991

Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides.

The structure of the photosynthetic reaction center (RC) from Rhodobacter sphaeroides was determined at 3.1-A resolution by the molecular replacement method, using the Rhodopseudomonas viridis RC as the search structure. Atomic coordinates were refined with the difference Fourier method and restrained least-squares refinement techniques to a current R factor of 22%. The tertiary structure of the RC complex is stabilized by hydrophobic interactions between the L and M chains, by interactions of the pigments with each other and with the L and M chains, by residues from the L and M chains that coordinate to the Fe2+, by salt bridges that are formed between the L and M chains and the H chain, and possibly by electrostatic forces between the ends of helices. The conserved residues at the N-termini of the L and M chains were identified as recognition sites for the H chain.

Amino Acids↗
PubMed1991

Comparison of reaction centers from Rhodobacter sphaeroides and Rhodopseudomonas viridis: overall architecture and protein-pigment interactions.

Photosynthetic reaction centers (RCs) from the photosynthetic bacteria Rhodobacter sphaeroides and Rhodopseudomonas viridis are protein complexes closely related in both structure and function. The structure of the Rps. viridis RC was used to determine the structure of the RC from Rb. sphaeroides. Small but meaningful differences between the positions of the helices and the cofactors in the two complexes were identified. The distances between helices AL and AM, between BL and BM, and between bacteriopheophytins BPL and BPM are significantly shorter in Rps. viridis than they are in Rb. sphaeroides RCs. There are a number of differences in the amino acid residues that surround the cofactors; some of these residues form hydrogen bonds with the cofactors. Differences in chemical properties and location of these residues account in some manner for the different spectral properties of the two RCs. In several instances, the hydrogen bonds, as well as the apparent distances between the histidine ligands and the Mg atoms of the bacteriochlorophylls, were found to significantly differ from the Rb. sphaeroides RC structure previously described by Yeates et al. [(1988) Proc. Natl. Acad. Sci. U.S.A. 85, 7993-7997] and Allen et al. [(1988) Proc. Natl. Acad. Sci. U.S.A. 85, 8487-8491].

Amino Acids↗
PubMed1986

Structure of Rhodopseudomonas sphaeroides R-26 reaction center.

The molecular replacement method has been successfully used to provide a structure for the photosynthetic reaction center of Rhodopseudomonas sphaeroides at 3.7 A resolution. Atomic coordinates derived from the R. viridis reaction center were used in the search structure. The crystallographic R-factor is 0.39 for reflections between 8 and 3.7 A. Validity of the resulting model is further suggested by the visualization of amino acid side chains not included in the R. viridis search structure, and by the arrangements of the reaction centers in the unit cell. In the initial calculations quinones or pigments were not included; nevertheless, in the resulting electron density map, electron density for both quinones QA and QB appears along with the bacteriochlorophylls and bacteriopheophytins. Kinetic analysis of the charge recombination shows that the secondary quinone is fully functional in the R. sphaeroides crystal.

Bacterial Proteins↗
PubMed1985

Characterization of bacterial photosynthetic reaction center crystals from Rhodopseudomonas sphaeroides R-26 by X-ray diffraction.

An orthorhombic crystal form (P2(1)2(1)2(1)) of the reaction center from the photosynthetic bacterium Rhodopseudomonas sphaeroides R-26 has been characterized. The crystals were grown from polyethylene glycol; the unit cell dimensions are a = 142.2 A, b = 139.6 A, and c = 78.7 A; and they contain one reaction center in each crystallographic asymmetric unit. The crystals diffract to at least 3.0 A resolution, and are suitable for detailed structural studies.

Bacterial Proteins↗
PubMed1977

[Neurofibroma--neurofibromatosis--neurofibrosarcoma].

The author presents 14 patients with the gradations "neurofibroma--neurofibromatosis-neurofibrosarcoma". The great variability of forms of this disease ist emphasized. Apart from pure soft-tissue tumours, primary and secondary osseous changes were demonstrated in 4 patients. Intra-oral neurofibromas were seen in 5 cases. In 3 of these, the tongue was involved. Suggestions are given for the treatment of this clinical picture.

Adolescent↗