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  • 1
    Electronic Resource
    Electronic Resource
    Electron Transfer in Proteins (1996)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 65 (1996), S. 537-561 
    Details
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.bi.65.070196.002541
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The red form of [Re(phen)(CO)3(H2O)]CF3SO3.H2O (1999)
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 55 (1999), S. 913-916 
    Details
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108270199001432
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  • 3
    Electronic Resource
    Electronic Resource
    The use of pseudocontact shifts to refine solution structures of paramagnetic metalloproteins: Met80Ala cyano-cytochrome c as an example (1996)
    Springer
    JBIC 1 (1996), S. 117-126 
    Details
    ISSN: 1432-1327
    Keywords: Key words Solution structure ; Paramagnetic biomolecules ; NMR ; Cytochrome c
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  The availability of NOE constraints and of the relative solution structure of a paramagnetic protein permits the use of pseudocontact shifts as further structural constraints. We have developed a strategy based on: (1) determination of the χ tensor anisotropy parameters from the starting structure; (2) recalculation of a new structure by using NOE and pseudocontact shift constraints simultaneously; (3) redetermination of the χ tensor anisotropy parameters from the new structure, and so on until self-consistency. The system investigated is the cyanide derivative of a variant of the oxidized Saccharomyces cerevisiae iso-1-cytochrome c containing the Met80Ala mutation. The structure has been substantially refined. It is shown that the analysis of the deviation of the experimental pseudocontact shifts from those calculated using the starting structure may be unsound, as may the simple structure refinement based on the pseudocontact shift constraints only.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050030
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  • 4
    Electronic Resource
    Electronic Resource
    Electron tunneling in proteins: role of the intervening medium (1997)
    Springer
    JBIC 2 (1997), S. 399-404 
    Details
    ISSN: 1432-1327
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  Analysis of electron-transfer (ET) kinetics data obtained from experiments on Ru-modified proteins (cytochrome c, azurin, myoglobin) reveals that distant donor-acceptor electronic couplings depend upon the secondary structure of the intervening polypeptide matrix. Rates of Fe2+→Ru3+ ET reactions in cytochrome c decay exponentially with tunneling-pathway length (decay constant 0.73 Å–1); these rates also decay exponentially with Ru-Fe distance (decay constant 1.1 Å–1). In azurin, a β-sheet protein, Cu+→Ru3+ rates exhibit an exponential Cu-Ru distance dependence with a decay constant of 1.1 Å–1. Comparison of distant couplings in azurin and myoglobin suggests that hydrogen bonds are better mediators across β sheets than through α helices.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050150
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  • 5
    Electronic Resource
    Electronic Resource
    Electron tunneling in proteins: role of the intervening medium (1996)
    Springer
    JBIC 1 (1996), S. 221-225 
    Details
    ISSN: 1432-1327
    Keywords: Key words Electron transfer ; Tunneling pathways ; Azurin ; Cytochrome c ; Myoglobin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract  Analysis of electron-transfer (ET) kinetics data obtained from experiments on Ru-modified proteins (azurin, cytochrome c, myoglobin) and the bacterial photosynthetic reaction center reveals that distant donor-acceptor electronic couplings depend upon the secondary structure of the intervening polypeptide matrix. The β-sheet azurin structure efficiently and isotropically mediates coupling with an exponential distance-decay constant of 1.1 Å–1. The experimentally derived distance-decay constant of 1.4 Å–1 for long-range ET in myoglobin and the reaction center suggests that hydrogen-bond couplings are weaker through α helices than across β sheets. The donor-acceptor interactions of systems with comparable tunneling energies fall into two coupling zones: the β zone (bounded by distance-decay constants of 0.9 and 1.15 Å–1) includes all the β-sheet (azurin) couplings and all but one coupling in cytochrome c; the α zone (boundaries: 1.25 and 1.6 Å–1) includes less strongly coupled donor-acceptor pairs in myoglobin and the reaction center as well as a relatively weakly coupled pair in cytochrome c.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007750050046
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