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  • Electronic Resource  (3)
  • 1995-1999  (3)
  • 1975-1979
  • Solution structure  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Solution structure of reduced horse heart cytochrome c (1999)
    Springer
    JBIC 4 (1999), S. 21-31 
    Details
    ISSN: 1432-1327
    Keywords: Key words Reduced cytochrome c ; Solution structure ; NMR ; Heme proteins ; Electron transfer proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  In the frame of a broad study on the structural differences between the two redox forms of cytochromes to be related to the electron transfer process, the NMR solution structure of horse heart cytochrome c in the reduced form has been determined. The structural data obtained in the present work are compared to those already available in the literature on the same protein and the presence of conformational differences is discussed in the light of the experimental method employed for the structure determination. Redox-state dependent changes are analyzed and in particular they are related to the role of propionate-7 of the heme. Also some hydrogen bonds are changed upon reduction of the heme iron. A substantial similarity is observed for the backbone fold, independently of the oxidation state. At variance, some meaningful differences are observed in the orientation of a few side chains. These changes are related to those found in the case of the highly homologous cytochrome c from Saccharomyces cerevisiae. The exchangeability of the NH protons has been investigated and found to be smaller than in the case of the oxidized protein. We think that this is a characteristic of reduced cytochromes and that mobility is a medium for molecular recognition in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050285
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The solution structure of a monomeric, reduced form of human copper,zinc superoxide dismutase bearing the same charge as the native protein (1999)
    Springer
    JBIC 4 (1999), S. 795-803 
    Details
    ISSN: 1432-1327
    Keywords: NMR ; Superoxide dismutase ; Solution structure ; Monomeric mutants ; Structure-function relationship
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: 2 , has RMSD values with respect to the average structure of 0.94 ± 0.14 Å2 and 1.50 ± 0.14 Å2 for the backbone and the heavy atoms, respectively. The overall folding, which includes the classical eight-stranded Greek-key β-barrel and a short α-helix, is very close to that of the previously characterized monomeric mutant E133QM2SOD and to that of wild-type SOD. The region involved in the subunit-subunit interactions in the dimeric protein is confirmed to be disordered in the monomeric species. It is also observed that a sizable rearrangement of the charged groups of the electrostatic loop and of Arg143 takes place in the monomeric species. The width of the active site channel, both at its entrance and at the bottleneck of the active site, is discussed in the light of the influence on the enzymatic activity and the latter with respect to the overall charge. It is also confirmed that the NH proton of His63 shields the Cu(I) from the bulk solvent, thus supporting the suggestion that superoxide may interact with the reduced metal ion in an outer-sphere fashion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050353
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Solution structure of reduced Clostridium pasteurianum rubredoxin (1998)
    Springer
    JBIC 3 (1998), S. 401-410 
    Details
    ISSN: 1432-1327
    Keywords: Key words Rubredoxin ; Solution structure ; Paramagnetism ; Nuclear relaxation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The solution structure of reduced Clostridium pasteurianum rubredoxin (MW 6100) is reported here. The protein is highly paramagnetic, with iron(II) being in the S=2 spin state. The Hβ protons of the ligating cysteines are barely observed, and not specifically assigned. Seventy-six percent of the protons have been assigned and 1267 NOESY peaks (of which 1037 are meaningful) have been observed. Nonselective T 1 measurements have been measured by recording four nonselective 180°-τ-NOESY at different τ values, and fitting the intensity recoveries to an exponential recovery. Thirty-six metal-proton upper and lower distance constraints have been obtained from the above measurements. The use of such constraints is assessed with respect to spin delocalization on the sulfur donor atoms. The solution structure obtained with the program DYANA has been refined through restrained energy minimization. A final family of 20 conformers is obtained with no distance violations larger than 0.24 Å, and RMSD values to the mean structure of 0.58 and 1.03 Å for backbone and all heavy atoms, respectively (measured on residues 3–53). The structure is compared to the X-ray structure of the oxidized and of the zinc substituted protein, and to the available structures of other rubredoxins. In particular, the comparison with the crystal structure and the solution structure of the Zn derivative of the highly thermostable Pyrococcus furiosus rubredoxin suggested that the relatively low thermal stability of the clostridial rubredoxin may be tentatively ascribed to the loosening of its secondary structure elements. This research is a further achievement at the frontier of solution structure determinations of paramagnetic proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1432-1033.1967.tb19543.x
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    Paper (German National Licenses)
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